erbb2  (Cell Signaling Technology Inc)


Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc erbb2
    ErbB3 interacts with <t>erbB2</t> to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.
    Erbb2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erbb2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erbb2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Targeting of erbB3 receptor to overcome resistance in cancer treatment"

    Article Title: Targeting of erbB3 receptor to overcome resistance in cancer treatment

    Journal: Molecular Cancer

    doi: 10.1186/1476-4598-13-105

    ErbB3 interacts with erbB2 to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.
    Figure Legend Snippet: ErbB3 interacts with erbB2 to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.

    Techniques Used: Activation Assay

    Current and novel therapeutic strategies targeting of erbB2 and/or erbB3 receptors for cancer therapy. Several erbB2-targeted therapies (trastuzumab, pertuzumab, T-DM1, and lapatinib) have being used in clinic, whereas no erbB3-targeted therapy has been approved for cancer treatment. Blocking Abs, such as MM-121, MM-111, AMG 888/U3-1287, and MP-RM-1/EV20, are the only agents being tested in early clinical and/or preclinical investigations. Our recent data show that entinostat, a class I HDAC inhibitor selectively downregulates erbB2/erbB3 via induction of specific miRNAs, miR-125a, miR-125b, and miR-205 in erbB2+ breast cancer cells. Further characterization demonstrates that these “sister” miRNAs (share common targets) act in concert to inhibit erbB2/erbB3 protein translation. Thus, the novel strategy, like cooperative miRNA targeting of erbB2/erbB3 may represent a new approach for cancer therapy.
    Figure Legend Snippet: Current and novel therapeutic strategies targeting of erbB2 and/or erbB3 receptors for cancer therapy. Several erbB2-targeted therapies (trastuzumab, pertuzumab, T-DM1, and lapatinib) have being used in clinic, whereas no erbB3-targeted therapy has been approved for cancer treatment. Blocking Abs, such as MM-121, MM-111, AMG 888/U3-1287, and MP-RM-1/EV20, are the only agents being tested in early clinical and/or preclinical investigations. Our recent data show that entinostat, a class I HDAC inhibitor selectively downregulates erbB2/erbB3 via induction of specific miRNAs, miR-125a, miR-125b, and miR-205 in erbB2+ breast cancer cells. Further characterization demonstrates that these “sister” miRNAs (share common targets) act in concert to inhibit erbB2/erbB3 protein translation. Thus, the novel strategy, like cooperative miRNA targeting of erbB2/erbB3 may represent a new approach for cancer therapy.

    Techniques Used: Blocking Assay

    erbb2  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc erbb2
    ErbB3 interacts with <t>erbB2</t> to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.
    Erbb2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erbb2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erbb2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Targeting of erbB3 receptor to overcome resistance in cancer treatment"

    Article Title: Targeting of erbB3 receptor to overcome resistance in cancer treatment

    Journal: Molecular Cancer

    doi: 10.1186/1476-4598-13-105

    ErbB3 interacts with erbB2 to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.
    Figure Legend Snippet: ErbB3 interacts with erbB2 to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.

    Techniques Used: Activation Assay

    Current and novel therapeutic strategies targeting of erbB2 and/or erbB3 receptors for cancer therapy. Several erbB2-targeted therapies (trastuzumab, pertuzumab, T-DM1, and lapatinib) have being used in clinic, whereas no erbB3-targeted therapy has been approved for cancer treatment. Blocking Abs, such as MM-121, MM-111, AMG 888/U3-1287, and MP-RM-1/EV20, are the only agents being tested in early clinical and/or preclinical investigations. Our recent data show that entinostat, a class I HDAC inhibitor selectively downregulates erbB2/erbB3 via induction of specific miRNAs, miR-125a, miR-125b, and miR-205 in erbB2+ breast cancer cells. Further characterization demonstrates that these “sister” miRNAs (share common targets) act in concert to inhibit erbB2/erbB3 protein translation. Thus, the novel strategy, like cooperative miRNA targeting of erbB2/erbB3 may represent a new approach for cancer therapy.
    Figure Legend Snippet: Current and novel therapeutic strategies targeting of erbB2 and/or erbB3 receptors for cancer therapy. Several erbB2-targeted therapies (trastuzumab, pertuzumab, T-DM1, and lapatinib) have being used in clinic, whereas no erbB3-targeted therapy has been approved for cancer treatment. Blocking Abs, such as MM-121, MM-111, AMG 888/U3-1287, and MP-RM-1/EV20, are the only agents being tested in early clinical and/or preclinical investigations. Our recent data show that entinostat, a class I HDAC inhibitor selectively downregulates erbB2/erbB3 via induction of specific miRNAs, miR-125a, miR-125b, and miR-205 in erbB2+ breast cancer cells. Further characterization demonstrates that these “sister” miRNAs (share common targets) act in concert to inhibit erbB2/erbB3 protein translation. Thus, the novel strategy, like cooperative miRNA targeting of erbB2/erbB3 may represent a new approach for cancer therapy.

    Techniques Used: Blocking Assay

    phosphorylated erbb2 tyr1248  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc phosphorylated erbb2 tyr1248
    (A) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Cell lysates were separated into cytosolic (supernatant) and total membrane (pellet) fractions. The pellet fraction was subjected to immunoprecipitation with anti-Myc (nucleolin) or anti-HA (control) antibodies and immunoblotted with specific ErbBs antibodies. Total pellet and supernatant extracts are shown in the right lanes of each panel. (B) COS7 cells were transiently co-transfected with expression vector of ErbB1 and Myc-Nucleolin. Nuclear and non-nuclear cell extracts were immunoblotted with anti-ErbB1 antibodies. As control for the fractionation purity Blots were reacted with anti-PARP antibodies (as a nuclear marker) and anti-tubulin antibodies (as a cytosolic marker). (C) Cell lysates prepared from SKBR3 cells were subjected to immunoprecipitation with either anti-nucleolin or anti <t>ErbB2</t> antibodies and immunoblotted with either anti- ErbB2 or anti-nucleolin antibodies as indicated, as a control total cell lysates are shown in the right lane of each panel.
    Phosphorylated Erbb2 Tyr1248, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphorylated erbb2 tyr1248/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphorylated erbb2 tyr1248 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Identification of Nucleolin as New ErbB Receptors- Interacting Protein"

    Article Title: Identification of Nucleolin as New ErbB Receptors- Interacting Protein

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0002310

    (A) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Cell lysates were separated into cytosolic (supernatant) and total membrane (pellet) fractions. The pellet fraction was subjected to immunoprecipitation with anti-Myc (nucleolin) or anti-HA (control) antibodies and immunoblotted with specific ErbBs antibodies. Total pellet and supernatant extracts are shown in the right lanes of each panel. (B) COS7 cells were transiently co-transfected with expression vector of ErbB1 and Myc-Nucleolin. Nuclear and non-nuclear cell extracts were immunoblotted with anti-ErbB1 antibodies. As control for the fractionation purity Blots were reacted with anti-PARP antibodies (as a nuclear marker) and anti-tubulin antibodies (as a cytosolic marker). (C) Cell lysates prepared from SKBR3 cells were subjected to immunoprecipitation with either anti-nucleolin or anti ErbB2 antibodies and immunoblotted with either anti- ErbB2 or anti-nucleolin antibodies as indicated, as a control total cell lysates are shown in the right lane of each panel.
    Figure Legend Snippet: (A) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Cell lysates were separated into cytosolic (supernatant) and total membrane (pellet) fractions. The pellet fraction was subjected to immunoprecipitation with anti-Myc (nucleolin) or anti-HA (control) antibodies and immunoblotted with specific ErbBs antibodies. Total pellet and supernatant extracts are shown in the right lanes of each panel. (B) COS7 cells were transiently co-transfected with expression vector of ErbB1 and Myc-Nucleolin. Nuclear and non-nuclear cell extracts were immunoblotted with anti-ErbB1 antibodies. As control for the fractionation purity Blots were reacted with anti-PARP antibodies (as a nuclear marker) and anti-tubulin antibodies (as a cytosolic marker). (C) Cell lysates prepared from SKBR3 cells were subjected to immunoprecipitation with either anti-nucleolin or anti ErbB2 antibodies and immunoblotted with either anti- ErbB2 or anti-nucleolin antibodies as indicated, as a control total cell lysates are shown in the right lane of each panel.

    Techniques Used: Transfection, Expressing, Plasmid Preparation, Immunoprecipitation, Fractionation, Marker

    (A) COS7 cells were transiently co-transfected with expression vector of either ErbB1 or ErbB2 receptors alone or with Myc-Nucleolin. Following 30 min serum deprivation, cells were either untreated or treated with EGF 100 ng/ml for 5 min. Cell lysates were immunoblotted with anti-phosphorylated EGFR or anti-phosphorylated ErbB2 antibodies respectively. As control, lysates were immunoblotted with anti-EGFR or anti-ErbB2 antibodies. Note that at time 0 phosphorylated receptors are detected in cells expressing nucleolin and EGFR or ErbB2. (B) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Following 30 min serum deprivation cells were untreated or treated with either EGF 100 ng/ml or NRG 100 ng/ml for 5 min as indicated. Cell lysates were subjected to immunoprecipitation with anti-phosphotyrosine antibodies (PY20) and immunoblotted with specific ErbB antibodies. Note that in untreated cells, phosphorylated receptor is detected in cells expressing nucleolin and ErbB receptor. The values represent fold induction compared to the receptor levels in untreated cells (1).
    Figure Legend Snippet: (A) COS7 cells were transiently co-transfected with expression vector of either ErbB1 or ErbB2 receptors alone or with Myc-Nucleolin. Following 30 min serum deprivation, cells were either untreated or treated with EGF 100 ng/ml for 5 min. Cell lysates were immunoblotted with anti-phosphorylated EGFR or anti-phosphorylated ErbB2 antibodies respectively. As control, lysates were immunoblotted with anti-EGFR or anti-ErbB2 antibodies. Note that at time 0 phosphorylated receptors are detected in cells expressing nucleolin and EGFR or ErbB2. (B) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Following 30 min serum deprivation cells were untreated or treated with either EGF 100 ng/ml or NRG 100 ng/ml for 5 min as indicated. Cell lysates were subjected to immunoprecipitation with anti-phosphotyrosine antibodies (PY20) and immunoblotted with specific ErbB antibodies. Note that in untreated cells, phosphorylated receptor is detected in cells expressing nucleolin and ErbB receptor. The values represent fold induction compared to the receptor levels in untreated cells (1).

