Name: human phospho-erbb2/her2 (y1248) antibody
Brand: Bio-Techne corporation
Rating: 94 (13 reviews)

human phospho-erbb2/her2 (y1248) antibody (Bio-Techne corporation)

Bio-Techne corporation human phospho-erbb2/her2 (y1248) antibody
Human Phospho Erbb2/Her2 (Y1248) Antibody, supplied by Bio-Techne corporation, 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/human phospho-erbb2/her2 (y1248) antibody/product/Bio-Techne corporation
Average 94 stars, based on 1 article reviews

human phospho-erbb2/her2 (y1248) antibody - by Bioz Stars, 2026-02

94/100 stars

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antibodies against pher2 (y1248) (GenScript corporation)

GenScript corporation antibodies against pher2 (y1248)
$CXCL12/CXCR4 transactivation of growth factor receptors occurs in lipid raft microdomains. a C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Total cell lysates were analyzed for phosphorylated and total HER2 and EGFR. b C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Cell lysates were immunoprecipated with anti-HER2 and EGFR antibodies and immunoblotted with total and <t>phosphorylated</t> <t>HER2</t> and EGFR antibodies. c C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Lipid raft membrane microdomains were isolated using a successive detergent solubilization method; both lipid rafts and cellular membranes and cytosol fractions were immunoblotted with phosphorylated and native HER2 and EGFR antibodies. d PC3 cells were lysed in a detergent-free lysis buffer and fractionated by sucrose density gradient centrifugation. Fractions were immunoblotted with lipid raft marker Flotillin-2 and cytosol marker β-Tubulin. The lipid raft enriched fraction (#5) was immunoblotted with HER2 and phosphorylated HER2 antibodies$
Antibodies Against Pher2 (Y1248), supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/antibodies against pher2 (y1248)/product/GenScript corporation
Average 90 stars, based on 1 article reviews

antibodies against pher2 (y1248) - by Bioz Stars, 2026-02

90/100 stars

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$CXCL12/CXCR4 transactivation of growth factor receptors occurs in lipid raft microdomains. a C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Total cell lysates were analyzed for phosphorylated and total HER2 and EGFR. b C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Cell lysates were immunoprecipated with anti-HER2 and EGFR antibodies and immunoblotted with total and phosphorylated HER2 and EGFR antibodies. c C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Lipid raft membrane microdomains were isolated using a successive detergent solubilization method; both lipid rafts and cellular membranes and cytosol fractions were immunoblotted with phosphorylated and native HER2 and EGFR antibodies. d PC3 cells were lysed in a detergent-free lysis buffer and fractionated by sucrose density gradient centrifugation. Fractions were immunoblotted with lipid raft marker Flotillin-2 and cytosol marker β-Tubulin. The lipid raft enriched fraction (#5) was immunoblotted with HER2 and phosphorylated HER2 antibodies$

Journal: Molecular Cancer

Article Title: Pharmacological targeting of CXCL12/CXCR4 signaling in prostate cancer bone metastasis

doi: 10.1186/s12943-016-0552-0

Figure Lengend Snippet: CXCL12/CXCR4 transactivation of growth factor receptors occurs in lipid raft microdomains. a C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Total cell lysates were analyzed for phosphorylated and total HER2 and EGFR. b C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Cell lysates were immunoprecipated with anti-HER2 and EGFR antibodies and immunoblotted with total and phosphorylated HER2 and EGFR antibodies. c C4-2B and PC3 cells were cultured in the presence or absence of CXCL12. Lipid raft membrane microdomains were isolated using a successive detergent solubilization method; both lipid rafts and cellular membranes and cytosol fractions were immunoblotted with phosphorylated and native HER2 and EGFR antibodies. d PC3 cells were lysed in a detergent-free lysis buffer and fractionated by sucrose density gradient centrifugation. Fractions were immunoblotted with lipid raft marker Flotillin-2 and cytosol marker β-Tubulin. The lipid raft enriched fraction (#5) was immunoblotted with HER2 and phosphorylated HER2 antibodies

Article Snippet: Immunoblot was performed with antibodies against pHER2 (Y1248) (Catalog # A00318-100, GenScript, Piscataway, NJ), total HER2 (Catalog #, SC-284, Santa Cruz Biotechnology, Dallas, TX) pEGFR (Y1173) (Catalog # 4407 s, Cell Signaling, Beverly, MA), total EGFR (Catalog # 4267 s, Cell Signaling, Beverly, MA), Flotillin (Catalog # 610383, BD Biosciences, San Jose, CA), β-tubulin (Catalog # SC-5274, Santa Cruz Biotechnology, Dallas, TX), pSrc (Catalog # 2101 s, Cell Signaling Technologies, Beverly, MA), total Src (Catalog # 2109 s, Cell Signaling Technologies, Beverly, MA), G αi2 (Catalog # SC-7276, Santa Cruz Biotechnology, Dallas, TX), pAkt (S473) (Catalog # 9271 s, Cell Signaling, Beverly, MA), Akt (Catalog # 2938 s, Cell Signaling, Beverly, MA), and GAPDH (Catalog #SC-25778, Santa Cruz Biotechnology, Santa Cruz, CA).