    Techniques Used: Transfection, Expressing, Plasmid Preparation, Immunoprecipitation

    her2  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc her2
    Relationships of AK4 and clinicopathological characteristics in 98 patients with <t> HER2 </t> overexpression breast cancer.
    Her2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/her2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    her2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "AK4 Promotes the Progression of HER2-Positive Breast Cancer by Facilitating Cell Proliferation and Invasion"

    Article Title: AK4 Promotes the Progression of HER2-Positive Breast Cancer by Facilitating Cell Proliferation and Invasion

    Journal: Disease Markers

    doi: 10.1155/2019/8186091

    Relationships of AK4 and clinicopathological characteristics in 98 patients with  HER2  overexpression breast cancer.
    Figure Legend Snippet: Relationships of AK4 and clinicopathological characteristics in 98 patients with HER2 overexpression breast cancer.

    Techniques Used: Over Expression, Expressing

    AK4 was highly expressed in human HER2-positive breast cancer tissues. (a) IHC assays were performed, and the representative photographs of AK4 expression levels in HER2-positive breast cancer tissues were detected and shown (×100 and ×200 magnification, respectively). (b) IHC staining showed AK4 expression levels in adjacent nontumor tissues (×100 and ×200 magnification, respectively).
    Figure Legend Snippet: AK4 was highly expressed in human HER2-positive breast cancer tissues. (a) IHC assays were performed, and the representative photographs of AK4 expression levels in HER2-positive breast cancer tissues were detected and shown (×100 and ×200 magnification, respectively). (b) IHC staining showed AK4 expression levels in adjacent nontumor tissues (×100 and ×200 magnification, respectively).

    Techniques Used: Expressing, Immunohistochemistry

    AK4 facilitates cell proliferation and invasion of HER2-positive breast cancer in vitro. (a) Colony formation assays were then performed using MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and colony number was counted. (b) The results of MTT assays showed the inhibition of cell proliferation caused by AK4 knockdown. (c) AK4 depletion resulted in the lower migration degree in MCF7 and MDA-MB-231 cells. Photographs showing that at the 0 and 24th-hour time point migrated cells were present. (d) Transwell assays using both MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and the degree of invasion was quantified by the invasion cell number. Results are presented as mean ± SD, ∗ P < 0.05.
    Figure Legend Snippet: AK4 facilitates cell proliferation and invasion of HER2-positive breast cancer in vitro. (a) Colony formation assays were then performed using MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and colony number was counted. (b) The results of MTT assays showed the inhibition of cell proliferation caused by AK4 knockdown. (c) AK4 depletion resulted in the lower migration degree in MCF7 and MDA-MB-231 cells. Photographs showing that at the 0 and 24th-hour time point migrated cells were present. (d) Transwell assays using both MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and the degree of invasion was quantified by the invasion cell number. Results are presented as mean ± SD, ∗ P < 0.05.

    Techniques Used: In Vitro, Transfection, shRNA, Inhibition, Migration

    AK4 induces tumor growth and metastasis of HER2-positive breast cancer in mice. (a) MCF7 cells infected with control or AK4 shRNA lentivirus were subcutaneously implanted into nude mice. After 2 weeks, tumors were isolated, and the volume of tumor was measured every 7 days ( n = 5 in each group). Tumor growth curves were calculated and evaluated based on the average volume of 5 tumors in AK4 knockdown and control groups. (b) MCF7 cells infected with control or AK4 shRNA lentivirus were implanted into the caudal vein of nude mice. After 8 weeks, tumors were isolated from mice in each group and weighted ( n = 5 for each group). (c) IHC assays showed the expression levels of AK4 in control or AK4 ablation tumors isolated from mice. Results are presented as mean ± SD, ∗ P < 0.05.
    Figure Legend Snippet: AK4 induces tumor growth and metastasis of HER2-positive breast cancer in mice. (a) MCF7 cells infected with control or AK4 shRNA lentivirus were subcutaneously implanted into nude mice. After 2 weeks, tumors were isolated, and the volume of tumor was measured every 7 days ( n = 5 in each group). Tumor growth curves were calculated and evaluated based on the average volume of 5 tumors in AK4 knockdown and control groups. (b) MCF7 cells infected with control or AK4 shRNA lentivirus were implanted into the caudal vein of nude mice. After 8 weeks, tumors were isolated from mice in each group and weighted ( n = 5 for each group). (c) IHC assays showed the expression levels of AK4 in control or AK4 ablation tumors isolated from mice. Results are presented as mean ± SD, ∗ P < 0.05.

    Techniques Used: Infection, shRNA, Isolation, Expressing

    her2 phosphorylation sites  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc her2 phosphorylation sites
    (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting <t>HER2</t> (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.
    Her2 Phosphorylation Sites, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/her2 phosphorylation sites/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    her2 phosphorylation sites - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators"

    Article Title: Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0051817

    (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting HER2 (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.
    Figure Legend Snippet: (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting HER2 (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.

    Techniques Used: Produced, Recombinant, Expressing, Isolation, Derivative Assay, Construct, Staining, Fluorescence, Activity Assay

    Cell-surface binding and solution state properties of  HER2  agonists and antagonists.
    Figure Legend Snippet: Cell-surface binding and solution state properties of HER2 agonists and antagonists.

    Techniques Used: Binding Assay

    (a) Four different thio-Fabs derived from trastuzumab were used to make ten bis-Fab analogs. Each thio-Fab mutant (LC-110, LC-205, HC-118, and HC-228) was reacted with the bis-maleimido crosslinker and recombined in a matrix format described in the Experimental Methods. Fabs were derived from several sources shown in and S 2B . Each chain of the Fab is represented by a different color (dark blue - heavy chain and light blue - light chain) and the position of the cysteine used in coupling is denoted by the red dot. (b) The matrix-generated bis-Fab linkage analogs are shown diagrammatically in this Figure. Color coded numbers indicate the type of activity observed, where tan signifies antagonist, dark blue signifies agonist, and light blue signifies no activity. (c) BT474 cells were incubated with the indicated concentrations of bis-Fabs shown in (b). The degree of cell proliferation was assessed after 5 days using AlamarBlue staining. The results are reported as a percentage of maximum proliferation relative to untreated controls. The measured values for each test sample, as well as individual replicates, are shown as raw data in . Color codes are the same as in (b). (d) A model of the complex formation between two HER2 extracelluar domains (ECD) and either an agonist (1321) or antagonist (1324) bis-Fab. Here is shown two light chain connected bis-Fabs with the heavy chain colored dark blue, the light chains colored lighter blue and the HER2 ECD colored magenta. In the left panel the two complexes are shown looking up at the membrane. The point of contact between the Fv-region of the Fab and the ECD is near the membrane. The HER2 protein terminates in this structure just prior to the point at which the transmembrane domain begins. The complex models are rotated 90 degrees on both the horizontal and vertical axis to produce this viewpoint. The plane of the membrane runs perpendicular to the page. The PBD ID Code used for model building was 1N8Z.
    Figure Legend Snippet: (a) Four different thio-Fabs derived from trastuzumab were used to make ten bis-Fab analogs. Each thio-Fab mutant (LC-110, LC-205, HC-118, and HC-228) was reacted with the bis-maleimido crosslinker and recombined in a matrix format described in the Experimental Methods. Fabs were derived from several sources shown in and S 2B . Each chain of the Fab is represented by a different color (dark blue - heavy chain and light blue - light chain) and the position of the cysteine used in coupling is denoted by the red dot. (b) The matrix-generated bis-Fab linkage analogs are shown diagrammatically in this Figure. Color coded numbers indicate the type of activity observed, where tan signifies antagonist, dark blue signifies agonist, and light blue signifies no activity. (c) BT474 cells were incubated with the indicated concentrations of bis-Fabs shown in (b). The degree of cell proliferation was assessed after 5 days using AlamarBlue staining. The results are reported as a percentage of maximum proliferation relative to untreated controls. The measured values for each test sample, as well as individual replicates, are shown as raw data in . Color codes are the same as in (b). (d) A model of the complex formation between two HER2 extracelluar domains (ECD) and either an agonist (1321) or antagonist (1324) bis-Fab. Here is shown two light chain connected bis-Fabs with the heavy chain colored dark blue, the light chains colored lighter blue and the HER2 ECD colored magenta. In the left panel the two complexes are shown looking up at the membrane. The point of contact between the Fv-region of the Fab and the ECD is near the membrane. The HER2 protein terminates in this structure just prior to the point at which the transmembrane domain begins. The complex models are rotated 90 degrees on both the horizontal and vertical axis to produce this viewpoint. The plane of the membrane runs perpendicular to the page. The PBD ID Code used for model building was 1N8Z.