Techniques: Cell Culture, Membrane, Isolation, Lysis, Gradient Centrifugation, Marker

$CXCL12 activation of HER2 and Src is mediated by G αi GTP proteins in lipid raft membrane microdomains and this activation induces cell invasion. a C4-2B cells were cultured in the presence or absence of increasing concentrations of pertussis toxin (PTX) for 3 h, followed by treatment with CXCL12 for 15 min. Cell lysate was collected, and protein expression of phosphorylated and total HER2 and Src was determined by Western blot analysis. Flotillin was utilized as a loading control for the lipid raft fraction; β-Tubulin was utilized as a control for the membranes and cytosol fractions. Bottom panel shows the quantitation of phosphorylated HER2 and Src. b C4-2B cells were transfected with wild type G αi (WT-Gαi2), constitutively active G αi (Q205L), or plasmid control (pcDNA3.1). Cells were then cultured in the presence or absence of CXCL12 for 15 min, and cell lysate was collected. Protein expression of phosphorylated and total HER2 and Src as well as G αi 2 were determined by Western blot analysis. c C4-2B cells were transfected with plasmid control or constitutively active G αi (Q205L) and cultured in the presence or absence of CXCL12. Lipid raft fractions were collected and immunoblotted with phospho HER2 and Src antibodies. d C4-2B cells were either treated or not, with PTX (200 ng/ml) and a chemoinvasion assay was performed in the presence or absence of 200 ng/ml CXCL12. e C4-2B cells were transfected with pcDNA3.1 or pcDNA3.1 G αi 2 Q205L plasmids and a chemoinvasion assay was performed in the presence or absence of 200 ng/ml CXCL12. Bottom panels show the quantitation of invaded cells. Experiment was performed in triplicates; a representative field of invading cells are shown ( d and e ). Number of invading cells was quantitated in three independent experiments and statistical analyses were performed using ANOVA; significance was calculated using Tukey Posttest analysis using GraphPad Prism software. P value <0.05 is shown as a *$

Journal: Molecular Cancer

Article Title: Pharmacological targeting of CXCL12/CXCR4 signaling in prostate cancer bone metastasis

doi: 10.1186/s12943-016-0552-0

Figure Lengend Snippet: CXCL12 activation of HER2 and Src is mediated by G αi GTP proteins in lipid raft membrane microdomains and this activation induces cell invasion. a C4-2B cells were cultured in the presence or absence of increasing concentrations of pertussis toxin (PTX) for 3 h, followed by treatment with CXCL12 for 15 min. Cell lysate was collected, and protein expression of phosphorylated and total HER2 and Src was determined by Western blot analysis. Flotillin was utilized as a loading control for the lipid raft fraction; β-Tubulin was utilized as a control for the membranes and cytosol fractions. Bottom panel shows the quantitation of phosphorylated HER2 and Src. b C4-2B cells were transfected with wild type G αi (WT-Gαi2), constitutively active G αi (Q205L), or plasmid control (pcDNA3.1). Cells were then cultured in the presence or absence of CXCL12 for 15 min, and cell lysate was collected. Protein expression of phosphorylated and total HER2 and Src as well as G αi 2 were determined by Western blot analysis. c C4-2B cells were transfected with plasmid control or constitutively active G αi (Q205L) and cultured in the presence or absence of CXCL12. Lipid raft fractions were collected and immunoblotted with phospho HER2 and Src antibodies. d C4-2B cells were either treated or not, with PTX (200 ng/ml) and a chemoinvasion assay was performed in the presence or absence of 200 ng/ml CXCL12. e C4-2B cells were transfected with pcDNA3.1 or pcDNA3.1 G αi 2 Q205L plasmids and a chemoinvasion assay was performed in the presence or absence of 200 ng/ml CXCL12. Bottom panels show the quantitation of invaded cells. Experiment was performed in triplicates; a representative field of invading cells are shown ( d and e ). Number of invading cells was quantitated in three independent experiments and statistical analyses were performed using ANOVA; significance was calculated using Tukey Posttest analysis using GraphPad Prism software. P value <0.05 is shown as a *

Techniques: Activation Assay, Membrane, Cell Culture, Expressing, Western Blot, Control, Quantitation Assay, Transfection, Plasmid Preparation, Software

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