    Techniques Used: Derivative Assay, Mutagenesis, Generated, Activity Assay, Incubation, Staining

    (a) A time course of cell growth activity in BT474 cells in the presence of 100 nM trastuzumab, 100 nM bis-Fab 1325, or 10 nM heregulin. BT474 were cultured in media containing 10% fetal bovine serum for up to 84 hours. At 12-hour intervals total number of cells were determined; three plates from each treatment group were counted for the total number of cells and plotted as the mean cell count. The error bars indicate standard deviation from the mean. At approximately 60 hours (indicated by the arrow) the cells reached confluence in the agonist treatment groups. (b) BT474 cells were treated with 100 nM of trastuzumab, 100 nM of bis-Fab 1325, or 100 nM of bis-Fab 1329 for 10, 30 and 120 minutes. At times indicated, cell lysates were prepared and analyzed by immunoblotting using phospho-specific antibodies for HER3, AKT, and MAPK as well as antibodies recognizing total protein. Data are representative of three independent experiments. (c) Quantification of AKT phosphorylation after treatment with 100 nM bis-Fab 1325, 100 nM trastuzumab, 2 nM heregulin and a non-specific control antibody (anti-gD) by PathScan p-AKT1 (S473) ELISA. All data points were collected in triplicates and the mean of the triplicate absorbance values were used to calculate the percent change in pAKT compared to untreated control group. The error bars indicate standard deviation from the mean. Data are representative of three independent experiments. (d) A model for the HER2 dimerization patterns induced by either the agonist antibody-analogs or trastuzumab. The diagram depicts three potential dimer conformations; 1) the basal state induced by high cell surface density, 2) the activated state induced by the bis-Fab agonist, and 3) the inhibited state stabilized by trastuzumab. The cell growth activity of agonist bis-Fabs may be due to stabilization of an allosterically activated conformation between HER2–HER2 dimers. Trastuzumab's antagonistic activity may arise from dimer orientations that favor the inactive allosteric interactions between kinases. A non-stabilized dimer may represent the basal state where interactions between the juxtamembrane (black line) loop of the activator kinase and the C-terminal lobe of the receiver kinase are not fully stabilized without agonist binding.
    Figure Legend Snippet: (a) A time course of cell growth activity in BT474 cells in the presence of 100 nM trastuzumab, 100 nM bis-Fab 1325, or 10 nM heregulin. BT474 were cultured in media containing 10% fetal bovine serum for up to 84 hours. At 12-hour intervals total number of cells were determined; three plates from each treatment group were counted for the total number of cells and plotted as the mean cell count. The error bars indicate standard deviation from the mean. At approximately 60 hours (indicated by the arrow) the cells reached confluence in the agonist treatment groups. (b) BT474 cells were treated with 100 nM of trastuzumab, 100 nM of bis-Fab 1325, or 100 nM of bis-Fab 1329 for 10, 30 and 120 minutes. At times indicated, cell lysates were prepared and analyzed by immunoblotting using phospho-specific antibodies for HER3, AKT, and MAPK as well as antibodies recognizing total protein. Data are representative of three independent experiments. (c) Quantification of AKT phosphorylation after treatment with 100 nM bis-Fab 1325, 100 nM trastuzumab, 2 nM heregulin and a non-specific control antibody (anti-gD) by PathScan p-AKT1 (S473) ELISA. All data points were collected in triplicates and the mean of the triplicate absorbance values were used to calculate the percent change in pAKT compared to untreated control group. The error bars indicate standard deviation from the mean. Data are representative of three independent experiments. (d) A model for the HER2 dimerization patterns induced by either the agonist antibody-analogs or trastuzumab. The diagram depicts three potential dimer conformations; 1) the basal state induced by high cell surface density, 2) the activated state induced by the bis-Fab agonist, and 3) the inhibited state stabilized by trastuzumab. The cell growth activity of agonist bis-Fabs may be due to stabilization of an allosterically activated conformation between HER2–HER2 dimers. Trastuzumab's antagonistic activity may arise from dimer orientations that favor the inactive allosteric interactions between kinases. A non-stabilized dimer may represent the basal state where interactions between the juxtamembrane (black line) loop of the activator kinase and the C-terminal lobe of the receiver kinase are not fully stabilized without agonist binding.

    Techniques Used: Activity Assay, Cell Culture, Cell Counting, Standard Deviation, Western Blot, Enzyme-linked Immunosorbent Assay, Binding Assay

    Quantification of  HER2 phosphorylation  and the differences after treatment.
    Figure Legend Snippet: Quantification of HER2 phosphorylation and the differences after treatment.

    Techniques Used:

    (a) This panel compares phosphorylation differences at fifteen sites in HER2 after treatment with either the agonist bis-Fab 1325 or trastuzumab. The top panel shows differences between agonist treatment and no treatment (basal phosphorylation). Seven of the sites showed statistically significant increases in phosphorylation (red dots above the line), five sites showed no change, and one site decreased. The same comparison is made between trastuzumab (antagonist) and no treatment shown in the second panel. A third comparison is made between bis-Fab 1325 and trastuzumab. Here, sites that show statistically significant differences between the treatments are indicated by red dots. Those phosphorylation sites that are significantly higher than trastuzumab treatment are highlighted with green background. The results were analyzed with a Tukey-Kramer all-pairwise test and the error bars indicate the 95% confidence level. Methods used are described in detail in the Supplementary Information. shows the raw data consisting of nine mass spec measurements for each treatment and phosphorylation site. Red color is used to indicate a statistically significant difference between the two samples with a P-value of <0.05. (b) This illustration of the HER2 intracellular domains shows phosphorylation sites identified by mass spectrometry. Phosphorylation sites colored orange denote sites with measureable increases, blue for decreases and uncolored for no change after agonist bis-Fab 1325 treatment. Phosphorylation sites that are significantly higher in agonist treatments compared to trastuzumab treatments are indicated by arrows.
    Figure Legend Snippet: (a) This panel compares phosphorylation differences at fifteen sites in HER2 after treatment with either the agonist bis-Fab 1325 or trastuzumab. The top panel shows differences between agonist treatment and no treatment (basal phosphorylation). Seven of the sites showed statistically significant increases in phosphorylation (red dots above the line), five sites showed no change, and one site decreased. The same comparison is made between trastuzumab (antagonist) and no treatment shown in the second panel. A third comparison is made between bis-Fab 1325 and trastuzumab. Here, sites that show statistically significant differences between the treatments are indicated by red dots. Those phosphorylation sites that are significantly higher than trastuzumab treatment are highlighted with green background. The results were analyzed with a Tukey-Kramer all-pairwise test and the error bars indicate the 95% confidence level. Methods used are described in detail in the Supplementary Information. shows the raw data consisting of nine mass spec measurements for each treatment and phosphorylation site. Red color is used to indicate a statistically significant difference between the two samples with a P-value of <0.05. (b) This illustration of the HER2 intracellular domains shows phosphorylation sites identified by mass spectrometry. Phosphorylation sites colored orange denote sites with measureable increases, blue for decreases and uncolored for no change after agonist bis-Fab 1325 treatment. Phosphorylation sites that are significantly higher in agonist treatments compared to trastuzumab treatments are indicated by arrows.

    Techniques Used: Mass Spectrometry

    p her2  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc p her2
    P Her2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p her2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p her2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    erbb2 tob  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc erbb2 tob
    Erbb2 Tob, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erbb2 tob/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erbb2 tob - by Bioz Stars, 2023-02
    94/100 stars

    Images

    erb b2  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc erb b2
    Erb B2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erb b2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erb b2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    erbb2 oncogene  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc erbb2 oncogene
    <t>ERBB2</t> and RAS protein levels were assessed by Western blots using antibodies against H-RAS or ERBB2 for total cell lysates prepared from prostate cancer cells transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Blots with antibodies against actin served as loading controls. Numbers in white represent fold changes in ERBB2 or RAS protein levels in ERBB2 - or RAS -overexpressing cells relative to those in their corresponding PBP control cells after the actin normalization.
    Erbb2 Oncogene, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erbb2 oncogene/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erbb2 oncogene - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells"

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0099525

    ERBB2 and RAS protein levels were assessed by Western blots using antibodies against H-RAS or ERBB2 for total cell lysates prepared from prostate cancer cells transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Blots with antibodies against actin served as loading controls. Numbers in white represent fold changes in ERBB2 or RAS protein levels in ERBB2 - or RAS -overexpressing cells relative to those in their corresponding PBP control cells after the actin normalization.
    Figure Legend Snippet: ERBB2 and RAS protein levels were assessed by Western blots using antibodies against H-RAS or ERBB2 for total cell lysates prepared from prostate cancer cells transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Blots with antibodies against actin served as loading controls. Numbers in white represent fold changes in ERBB2 or RAS protein levels in ERBB2 - or RAS -overexpressing cells relative to those in their corresponding PBP control cells after the actin normalization.

    Techniques Used: Western Blot, Transfection

    Cell growth rates were assessed by cell counting every 12 hours or 24 hours for various prostate cancer cells that were transfected with control retroviruses ( PBP ), or retroviruses overexpressing either PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ).
    Figure Legend Snippet: Cell growth rates were assessed by cell counting every 12 hours or 24 hours for various prostate cancer cells that were transfected with control retroviruses ( PBP ), or retroviruses overexpressing either PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ).

    Techniques Used: Cell Counting, Transfection

    Cell migration rates were estimated by a wound healing assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Left panels showed percentages of wounds remained at different time points. The percentages of wounds were estimated based on the average of 12 measurements on each plate reflecting measurements of four evenly distributed sections on each of the three wounds/scratches on each plate. Data were presented as means ± SD from three replicates. Right panels showed representative images taken at different time points. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.
    Figure Legend Snippet: Cell migration rates were estimated by a wound healing assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Left panels showed percentages of wounds remained at different time points. The percentages of wounds were estimated based on the average of 12 measurements on each plate reflecting measurements of four evenly distributed sections on each of the three wounds/scratches on each plate. Data were presented as means ± SD from three replicates. Right panels showed representative images taken at different time points. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Techniques Used: Migration, Wound Healing Assay, Transfection

    Cell motilities were assessed by a transwell-based motility assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the relative numbers of cells that have passed through the transwell inserts/membranes, which were stained and counted under a microscope for at least 10 fields per insert. Data were presented as means ± SD from three replicates. Representative images taken at a given time point were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.
    Figure Legend Snippet: Cell motilities were assessed by a transwell-based motility assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the relative numbers of cells that have passed through the transwell inserts/membranes, which were stained and counted under a microscope for at least 10 fields per insert. Data were presented as means ± SD from three replicates. Representative images taken at a given time point were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Techniques Used: Motility Assay, Transfection, Staining, Microscopy

    Cell invasiveness was assessed by a transwell-based invasion assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the numbers of cells that have passed through the collagen matrix either 72 hours (for PC3 cells) or 96 hours (for DU145 cells) after plating. Transwell inserts were stained and invading cells were counted for the entire inserts. Data were presented as means ± SD from three replicates. Representative images were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.
    Figure Legend Snippet: Cell invasiveness was assessed by a transwell-based invasion assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the numbers of cells that have passed through the collagen matrix either 72 hours (for PC3 cells) or 96 hours (for DU145 cells) after plating. Transwell inserts were stained and invading cells were counted for the entire inserts. Data were presented as means ± SD from three replicates. Representative images were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Techniques Used: Transwell Invasion Assay, Transfection, Staining

    (A) Senescence-associated β-galactosidase activities were assessed by X-gal staining for human prostate cancer cell lines transfected with either control retroviruses ( PBP ) or retroviruses overexpressing PBP-H-RAS ( RAS ). PC3 cells expressing an extremely high level of RAS ( Hi-RAS ) were included for comparisons. Senescent BJ human skin fibroblast cells were used as a positive control for X-gal staining. Representative images were shown with representative X-gal-positive cells being marked with red arrows. Inserts in each image showed magnified, representative X-gal-positive cells. ( B ) Quantifications of data collected from panel ( A ). Data were presented as means ± SD from three replicates. ( C ) RAS protein levels assessed by Western blot analysis with antibodies against H-RAS for parental PC3 cells (P), PC3 cells transfected with control retroviruses ( PBP ), or PC3 cells transfected with the PBP-H-RAS retroviruses overexpressing a moderate level of RAS ( RAS ) or a much higher level of RAS ( Hi-RAS ). A blot using antibodies against actin was used as a loading control. Numbers in white represent RAS protein levels in fold changes in ERBB2 - or RAS -overexpressing cells relative to those in PBP control cells after the actin normalization. Scare bar: 100 µM.
    Figure Legend Snippet: (A) Senescence-associated β-galactosidase activities were assessed by X-gal staining for human prostate cancer cell lines transfected with either control retroviruses ( PBP ) or retroviruses overexpressing PBP-H-RAS ( RAS ). PC3 cells expressing an extremely high level of RAS ( Hi-RAS ) were included for comparisons. Senescent BJ human skin fibroblast cells were used as a positive control for X-gal staining. Representative images were shown with representative X-gal-positive cells being marked with red arrows. Inserts in each image showed magnified, representative X-gal-positive cells. ( B ) Quantifications of data collected from panel ( A ). Data were presented as means ± SD from three replicates. ( C ) RAS protein levels assessed by Western blot analysis with antibodies against H-RAS for parental PC3 cells (P), PC3 cells transfected with control retroviruses ( PBP ), or PC3 cells transfected with the PBP-H-RAS retroviruses overexpressing a moderate level of RAS ( RAS ) or a much higher level of RAS ( Hi-RAS ). A blot using antibodies against actin was used as a loading control. Numbers in white represent RAS protein levels in fold changes in ERBB2 - or RAS -overexpressing cells relative to those in PBP control cells after the actin normalization. Scare bar: 100 µM.

    Techniques Used: Staining, Transfection, Expressing, Positive Control, Western Blot

    Protein levels for various kinases and their phosphorylated forms were assessed by Western blot analyses for parental prostate cancer cells that were transfected either with control retroviruses ( PBP ), or with retroviruses overexpressing PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Actin was used as a loading control. Numbers in white represent protein levels in fold changes relative to those in PBP control cells after the actin normalization.
    Figure Legend Snippet: Protein levels for various kinases and their phosphorylated forms were assessed by Western blot analyses for parental prostate cancer cells that were transfected either with control retroviruses ( PBP ), or with retroviruses overexpressing PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Actin was used as a loading control. Numbers in white represent protein levels in fold changes relative to those in PBP control cells after the actin normalization.

    Techniques Used: Western Blot, Transfection

    phospho her2  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc phospho her2
    Lapatinib treatment inhibits AKT signaling in HPV-positive cells. Notes: Cells were treated with lapatinib (1 μM) or DMSO (vehicle control) 16 hours after plating. After 24-hour treatment, protein extraction was performed. The phosphorylation and levels of EGFR (Tyr1068), <t>HER2</t> (Tyr1221/1222), and AKT (Ser473) were analyzed by Western blotting of HPV-positive ( A ) and HPV-negative cell lines ( B ). Beta-actin immunoblotting was used as a loading control. A representative picture of three independent experiments is shown. Quantification of AKT and pAKT was performed by densitometric analysis, and the mean ratio of pAKT/AKT from three independent experiments is depicted in the right panels. *** P ,0.001, paired t -test. Abbreviations: HPV, human papillomavirus; DMSO, dimethylsulfoxide.
    Phospho Her2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho her2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho her2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Cytotoxic effect of lapatinib is restricted to human papillomavirus-positive head and neck squamous cell carcinoma cell lines"

    Article Title: Cytotoxic effect of lapatinib is restricted to human papillomavirus-positive head and neck squamous cell carcinoma cell lines

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S68235

    Lapatinib treatment inhibits AKT signaling in HPV-positive cells. Notes: Cells were treated with lapatinib (1 μM) or DMSO (vehicle control) 16 hours after plating. After 24-hour treatment, protein extraction was performed. The phosphorylation and levels of EGFR (Tyr1068), HER2 (Tyr1221/1222), and AKT (Ser473) were analyzed by Western blotting of HPV-positive ( A ) and HPV-negative cell lines ( B ). Beta-actin immunoblotting was used as a loading control. A representative picture of three independent experiments is shown. Quantification of AKT and pAKT was performed by densitometric analysis, and the mean ratio of pAKT/AKT from three independent experiments is depicted in the right panels. *** P ,0.001, paired t -test. Abbreviations: HPV, human papillomavirus; DMSO, dimethylsulfoxide.
    Figure Legend Snippet: Lapatinib treatment inhibits AKT signaling in HPV-positive cells. Notes: Cells were treated with lapatinib (1 μM) or DMSO (vehicle control) 16 hours after plating. After 24-hour treatment, protein extraction was performed. The phosphorylation and levels of EGFR (Tyr1068), HER2 (Tyr1221/1222), and AKT (Ser473) were analyzed by Western blotting of HPV-positive ( A ) and HPV-negative cell lines ( B ). Beta-actin immunoblotting was used as a loading control. A representative picture of three independent experiments is shown. Quantification of AKT and pAKT was performed by densitometric analysis, and the mean ratio of pAKT/AKT from three independent experiments is depicted in the right panels. *** P ,0.001, paired t -test. Abbreviations: HPV, human papillomavirus; DMSO, dimethylsulfoxide.

    Techniques Used: Protein Extraction, Western Blot

    List of antibodies
    Figure Legend Snippet: List of antibodies

    Techniques Used:

    her 2 c erb b2  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc her 2 c erb b2
    Her 2 C Erb B2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/her 2 c erb b2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    her 2 c erb b2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Cell Signaling Technology Inc erbb2
    ErbB3 interacts with <t>erbB2</t> to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.
    Erbb2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erbb2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erbb2 - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc phosphorylated erbb2 tyr1248
    (A) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Cell lysates were separated into cytosolic (supernatant) and total membrane (pellet) fractions. The pellet fraction was subjected to immunoprecipitation with anti-Myc (nucleolin) or anti-HA (control) antibodies and immunoblotted with specific ErbBs antibodies. Total pellet and supernatant extracts are shown in the right lanes of each panel. (B) COS7 cells were transiently co-transfected with expression vector of ErbB1 and Myc-Nucleolin. Nuclear and non-nuclear cell extracts were immunoblotted with anti-ErbB1 antibodies. As control for the fractionation purity Blots were reacted with anti-PARP antibodies (as a nuclear marker) and anti-tubulin antibodies (as a cytosolic marker). (C) Cell lysates prepared from SKBR3 cells were subjected to immunoprecipitation with either anti-nucleolin or anti <t>ErbB2</t> antibodies and immunoblotted with either anti- ErbB2 or anti-nucleolin antibodies as indicated, as a control total cell lysates are shown in the right lane of each panel.
    Phosphorylated Erbb2 Tyr1248, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphorylated erbb2 tyr1248/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphorylated erbb2 tyr1248 - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc her2
    Relationships of AK4 and clinicopathological characteristics in 98 patients with <t> HER2 </t> overexpression breast cancer.
    Her2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/her2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    her2 - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc her2 phosphorylation sites
    (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting <t>HER2</t> (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.
    Her2 Phosphorylation Sites, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/her2 phosphorylation sites/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    her2 phosphorylation sites - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc p her2
    (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting <t>HER2</t> (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.
    P Her2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p her2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p her2 - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc erbb2 tob
    (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting <t>HER2</t> (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.
    Erbb2 Tob, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erbb2 tob/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erbb2 tob - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc erb b2
    (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting <t>HER2</t> (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.
    Erb B2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erb b2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erb b2 - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc erbb2 oncogene
    <t>ERBB2</t> and RAS protein levels were assessed by Western blots using antibodies against H-RAS or ERBB2 for total cell lysates prepared from prostate cancer cells transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Blots with antibodies against actin served as loading controls. Numbers in white represent fold changes in ERBB2 or RAS protein levels in ERBB2 - or RAS -overexpressing cells relative to those in their corresponding PBP control cells after the actin normalization.
    Erbb2 Oncogene, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/erbb2 oncogene/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    erbb2 oncogene - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc phospho her2
    Lapatinib treatment inhibits AKT signaling in HPV-positive cells. Notes: Cells were treated with lapatinib (1 μM) or DMSO (vehicle control) 16 hours after plating. After 24-hour treatment, protein extraction was performed. The phosphorylation and levels of EGFR (Tyr1068), <t>HER2</t> (Tyr1221/1222), and AKT (Ser473) were analyzed by Western blotting of HPV-positive ( A ) and HPV-negative cell lines ( B ). Beta-actin immunoblotting was used as a loading control. A representative picture of three independent experiments is shown. Quantification of AKT and pAKT was performed by densitometric analysis, and the mean ratio of pAKT/AKT from three independent experiments is depicted in the right panels. *** P ,0.001, paired t -test. Abbreviations: HPV, human papillomavirus; DMSO, dimethylsulfoxide.
    Phospho Her2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho her2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho her2 - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc her 2 c erb b2
    Lapatinib treatment inhibits AKT signaling in HPV-positive cells. Notes: Cells were treated with lapatinib (1 μM) or DMSO (vehicle control) 16 hours after plating. After 24-hour treatment, protein extraction was performed. The phosphorylation and levels of EGFR (Tyr1068), <t>HER2</t> (Tyr1221/1222), and AKT (Ser473) were analyzed by Western blotting of HPV-positive ( A ) and HPV-negative cell lines ( B ). Beta-actin immunoblotting was used as a loading control. A representative picture of three independent experiments is shown. Quantification of AKT and pAKT was performed by densitometric analysis, and the mean ratio of pAKT/AKT from three independent experiments is depicted in the right panels. *** P ,0.001, paired t -test. Abbreviations: HPV, human papillomavirus; DMSO, dimethylsulfoxide.
    Her 2 C Erb B2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/her 2 c erb b2/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    her 2 c erb b2 - by Bioz Stars, 2023-02
    94/100 stars
      Buy from Supplier

    Image Search Results


    ErbB3 interacts with erbB2 to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.

    Journal: Molecular Cancer

    Article Title: Targeting of erbB3 receptor to overcome resistance in cancer treatment

    doi: 10.1186/1476-4598-13-105

    Figure Lengend Snippet: ErbB3 interacts with erbB2 to activate signaling pathways leading to multi-drug resistance in breast cancer. Hetero-dimerization of erbB2 and erbB3 is able to induce activation of multiple downstream signaling pathways. In both luminal B and erbB2+ subtypes of human breast cancer, erbB2/erbB3 association may recruit IGF-1R to form a trimeric complex activating PI-3 K/Akt signaling and Src kinase and resulting in trastuzumab resistance. In erbB2+ breast cancer, interaction between erbB2 and erbB3 upregulates Survivin via a PI-3 K/Akt-dependent mechanism, and thereby confers paclitaxel resistance. In luminal B breast cancer, the erbB2/erbB3 hetero-dimers modulate ERα phosphorylation (activation) mainly through MEK/MAPK and/or PI-3 K/Akt signaling pathways, and subsequently alter tamoxifen sensitivity. These data support the hypothesis that targeting of erbB3 will significantly enhance the efficacy of those commonly used therapeutics in the treatment of erbB2+ breast cancer.

    Article Snippet: It has been reported that erbB3 functions primarily to drive erbB2-mediated cell signaling [ , ].

    Techniques: Activation Assay

    Current and novel therapeutic strategies targeting of erbB2 and/or erbB3 receptors for cancer therapy. Several erbB2-targeted therapies (trastuzumab, pertuzumab, T-DM1, and lapatinib) have being used in clinic, whereas no erbB3-targeted therapy has been approved for cancer treatment. Blocking Abs, such as MM-121, MM-111, AMG 888/U3-1287, and MP-RM-1/EV20, are the only agents being tested in early clinical and/or preclinical investigations. Our recent data show that entinostat, a class I HDAC inhibitor selectively downregulates erbB2/erbB3 via induction of specific miRNAs, miR-125a, miR-125b, and miR-205 in erbB2+ breast cancer cells. Further characterization demonstrates that these “sister” miRNAs (share common targets) act in concert to inhibit erbB2/erbB3 protein translation. Thus, the novel strategy, like cooperative miRNA targeting of erbB2/erbB3 may represent a new approach for cancer therapy.

    Journal: Molecular Cancer

    Article Title: Targeting of erbB3 receptor to overcome resistance in cancer treatment

    doi: 10.1186/1476-4598-13-105

    Figure Lengend Snippet: Current and novel therapeutic strategies targeting of erbB2 and/or erbB3 receptors for cancer therapy. Several erbB2-targeted therapies (trastuzumab, pertuzumab, T-DM1, and lapatinib) have being used in clinic, whereas no erbB3-targeted therapy has been approved for cancer treatment. Blocking Abs, such as MM-121, MM-111, AMG 888/U3-1287, and MP-RM-1/EV20, are the only agents being tested in early clinical and/or preclinical investigations. Our recent data show that entinostat, a class I HDAC inhibitor selectively downregulates erbB2/erbB3 via induction of specific miRNAs, miR-125a, miR-125b, and miR-205 in erbB2+ breast cancer cells. Further characterization demonstrates that these “sister” miRNAs (share common targets) act in concert to inhibit erbB2/erbB3 protein translation. Thus, the novel strategy, like cooperative miRNA targeting of erbB2/erbB3 may represent a new approach for cancer therapy.

    Article Snippet: It has been reported that erbB3 functions primarily to drive erbB2-mediated cell signaling [ , ].

    Techniques: Blocking Assay

    (A) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Cell lysates were separated into cytosolic (supernatant) and total membrane (pellet) fractions. The pellet fraction was subjected to immunoprecipitation with anti-Myc (nucleolin) or anti-HA (control) antibodies and immunoblotted with specific ErbBs antibodies. Total pellet and supernatant extracts are shown in the right lanes of each panel. (B) COS7 cells were transiently co-transfected with expression vector of ErbB1 and Myc-Nucleolin. Nuclear and non-nuclear cell extracts were immunoblotted with anti-ErbB1 antibodies. As control for the fractionation purity Blots were reacted with anti-PARP antibodies (as a nuclear marker) and anti-tubulin antibodies (as a cytosolic marker). (C) Cell lysates prepared from SKBR3 cells were subjected to immunoprecipitation with either anti-nucleolin or anti ErbB2 antibodies and immunoblotted with either anti- ErbB2 or anti-nucleolin antibodies as indicated, as a control total cell lysates are shown in the right lane of each panel.

    Journal: PLoS ONE

    Article Title: Identification of Nucleolin as New ErbB Receptors- Interacting Protein

    doi: 10.1371/journal.pone.0002310

    Figure Lengend Snippet: (A) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Cell lysates were separated into cytosolic (supernatant) and total membrane (pellet) fractions. The pellet fraction was subjected to immunoprecipitation with anti-Myc (nucleolin) or anti-HA (control) antibodies and immunoblotted with specific ErbBs antibodies. Total pellet and supernatant extracts are shown in the right lanes of each panel. (B) COS7 cells were transiently co-transfected with expression vector of ErbB1 and Myc-Nucleolin. Nuclear and non-nuclear cell extracts were immunoblotted with anti-ErbB1 antibodies. As control for the fractionation purity Blots were reacted with anti-PARP antibodies (as a nuclear marker) and anti-tubulin antibodies (as a cytosolic marker). (C) Cell lysates prepared from SKBR3 cells were subjected to immunoprecipitation with either anti-nucleolin or anti ErbB2 antibodies and immunoblotted with either anti- ErbB2 or anti-nucleolin antibodies as indicated, as a control total cell lysates are shown in the right lane of each panel.

    Article Snippet: Polyclonal rabbit anti phosphorylated ErbB1 (Tyr1068) and phosphorylated ErbB2 (Tyr1248) were purchased from Cell Signaling technology.

    Techniques: Transfection, Expressing, Plasmid Preparation, Immunoprecipitation, Fractionation, Marker

    (A) COS7 cells were transiently co-transfected with expression vector of either ErbB1 or ErbB2 receptors alone or with Myc-Nucleolin. Following 30 min serum deprivation, cells were either untreated or treated with EGF 100 ng/ml for 5 min. Cell lysates were immunoblotted with anti-phosphorylated EGFR or anti-phosphorylated ErbB2 antibodies respectively. As control, lysates were immunoblotted with anti-EGFR or anti-ErbB2 antibodies. Note that at time 0 phosphorylated receptors are detected in cells expressing nucleolin and EGFR or ErbB2. (B) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Following 30 min serum deprivation cells were untreated or treated with either EGF 100 ng/ml or NRG 100 ng/ml for 5 min as indicated. Cell lysates were subjected to immunoprecipitation with anti-phosphotyrosine antibodies (PY20) and immunoblotted with specific ErbB antibodies. Note that in untreated cells, phosphorylated receptor is detected in cells expressing nucleolin and ErbB receptor. The values represent fold induction compared to the receptor levels in untreated cells (1).

    Journal: PLoS ONE

    Article Title: Identification of Nucleolin as New ErbB Receptors- Interacting Protein

    doi: 10.1371/journal.pone.0002310

    Figure Lengend Snippet: (A) COS7 cells were transiently co-transfected with expression vector of either ErbB1 or ErbB2 receptors alone or with Myc-Nucleolin. Following 30 min serum deprivation, cells were either untreated or treated with EGF 100 ng/ml for 5 min. Cell lysates were immunoblotted with anti-phosphorylated EGFR or anti-phosphorylated ErbB2 antibodies respectively. As control, lysates were immunoblotted with anti-EGFR or anti-ErbB2 antibodies. Note that at time 0 phosphorylated receptors are detected in cells expressing nucleolin and EGFR or ErbB2. (B) COS7 cells were transiently co-transfected with expression vector of each of the ErbB receptors and Myc-Nucleolin. Following 30 min serum deprivation cells were untreated or treated with either EGF 100 ng/ml or NRG 100 ng/ml for 5 min as indicated. Cell lysates were subjected to immunoprecipitation with anti-phosphotyrosine antibodies (PY20) and immunoblotted with specific ErbB antibodies. Note that in untreated cells, phosphorylated receptor is detected in cells expressing nucleolin and ErbB receptor. The values represent fold induction compared to the receptor levels in untreated cells (1).

    Article Snippet: Polyclonal rabbit anti phosphorylated ErbB1 (Tyr1068) and phosphorylated ErbB2 (Tyr1248) were purchased from Cell Signaling technology.

    Techniques: Transfection, Expressing, Plasmid Preparation, Immunoprecipitation

    Relationships of AK4 and clinicopathological characteristics in 98 patients with  HER2  overexpression breast cancer.

    Journal: Disease Markers

    Article Title: AK4 Promotes the Progression of HER2-Positive Breast Cancer by Facilitating Cell Proliferation and Invasion

    doi: 10.1155/2019/8186091

    Figure Lengend Snippet: Relationships of AK4 and clinicopathological characteristics in 98 patients with HER2 overexpression breast cancer.

    Article Snippet: Tumor cells or tissues of HER2-positive breast cancers were lysed in RIPA Buffer (9800, Cell Signaling Technology, Danvers, MA).

    Techniques: Over Expression, Expressing

    AK4 was highly expressed in human HER2-positive breast cancer tissues. (a) IHC assays were performed, and the representative photographs of AK4 expression levels in HER2-positive breast cancer tissues were detected and shown (×100 and ×200 magnification, respectively). (b) IHC staining showed AK4 expression levels in adjacent nontumor tissues (×100 and ×200 magnification, respectively).

    Journal: Disease Markers

    Article Title: AK4 Promotes the Progression of HER2-Positive Breast Cancer by Facilitating Cell Proliferation and Invasion

    doi: 10.1155/2019/8186091

    Figure Lengend Snippet: AK4 was highly expressed in human HER2-positive breast cancer tissues. (a) IHC assays were performed, and the representative photographs of AK4 expression levels in HER2-positive breast cancer tissues were detected and shown (×100 and ×200 magnification, respectively). (b) IHC staining showed AK4 expression levels in adjacent nontumor tissues (×100 and ×200 magnification, respectively).

    Article Snippet: Tumor cells or tissues of HER2-positive breast cancers were lysed in RIPA Buffer (9800, Cell Signaling Technology, Danvers, MA).

    Techniques: Expressing, Immunohistochemistry

    AK4 facilitates cell proliferation and invasion of HER2-positive breast cancer in vitro. (a) Colony formation assays were then performed using MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and colony number was counted. (b) The results of MTT assays showed the inhibition of cell proliferation caused by AK4 knockdown. (c) AK4 depletion resulted in the lower migration degree in MCF7 and MDA-MB-231 cells. Photographs showing that at the 0 and 24th-hour time point migrated cells were present. (d) Transwell assays using both MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and the degree of invasion was quantified by the invasion cell number. Results are presented as mean ± SD, ∗ P < 0.05.

    Journal: Disease Markers

    Article Title: AK4 Promotes the Progression of HER2-Positive Breast Cancer by Facilitating Cell Proliferation and Invasion

    doi: 10.1155/2019/8186091

    Figure Lengend Snippet: AK4 facilitates cell proliferation and invasion of HER2-positive breast cancer in vitro. (a) Colony formation assays were then performed using MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and colony number was counted. (b) The results of MTT assays showed the inhibition of cell proliferation caused by AK4 knockdown. (c) AK4 depletion resulted in the lower migration degree in MCF7 and MDA-MB-231 cells. Photographs showing that at the 0 and 24th-hour time point migrated cells were present. (d) Transwell assays using both MCF7 and MDA-MB-231 cells transfected with control or AK4 shRNA plasmids, and the degree of invasion was quantified by the invasion cell number. Results are presented as mean ± SD, ∗ P < 0.05.

    Article Snippet: Tumor cells or tissues of HER2-positive breast cancers were lysed in RIPA Buffer (9800, Cell Signaling Technology, Danvers, MA).

    Techniques: In Vitro, Transfection, shRNA, Inhibition, Migration

    AK4 induces tumor growth and metastasis of HER2-positive breast cancer in mice. (a) MCF7 cells infected with control or AK4 shRNA lentivirus were subcutaneously implanted into nude mice. After 2 weeks, tumors were isolated, and the volume of tumor was measured every 7 days ( n = 5 in each group). Tumor growth curves were calculated and evaluated based on the average volume of 5 tumors in AK4 knockdown and control groups. (b) MCF7 cells infected with control or AK4 shRNA lentivirus were implanted into the caudal vein of nude mice. After 8 weeks, tumors were isolated from mice in each group and weighted ( n = 5 for each group). (c) IHC assays showed the expression levels of AK4 in control or AK4 ablation tumors isolated from mice. Results are presented as mean ± SD, ∗ P < 0.05.

    Journal: Disease Markers

    Article Title: AK4 Promotes the Progression of HER2-Positive Breast Cancer by Facilitating Cell Proliferation and Invasion

    doi: 10.1155/2019/8186091

    Figure Lengend Snippet: AK4 induces tumor growth and metastasis of HER2-positive breast cancer in mice. (a) MCF7 cells infected with control or AK4 shRNA lentivirus were subcutaneously implanted into nude mice. After 2 weeks, tumors were isolated, and the volume of tumor was measured every 7 days ( n = 5 in each group). Tumor growth curves were calculated and evaluated based on the average volume of 5 tumors in AK4 knockdown and control groups. (b) MCF7 cells infected with control or AK4 shRNA lentivirus were implanted into the caudal vein of nude mice. After 8 weeks, tumors were isolated from mice in each group and weighted ( n = 5 for each group). (c) IHC assays showed the expression levels of AK4 in control or AK4 ablation tumors isolated from mice. Results are presented as mean ± SD, ∗ P < 0.05.

    Article Snippet: Tumor cells or tissues of HER2-positive breast cancers were lysed in RIPA Buffer (9800, Cell Signaling Technology, Danvers, MA).

    Techniques: Infection, shRNA, Isolation, Expressing

    (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting HER2 (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.

    Journal: PLoS ONE

    Article Title: Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

    doi: 10.1371/journal.pone.0051817

    Figure Lengend Snippet: (a) A brief description of the bis-Fab synthesis process is illustrated here. The thio-Fabs of interest are produced by engineering an unpaired cysteine into the Fab region of an antibody followed by recombinant expression and isolation of the thio-Fab containing the unpaired cysteine. A homobifunctional crosslinking reagent is then used in a two-step process to efficiently couple two thio-Fabs together. A more detailed explanation of the procedure can be found in the Experimental Methods and . (b) A matrix combination of thioFabs using the two-step synthesis process was used to produce a panel of bis-Fab molecules for use in biological and biochemical assays. Two Fabs targeting EGFR (α-HER1-a targets domain III and α-HER1-b targets domain III) and two Fabs targeting HER2 (α-HER2-a derived from trastuzumab targets domain IV and α-HER2-b derived from pertuzumab targets domain II) were used to construct the matrix. (c) Trastuzumab and bis-Fab 1321, consisting of two trastuzumab Fabs linked together at position 110 in the light chain, were examined for their effect on cell growth. Increasing concentrations of trastuzumab (blue line) or bis-Fab 1321 (orange line) were added to BT474 cells and cell proliferation was measured after five days using AlamarBlue staining. The relative fluorescence units are reported for the different treatment concentrations. Individual data points for two independent experiments are shown in the plot as well as an average of the two, which are represented by the lines and open shapes. Trastuzumab analog (bis-Fab 1321) showed agonistic activity as measured by increased cell proliferation, whereas trastuzumab inhibited cell proliferation. (d) The schematic illustrates the site of covalent attachment between the Fabs of the parent antibody trastuzumab and bis-Fab 1321. Although the global conformations of the Fab domains are unknown, this figure highlights the distinct difference in the points of connection. The native interchain disulfides (hinge region, near HC-228) in the heavy chains of trastuzumab provided the covalent attachment site for the Fab arms in the antibody. In contrast, bis-Fab 1321 was covalently linked through light chains at LC-110 using a bis-maleimido crosslinker. The resultant molecules presented Fab Fv-regions in different relative orientations.

    Article Snippet: Isotopically-labeled synthetic peptides containing experimentally determined HER2 phosphorylation sites were custom made by Cell Signaling Technologies.

    Techniques: Produced, Recombinant, Expressing, Isolation, Derivative Assay, Construct, Staining, Fluorescence, Activity Assay

    Cell-surface binding and solution state properties of  HER2  agonists and antagonists.

    Journal: PLoS ONE

    Article Title: Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

    doi: 10.1371/journal.pone.0051817

    Figure Lengend Snippet: Cell-surface binding and solution state properties of HER2 agonists and antagonists.

    Article Snippet: Isotopically-labeled synthetic peptides containing experimentally determined HER2 phosphorylation sites were custom made by Cell Signaling Technologies.

    Techniques: Binding Assay

    (a) Four different thio-Fabs derived from trastuzumab were used to make ten bis-Fab analogs. Each thio-Fab mutant (LC-110, LC-205, HC-118, and HC-228) was reacted with the bis-maleimido crosslinker and recombined in a matrix format described in the Experimental Methods. Fabs were derived from several sources shown in and S 2B . Each chain of the Fab is represented by a different color (dark blue - heavy chain and light blue - light chain) and the position of the cysteine used in coupling is denoted by the red dot. (b) The matrix-generated bis-Fab linkage analogs are shown diagrammatically in this Figure. Color coded numbers indicate the type of activity observed, where tan signifies antagonist, dark blue signifies agonist, and light blue signifies no activity. (c) BT474 cells were incubated with the indicated concentrations of bis-Fabs shown in (b). The degree of cell proliferation was assessed after 5 days using AlamarBlue staining. The results are reported as a percentage of maximum proliferation relative to untreated controls. The measured values for each test sample, as well as individual replicates, are shown as raw data in . Color codes are the same as in (b). (d) A model of the complex formation between two HER2 extracelluar domains (ECD) and either an agonist (1321) or antagonist (1324) bis-Fab. Here is shown two light chain connected bis-Fabs with the heavy chain colored dark blue, the light chains colored lighter blue and the HER2 ECD colored magenta. In the left panel the two complexes are shown looking up at the membrane. The point of contact between the Fv-region of the Fab and the ECD is near the membrane. The HER2 protein terminates in this structure just prior to the point at which the transmembrane domain begins. The complex models are rotated 90 degrees on both the horizontal and vertical axis to produce this viewpoint. The plane of the membrane runs perpendicular to the page. The PBD ID Code used for model building was 1N8Z.

    Journal: PLoS ONE

    Article Title: Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

    doi: 10.1371/journal.pone.0051817

    Figure Lengend Snippet: (a) Four different thio-Fabs derived from trastuzumab were used to make ten bis-Fab analogs. Each thio-Fab mutant (LC-110, LC-205, HC-118, and HC-228) was reacted with the bis-maleimido crosslinker and recombined in a matrix format described in the Experimental Methods. Fabs were derived from several sources shown in and S 2B . Each chain of the Fab is represented by a different color (dark blue - heavy chain and light blue - light chain) and the position of the cysteine used in coupling is denoted by the red dot. (b) The matrix-generated bis-Fab linkage analogs are shown diagrammatically in this Figure. Color coded numbers indicate the type of activity observed, where tan signifies antagonist, dark blue signifies agonist, and light blue signifies no activity. (c) BT474 cells were incubated with the indicated concentrations of bis-Fabs shown in (b). The degree of cell proliferation was assessed after 5 days using AlamarBlue staining. The results are reported as a percentage of maximum proliferation relative to untreated controls. The measured values for each test sample, as well as individual replicates, are shown as raw data in . Color codes are the same as in (b). (d) A model of the complex formation between two HER2 extracelluar domains (ECD) and either an agonist (1321) or antagonist (1324) bis-Fab. Here is shown two light chain connected bis-Fabs with the heavy chain colored dark blue, the light chains colored lighter blue and the HER2 ECD colored magenta. In the left panel the two complexes are shown looking up at the membrane. The point of contact between the Fv-region of the Fab and the ECD is near the membrane. The HER2 protein terminates in this structure just prior to the point at which the transmembrane domain begins. The complex models are rotated 90 degrees on both the horizontal and vertical axis to produce this viewpoint. The plane of the membrane runs perpendicular to the page. The PBD ID Code used for model building was 1N8Z.

    Article Snippet: Isotopically-labeled synthetic peptides containing experimentally determined HER2 phosphorylation sites were custom made by Cell Signaling Technologies.

    Techniques: Derivative Assay, Mutagenesis, Generated, Activity Assay, Incubation, Staining

    (a) A time course of cell growth activity in BT474 cells in the presence of 100 nM trastuzumab, 100 nM bis-Fab 1325, or 10 nM heregulin. BT474 were cultured in media containing 10% fetal bovine serum for up to 84 hours. At 12-hour intervals total number of cells were determined; three plates from each treatment group were counted for the total number of cells and plotted as the mean cell count. The error bars indicate standard deviation from the mean. At approximately 60 hours (indicated by the arrow) the cells reached confluence in the agonist treatment groups. (b) BT474 cells were treated with 100 nM of trastuzumab, 100 nM of bis-Fab 1325, or 100 nM of bis-Fab 1329 for 10, 30 and 120 minutes. At times indicated, cell lysates were prepared and analyzed by immunoblotting using phospho-specific antibodies for HER3, AKT, and MAPK as well as antibodies recognizing total protein. Data are representative of three independent experiments. (c) Quantification of AKT phosphorylation after treatment with 100 nM bis-Fab 1325, 100 nM trastuzumab, 2 nM heregulin and a non-specific control antibody (anti-gD) by PathScan p-AKT1 (S473) ELISA. All data points were collected in triplicates and the mean of the triplicate absorbance values were used to calculate the percent change in pAKT compared to untreated control group. The error bars indicate standard deviation from the mean. Data are representative of three independent experiments. (d) A model for the HER2 dimerization patterns induced by either the agonist antibody-analogs or trastuzumab. The diagram depicts three potential dimer conformations; 1) the basal state induced by high cell surface density, 2) the activated state induced by the bis-Fab agonist, and 3) the inhibited state stabilized by trastuzumab. The cell growth activity of agonist bis-Fabs may be due to stabilization of an allosterically activated conformation between HER2–HER2 dimers. Trastuzumab's antagonistic activity may arise from dimer orientations that favor the inactive allosteric interactions between kinases. A non-stabilized dimer may represent the basal state where interactions between the juxtamembrane (black line) loop of the activator kinase and the C-terminal lobe of the receiver kinase are not fully stabilized without agonist binding.

    Journal: PLoS ONE

    Article Title: Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

    doi: 10.1371/journal.pone.0051817

    Figure Lengend Snippet: (a) A time course of cell growth activity in BT474 cells in the presence of 100 nM trastuzumab, 100 nM bis-Fab 1325, or 10 nM heregulin. BT474 were cultured in media containing 10% fetal bovine serum for up to 84 hours. At 12-hour intervals total number of cells were determined; three plates from each treatment group were counted for the total number of cells and plotted as the mean cell count. The error bars indicate standard deviation from the mean. At approximately 60 hours (indicated by the arrow) the cells reached confluence in the agonist treatment groups. (b) BT474 cells were treated with 100 nM of trastuzumab, 100 nM of bis-Fab 1325, or 100 nM of bis-Fab 1329 for 10, 30 and 120 minutes. At times indicated, cell lysates were prepared and analyzed by immunoblotting using phospho-specific antibodies for HER3, AKT, and MAPK as well as antibodies recognizing total protein. Data are representative of three independent experiments. (c) Quantification of AKT phosphorylation after treatment with 100 nM bis-Fab 1325, 100 nM trastuzumab, 2 nM heregulin and a non-specific control antibody (anti-gD) by PathScan p-AKT1 (S473) ELISA. All data points were collected in triplicates and the mean of the triplicate absorbance values were used to calculate the percent change in pAKT compared to untreated control group. The error bars indicate standard deviation from the mean. Data are representative of three independent experiments. (d) A model for the HER2 dimerization patterns induced by either the agonist antibody-analogs or trastuzumab. The diagram depicts three potential dimer conformations; 1) the basal state induced by high cell surface density, 2) the activated state induced by the bis-Fab agonist, and 3) the inhibited state stabilized by trastuzumab. The cell growth activity of agonist bis-Fabs may be due to stabilization of an allosterically activated conformation between HER2–HER2 dimers. Trastuzumab's antagonistic activity may arise from dimer orientations that favor the inactive allosteric interactions between kinases. A non-stabilized dimer may represent the basal state where interactions between the juxtamembrane (black line) loop of the activator kinase and the C-terminal lobe of the receiver kinase are not fully stabilized without agonist binding.

    Article Snippet: Isotopically-labeled synthetic peptides containing experimentally determined HER2 phosphorylation sites were custom made by Cell Signaling Technologies.

    Techniques: Activity Assay, Cell Culture, Cell Counting, Standard Deviation, Western Blot, Enzyme-linked Immunosorbent Assay, Binding Assay

    Quantification of  HER2 phosphorylation  and the differences after treatment.

    Journal: PLoS ONE

    Article Title: Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

    doi: 10.1371/journal.pone.0051817

    Figure Lengend Snippet: Quantification of HER2 phosphorylation and the differences after treatment.

    Article Snippet: Isotopically-labeled synthetic peptides containing experimentally determined HER2 phosphorylation sites were custom made by Cell Signaling Technologies.

    Techniques:

    (a) This panel compares phosphorylation differences at fifteen sites in HER2 after treatment with either the agonist bis-Fab 1325 or trastuzumab. The top panel shows differences between agonist treatment and no treatment (basal phosphorylation). Seven of the sites showed statistically significant increases in phosphorylation (red dots above the line), five sites showed no change, and one site decreased. The same comparison is made between trastuzumab (antagonist) and no treatment shown in the second panel. A third comparison is made between bis-Fab 1325 and trastuzumab. Here, sites that show statistically significant differences between the treatments are indicated by red dots. Those phosphorylation sites that are significantly higher than trastuzumab treatment are highlighted with green background. The results were analyzed with a Tukey-Kramer all-pairwise test and the error bars indicate the 95% confidence level. Methods used are described in detail in the Supplementary Information. shows the raw data consisting of nine mass spec measurements for each treatment and phosphorylation site. Red color is used to indicate a statistically significant difference between the two samples with a P-value of <0.05. (b) This illustration of the HER2 intracellular domains shows phosphorylation sites identified by mass spectrometry. Phosphorylation sites colored orange denote sites with measureable increases, blue for decreases and uncolored for no change after agonist bis-Fab 1325 treatment. Phosphorylation sites that are significantly higher in agonist treatments compared to trastuzumab treatments are indicated by arrows.

    Journal: PLoS ONE

    Article Title: Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

    doi: 10.1371/journal.pone.0051817

    Figure Lengend Snippet: (a) This panel compares phosphorylation differences at fifteen sites in HER2 after treatment with either the agonist bis-Fab 1325 or trastuzumab. The top panel shows differences between agonist treatment and no treatment (basal phosphorylation). Seven of the sites showed statistically significant increases in phosphorylation (red dots above the line), five sites showed no change, and one site decreased. The same comparison is made between trastuzumab (antagonist) and no treatment shown in the second panel. A third comparison is made between bis-Fab 1325 and trastuzumab. Here, sites that show statistically significant differences between the treatments are indicated by red dots. Those phosphorylation sites that are significantly higher than trastuzumab treatment are highlighted with green background. The results were analyzed with a Tukey-Kramer all-pairwise test and the error bars indicate the 95% confidence level. Methods used are described in detail in the Supplementary Information. shows the raw data consisting of nine mass spec measurements for each treatment and phosphorylation site. Red color is used to indicate a statistically significant difference between the two samples with a P-value of <0.05. (b) This illustration of the HER2 intracellular domains shows phosphorylation sites identified by mass spectrometry. Phosphorylation sites colored orange denote sites with measureable increases, blue for decreases and uncolored for no change after agonist bis-Fab 1325 treatment. Phosphorylation sites that are significantly higher in agonist treatments compared to trastuzumab treatments are indicated by arrows.

    Article Snippet: Isotopically-labeled synthetic peptides containing experimentally determined HER2 phosphorylation sites were custom made by Cell Signaling Technologies.

    Techniques: Mass Spectrometry

    ERBB2 and RAS protein levels were assessed by Western blots using antibodies against H-RAS or ERBB2 for total cell lysates prepared from prostate cancer cells transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Blots with antibodies against actin served as loading controls. Numbers in white represent fold changes in ERBB2 or RAS protein levels in ERBB2 - or RAS -overexpressing cells relative to those in their corresponding PBP control cells after the actin normalization.

    Journal: PLoS ONE

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    doi: 10.1371/journal.pone.0099525

    Figure Lengend Snippet: ERBB2 and RAS protein levels were assessed by Western blots using antibodies against H-RAS or ERBB2 for total cell lysates prepared from prostate cancer cells transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Blots with antibodies against actin served as loading controls. Numbers in white represent fold changes in ERBB2 or RAS protein levels in ERBB2 - or RAS -overexpressing cells relative to those in their corresponding PBP control cells after the actin normalization.

    Article Snippet: Cell signaling pathways activated by the ERBB2 oncogene or the RAS oncogene are frequently found to be altered in metastatic prostate cancers.

    Techniques: Western Blot, Transfection

    Cell growth rates were assessed by cell counting every 12 hours or 24 hours for various prostate cancer cells that were transfected with control retroviruses ( PBP ), or retroviruses overexpressing either PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ).

    Journal: PLoS ONE

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    doi: 10.1371/journal.pone.0099525

    Figure Lengend Snippet: Cell growth rates were assessed by cell counting every 12 hours or 24 hours for various prostate cancer cells that were transfected with control retroviruses ( PBP ), or retroviruses overexpressing either PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ).

    Article Snippet: Cell signaling pathways activated by the ERBB2 oncogene or the RAS oncogene are frequently found to be altered in metastatic prostate cancers.

    Techniques: Cell Counting, Transfection

    Cell migration rates were estimated by a wound healing assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Left panels showed percentages of wounds remained at different time points. The percentages of wounds were estimated based on the average of 12 measurements on each plate reflecting measurements of four evenly distributed sections on each of the three wounds/scratches on each plate. Data were presented as means ± SD from three replicates. Right panels showed representative images taken at different time points. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Journal: PLoS ONE

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    doi: 10.1371/journal.pone.0099525

    Figure Lengend Snippet: Cell migration rates were estimated by a wound healing assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Left panels showed percentages of wounds remained at different time points. The percentages of wounds were estimated based on the average of 12 measurements on each plate reflecting measurements of four evenly distributed sections on each of the three wounds/scratches on each plate. Data were presented as means ± SD from three replicates. Right panels showed representative images taken at different time points. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Article Snippet: Cell signaling pathways activated by the ERBB2 oncogene or the RAS oncogene are frequently found to be altered in metastatic prostate cancers.

    Techniques: Migration, Wound Healing Assay, Transfection

    Cell motilities were assessed by a transwell-based motility assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the relative numbers of cells that have passed through the transwell inserts/membranes, which were stained and counted under a microscope for at least 10 fields per insert. Data were presented as means ± SD from three replicates. Representative images taken at a given time point were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Journal: PLoS ONE

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    doi: 10.1371/journal.pone.0099525

    Figure Lengend Snippet: Cell motilities were assessed by a transwell-based motility assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the relative numbers of cells that have passed through the transwell inserts/membranes, which were stained and counted under a microscope for at least 10 fields per insert. Data were presented as means ± SD from three replicates. Representative images taken at a given time point were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Article Snippet: Cell signaling pathways activated by the ERBB2 oncogene or the RAS oncogene are frequently found to be altered in metastatic prostate cancers.

    Techniques: Motility Assay, Transfection, Staining, Microscopy

    Cell invasiveness was assessed by a transwell-based invasion assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the numbers of cells that have passed through the collagen matrix either 72 hours (for PC3 cells) or 96 hours (for DU145 cells) after plating. Transwell inserts were stained and invading cells were counted for the entire inserts. Data were presented as means ± SD from three replicates. Representative images were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Journal: PLoS ONE

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    doi: 10.1371/journal.pone.0099525

    Figure Lengend Snippet: Cell invasiveness was assessed by a transwell-based invasion assay for prostate cancer cells that were transfected with either control retroviruses ( PBP ), or retroviruses overexpressing PBP - H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Each bar graph showed the numbers of cells that have passed through the collagen matrix either 72 hours (for PC3 cells) or 96 hours (for DU145 cells) after plating. Transwell inserts were stained and invading cells were counted for the entire inserts. Data were presented as means ± SD from three replicates. Representative images were shown underneath each bar graph. All images were taken at the same scale with a scale bar of 200 µM displayed in the first image.

    Article Snippet: Cell signaling pathways activated by the ERBB2 oncogene or the RAS oncogene are frequently found to be altered in metastatic prostate cancers.

    Techniques: Transwell Invasion Assay, Transfection, Staining

    (A) Senescence-associated β-galactosidase activities were assessed by X-gal staining for human prostate cancer cell lines transfected with either control retroviruses ( PBP ) or retroviruses overexpressing PBP-H-RAS ( RAS ). PC3 cells expressing an extremely high level of RAS ( Hi-RAS ) were included for comparisons. Senescent BJ human skin fibroblast cells were used as a positive control for X-gal staining. Representative images were shown with representative X-gal-positive cells being marked with red arrows. Inserts in each image showed magnified, representative X-gal-positive cells. ( B ) Quantifications of data collected from panel ( A ). Data were presented as means ± SD from three replicates. ( C ) RAS protein levels assessed by Western blot analysis with antibodies against H-RAS for parental PC3 cells (P), PC3 cells transfected with control retroviruses ( PBP ), or PC3 cells transfected with the PBP-H-RAS retroviruses overexpressing a moderate level of RAS ( RAS ) or a much higher level of RAS ( Hi-RAS ). A blot using antibodies against actin was used as a loading control. Numbers in white represent RAS protein levels in fold changes in ERBB2 - or RAS -overexpressing cells relative to those in PBP control cells after the actin normalization. Scare bar: 100 µM.

    Journal: PLoS ONE

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    doi: 10.1371/journal.pone.0099525

    Figure Lengend Snippet: (A) Senescence-associated β-galactosidase activities were assessed by X-gal staining for human prostate cancer cell lines transfected with either control retroviruses ( PBP ) or retroviruses overexpressing PBP-H-RAS ( RAS ). PC3 cells expressing an extremely high level of RAS ( Hi-RAS ) were included for comparisons. Senescent BJ human skin fibroblast cells were used as a positive control for X-gal staining. Representative images were shown with representative X-gal-positive cells being marked with red arrows. Inserts in each image showed magnified, representative X-gal-positive cells. ( B ) Quantifications of data collected from panel ( A ). Data were presented as means ± SD from three replicates. ( C ) RAS protein levels assessed by Western blot analysis with antibodies against H-RAS for parental PC3 cells (P), PC3 cells transfected with control retroviruses ( PBP ), or PC3 cells transfected with the PBP-H-RAS retroviruses overexpressing a moderate level of RAS ( RAS ) or a much higher level of RAS ( Hi-RAS ). A blot using antibodies against actin was used as a loading control. Numbers in white represent RAS protein levels in fold changes in ERBB2 - or RAS -overexpressing cells relative to those in PBP control cells after the actin normalization. Scare bar: 100 µM.

    Article Snippet: Cell signaling pathways activated by the ERBB2 oncogene or the RAS oncogene are frequently found to be altered in metastatic prostate cancers.

    Techniques: Staining, Transfection, Expressing, Positive Control, Western Blot

    Protein levels for various kinases and their phosphorylated forms were assessed by Western blot analyses for parental prostate cancer cells that were transfected either with control retroviruses ( PBP ), or with retroviruses overexpressing PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Actin was used as a loading control. Numbers in white represent protein levels in fold changes relative to those in PBP control cells after the actin normalization.

    Journal: PLoS ONE

    Article Title: ERBB2 Increases Metastatic Potentials Specifically in Androgen-Insensitive Prostate Cancer Cells

    doi: 10.1371/journal.pone.0099525

    Figure Lengend Snippet: Protein levels for various kinases and their phosphorylated forms were assessed by Western blot analyses for parental prostate cancer cells that were transfected either with control retroviruses ( PBP ), or with retroviruses overexpressing PBP-H-RAS ( RAS ) or PBP-ERBB2 ( ERBB2 ). Actin was used as a loading control. Numbers in white represent protein levels in fold changes relative to those in PBP control cells after the actin normalization.

    Article Snippet: Cell signaling pathways activated by the ERBB2 oncogene or the RAS oncogene are frequently found to be altered in metastatic prostate cancers.

    Techniques: Western Blot, Transfection

    Lapatinib treatment inhibits AKT signaling in HPV-positive cells. Notes: Cells were treated with lapatinib (1 μM) or DMSO (vehicle control) 16 hours after plating. After 24-hour treatment, protein extraction was performed. The phosphorylation and levels of EGFR (Tyr1068), HER2 (Tyr1221/1222), and AKT (Ser473) were analyzed by Western blotting of HPV-positive ( A ) and HPV-negative cell lines ( B ). Beta-actin immunoblotting was used as a loading control. A representative picture of three independent experiments is shown. Quantification of AKT and pAKT was performed by densitometric analysis, and the mean ratio of pAKT/AKT from three independent experiments is depicted in the right panels. *** P ,0.001, paired t -test. Abbreviations: HPV, human papillomavirus; DMSO, dimethylsulfoxide.

    Journal: OncoTargets and therapy

    Article Title: Cytotoxic effect of lapatinib is restricted to human papillomavirus-positive head and neck squamous cell carcinoma cell lines

    doi: 10.2147/OTT.S68235

    Figure Lengend Snippet: Lapatinib treatment inhibits AKT signaling in HPV-positive cells. Notes: Cells were treated with lapatinib (1 μM) or DMSO (vehicle control) 16 hours after plating. After 24-hour treatment, protein extraction was performed. The phosphorylation and levels of EGFR (Tyr1068), HER2 (Tyr1221/1222), and AKT (Ser473) were analyzed by Western blotting of HPV-positive ( A ) and HPV-negative cell lines ( B ). Beta-actin immunoblotting was used as a loading control. A representative picture of three independent experiments is shown. Quantification of AKT and pAKT was performed by densitometric analysis, and the mean ratio of pAKT/AKT from three independent experiments is depicted in the right panels. *** P ,0.001, paired t -test. Abbreviations: HPV, human papillomavirus; DMSO, dimethylsulfoxide.

    Article Snippet: pHER2 , Cell Signaling Technology , #2249 , Phospho-HER2 (Tyr 1221/1222).

    Techniques: Protein Extraction, Western Blot

    List of antibodies

    Journal: OncoTargets and therapy

    Article Title: Cytotoxic effect of lapatinib is restricted to human papillomavirus-positive head and neck squamous cell carcinoma cell lines

    doi: 10.2147/OTT.S68235

    Figure Lengend Snippet: List of antibodies

    Article Snippet: pHER2 , Cell Signaling Technology , #2249 , Phospho-HER2 (Tyr 1221/1222).

    Techniques: