rabbit anti-human primary anti cdk2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti-human primary anti cdk2
    Rabbit Anti Human Primary Anti Cdk2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit anti-human primary anti cdk2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti-human primary anti cdk2
    Rabbit Anti Human Primary Anti Cdk2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cdk2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cdk2
    Cdk2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho cdk2 thr160 antibodies  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho cdk2 thr160 antibodies
    ( A ) Dose-dependent inhibition of Cdk7 kinase activity abolishes <t>Cdk2</t> phosphorylation in vivo . Asynchronous HCT116-Cdk7 +/+ and HCT116-Cdk7 as/as cells were incubated 14 h with the indicated concentrations of 1-NMPP1, and the cell lysates were analyzed by Western blotting using anti-phospho-Cdk2 <t>(P-Thr160)</t> antibody. The cellular protein lamin B serves as a loading control. ( B and C ) CAK inhibition does not affect the removal of CPD and 6-4PP from the genome. HCT116-Cdk7 as/as cells were starved in serum-free medium overnight and the cells were pretreated with 1-NMPP1 (10 µM) or DMSO (vehicle) for 14 h. The cells were then UV-irradiated with 20 J/m 2 and allowed to repair DNA in fresh medium with similar composition to the pretreatment for the indicated times. Identical amounts of genomic DNA were subjected to immuoslot-blot analysis of CPD and 6-4PP using the corresponding antibodies. The quantitative data presented in the graph indicate mean ± S.E. of the remaining CPD or 6-4PP from three independent experiments.
    Phospho Cdk2 Thr160 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Dissociation of CAK from Core TFIIH Reveals a Functional Link between XP-G/CS and the TFIIH Disassembly State"

    Article Title: Dissociation of CAK from Core TFIIH Reveals a Functional Link between XP-G/CS and the TFIIH Disassembly State

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0011007

    ( A ) Dose-dependent inhibition of Cdk7 kinase activity abolishes Cdk2 phosphorylation in vivo . Asynchronous HCT116-Cdk7 +/+ and HCT116-Cdk7 as/as cells were incubated 14 h with the indicated concentrations of 1-NMPP1, and the cell lysates were analyzed by Western blotting using anti-phospho-Cdk2 (P-Thr160) antibody. The cellular protein lamin B serves as a loading control. ( B and C ) CAK inhibition does not affect the removal of CPD and 6-4PP from the genome. HCT116-Cdk7 as/as cells were starved in serum-free medium overnight and the cells were pretreated with 1-NMPP1 (10 µM) or DMSO (vehicle) for 14 h. The cells were then UV-irradiated with 20 J/m 2 and allowed to repair DNA in fresh medium with similar composition to the pretreatment for the indicated times. Identical amounts of genomic DNA were subjected to immuoslot-blot analysis of CPD and 6-4PP using the corresponding antibodies. The quantitative data presented in the graph indicate mean ± S.E. of the remaining CPD or 6-4PP from three independent experiments.
    Figure Legend Snippet: ( A ) Dose-dependent inhibition of Cdk7 kinase activity abolishes Cdk2 phosphorylation in vivo . Asynchronous HCT116-Cdk7 +/+ and HCT116-Cdk7 as/as cells were incubated 14 h with the indicated concentrations of 1-NMPP1, and the cell lysates were analyzed by Western blotting using anti-phospho-Cdk2 (P-Thr160) antibody. The cellular protein lamin B serves as a loading control. ( B and C ) CAK inhibition does not affect the removal of CPD and 6-4PP from the genome. HCT116-Cdk7 as/as cells were starved in serum-free medium overnight and the cells were pretreated with 1-NMPP1 (10 µM) or DMSO (vehicle) for 14 h. The cells were then UV-irradiated with 20 J/m 2 and allowed to repair DNA in fresh medium with similar composition to the pretreatment for the indicated times. Identical amounts of genomic DNA were subjected to immuoslot-blot analysis of CPD and 6-4PP using the corresponding antibodies. The quantitative data presented in the graph indicate mean ± S.E. of the remaining CPD or 6-4PP from three independent experiments.

    Techniques Used: Inhibition, Activity Assay, In Vivo, Incubation, Western Blot, Irradiation

    phospho cdk2 thr160  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho cdk2 thr160
    Protein expression of AR, Skp2, <t>Cdk2,</t> phospho-Cdk2 Tyr15, phospho-Cdk2 Thr14, phospho-Cdk2 <t>Thr160,</t> Cdk7, cyclin E, cyclinA, cyclin H, p21 cip , p27 Kip , c-Myc, and E2F-1 was determined by Western blotting assay in LNCaP 104-R1, PC-3 LNCX-2 , PC-3 AR , and PC-3 LNCaP-AR cells treated with different concentration of R1881 for 96 h. Protein abundance of α-tubulin was used as loading control.
    Phospho Cdk2 Thr160, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Androgen Suppresses the Proliferation of Androgen Receptor-Positive Castration-Resistant Prostate Cancer Cells via Inhibition of Cdk2, CyclinA, and Skp2"

    Article Title: Androgen Suppresses the Proliferation of Androgen Receptor-Positive Castration-Resistant Prostate Cancer Cells via Inhibition of Cdk2, CyclinA, and Skp2

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0109170

    Protein expression of AR, Skp2, Cdk2, phospho-Cdk2 Tyr15, phospho-Cdk2 Thr14, phospho-Cdk2 Thr160, Cdk7, cyclin E, cyclinA, cyclin H, p21 cip , p27 Kip , c-Myc, and E2F-1 was determined by Western blotting assay in LNCaP 104-R1, PC-3 LNCX-2 , PC-3 AR , and PC-3 LNCaP-AR cells treated with different concentration of R1881 for 96 h. Protein abundance of α-tubulin was used as loading control.
    Figure Legend Snippet: Protein expression of AR, Skp2, Cdk2, phospho-Cdk2 Tyr15, phospho-Cdk2 Thr14, phospho-Cdk2 Thr160, Cdk7, cyclin E, cyclinA, cyclin H, p21 cip , p27 Kip , c-Myc, and E2F-1 was determined by Western blotting assay in LNCaP 104-R1, PC-3 LNCX-2 , PC-3 AR , and PC-3 LNCaP-AR cells treated with different concentration of R1881 for 96 h. Protein abundance of α-tubulin was used as loading control.

    Techniques Used: Expressing, Western Blot, Concentration Assay

    (A) Gene expression of CDKN1B was determined in LNCaP 104-R1 cells treated with 0, 0.1, or 10 nM R1881 for 96 h using qRT-PCR. LNCaP 104-R1 cells treated with 10 n m R1881 in the presence or absence of 5 µ m anti-androgen Casodex for 96 h. Asterisk * denotes significant difference p <0.05 of the treated cells as compared to control cells. (B) Relative cell number was determined by fluorometric DNA assay. (C) Percentage of cell population in S phase was determined by flow cytometry analysis. Asterisk * denotes a significant difference ( p <0.05) of the treated cells as compared to control cells. (D) Histone H1 phosphorylation was assayed using Cdk2 immunoprecipitated from cell lysate containing 2 mg protein. Relative radioactivity was determined by scanning with a Storm 860 phosphoimager (Molecular Dynamics, Sunnyvale, CA, U.S.A.). Protein expression level of Cdk2, p27 Kip1 , and β-actin were determined by Western blotting from the same cell lysates. Abundance of β-actin protein was used as loading control.
    Figure Legend Snippet: (A) Gene expression of CDKN1B was determined in LNCaP 104-R1 cells treated with 0, 0.1, or 10 nM R1881 for 96 h using qRT-PCR. LNCaP 104-R1 cells treated with 10 n m R1881 in the presence or absence of 5 µ m anti-androgen Casodex for 96 h. Asterisk * denotes significant difference p <0.05 of the treated cells as compared to control cells. (B) Relative cell number was determined by fluorometric DNA assay. (C) Percentage of cell population in S phase was determined by flow cytometry analysis. Asterisk * denotes a significant difference ( p <0.05) of the treated cells as compared to control cells. (D) Histone H1 phosphorylation was assayed using Cdk2 immunoprecipitated from cell lysate containing 2 mg protein. Relative radioactivity was determined by scanning with a Storm 860 phosphoimager (Molecular Dynamics, Sunnyvale, CA, U.S.A.). Protein expression level of Cdk2, p27 Kip1 , and β-actin were determined by Western blotting from the same cell lysates. Abundance of β-actin protein was used as loading control.

    Techniques Used: Expressing, Quantitative RT-PCR, Flow Cytometry, Immunoprecipitation, Radioactivity, Western Blot

    (A) Protein expression level of Skp2 and p27 Kip1 in LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 was determined by Western blotting. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Cdk2 activity was measured by in vitro phosphorylation of histone H1 using Cdk2 immunoprecipitates. Abundance of β-actin protein was used as loading control. (B) Cell proliferation of LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 treated with or without 10 nM R1881 for 96 hours was determined using the fluorometric DNA assay and was normalized to the cell number of control group (no treatment). (C) Percentage of LNCaP 104-R1 cells in S phase was determined by flow cytometry. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Asterisk denotes a significant difference ( p <0.05) from control cells. (D) LNCaP 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Fusion proteins of control GST (lanes 1–3) and bacterially-expressed GST-Skp2 (lanes 4–6) bound to glutathione-agarose beads was incubated with 200 µg whole cell lysates from untreated and androgen-treated 104-R1 cells in the presence of 10 µCi [ 32 P]-ATP for 30 min at room temperature. “nl” represents as no lysate. Phosphorylated proteins were eluted in Laemmli gel loading buffer and separated on a 10% SDS-PAGE gel that was then dried and exposed to Kodak X OMAT AR film for 3 days. (E) 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Phosphorylation of eluted GST (lanes 1–3) and GST-Skp2 (lanes 4–6) fusion proteins was determined by immunoprecipitated Cdk2. Cdk2 was immunoprecipitated from aliquots of lysate containing 1 mg protein prepared from untreated (lanes 2, 5 and 8) or R1881-treated (lanes 3, 6 and 9) 104-R1 cells. Control lanes (lanes 1, 4, and 7) labeled “ni” indicated no immunoprecipitated Cdk2. Cdk2 activity was determined by methods described in .
    Figure Legend Snippet: (A) Protein expression level of Skp2 and p27 Kip1 in LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 was determined by Western blotting. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Cdk2 activity was measured by in vitro phosphorylation of histone H1 using Cdk2 immunoprecipitates. Abundance of β-actin protein was used as loading control. (B) Cell proliferation of LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 treated with or without 10 nM R1881 for 96 hours was determined using the fluorometric DNA assay and was normalized to the cell number of control group (no treatment). (C) Percentage of LNCaP 104-R1 cells in S phase was determined by flow cytometry. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Asterisk denotes a significant difference ( p <0.05) from control cells. (D) LNCaP 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Fusion proteins of control GST (lanes 1–3) and bacterially-expressed GST-Skp2 (lanes 4–6) bound to glutathione-agarose beads was incubated with 200 µg whole cell lysates from untreated and androgen-treated 104-R1 cells in the presence of 10 µCi [ 32 P]-ATP for 30 min at room temperature. “nl” represents as no lysate. Phosphorylated proteins were eluted in Laemmli gel loading buffer and separated on a 10% SDS-PAGE gel that was then dried and exposed to Kodak X OMAT AR film for 3 days. (E) 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Phosphorylation of eluted GST (lanes 1–3) and GST-Skp2 (lanes 4–6) fusion proteins was determined by immunoprecipitated Cdk2. Cdk2 was immunoprecipitated from aliquots of lysate containing 1 mg protein prepared from untreated (lanes 2, 5 and 8) or R1881-treated (lanes 3, 6 and 9) 104-R1 cells. Control lanes (lanes 1, 4, and 7) labeled “ni” indicated no immunoprecipitated Cdk2. Cdk2 activity was determined by methods described in .

    Techniques Used: Expressing, Infection, Western Blot, Activity Assay, In Vitro, Flow Cytometry, Incubation, SDS Page, Immunoprecipitation, Labeling

    Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for CCNA2, CDK2, and SKP2 were 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1943_at, 1792_at, and 39449_at in Singh prostate dataset.
    Figure Legend Snippet: Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for CCNA2, CDK2, and SKP2 were 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1943_at, 1792_at, and 39449_at in Singh prostate dataset.

    Techniques Used:

    Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for Cdk7, CCNA2, CDK2, and SKP2 were 1969_s_at, 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1969_s_at, 1943_at, 1792_at, and 39449_at in Singh prostate dataset.
    Figure Legend Snippet: Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for Cdk7, CCNA2, CDK2, and SKP2 were 1969_s_at, 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1969_s_at, 1943_at, 1792_at, and 39449_at in Singh prostate dataset.

    Techniques Used:

    cdk2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cdk2
    The cells were treated with either vehicle (0.1% DMSO in medium) or GSPs (20, 40, 60 and 80 µg/mL) for 48 h and thereafter harvested, cell lysates prepared and then subjected to SDS-PAGE followed by Western blot analysis, as described in . Effect of GSPs was determined on the following: ( A ) the expression of cyclin D1, cyclin D2 and cyclin E, and the expression levels of <t>Cdk2,</t> Cdk4 and Cdk6; and ( B ) the expression of Kip1/p27 and Cip1/p21. β-actin was used to verify equal loading of the samples. Representative blots are shown from three independent experiments with almost identical results. ( C ) In binding assay, Cip1/p21 and Kip1/p27 were immunoprecipitated using specific antibody from total protein lysates followed by SDS-PAGE and western blot analysis for Cdk2, Cdk4 and Ckd6 as detailed in . IP, immunoprecipitation; IB, immunoblotting.
    Cdk2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Grape Proanthocyanidins Induce Apoptosis by Loss of Mitochondrial Membrane Potential of Human Non-Small Cell Lung Cancer Cells In Vitro and In Vivo"

    Article Title: Grape Proanthocyanidins Induce Apoptosis by Loss of Mitochondrial Membrane Potential of Human Non-Small Cell Lung Cancer Cells In Vitro and In Vivo

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0027444

    The cells were treated with either vehicle (0.1% DMSO in medium) or GSPs (20, 40, 60 and 80 µg/mL) for 48 h and thereafter harvested, cell lysates prepared and then subjected to SDS-PAGE followed by Western blot analysis, as described in . Effect of GSPs was determined on the following: ( A ) the expression of cyclin D1, cyclin D2 and cyclin E, and the expression levels of Cdk2, Cdk4 and Cdk6; and ( B ) the expression of Kip1/p27 and Cip1/p21. β-actin was used to verify equal loading of the samples. Representative blots are shown from three independent experiments with almost identical results. ( C ) In binding assay, Cip1/p21 and Kip1/p27 were immunoprecipitated using specific antibody from total protein lysates followed by SDS-PAGE and western blot analysis for Cdk2, Cdk4 and Ckd6 as detailed in . IP, immunoprecipitation; IB, immunoblotting.
    Figure Legend Snippet: The cells were treated with either vehicle (0.1% DMSO in medium) or GSPs (20, 40, 60 and 80 µg/mL) for 48 h and thereafter harvested, cell lysates prepared and then subjected to SDS-PAGE followed by Western blot analysis, as described in . Effect of GSPs was determined on the following: ( A ) the expression of cyclin D1, cyclin D2 and cyclin E, and the expression levels of Cdk2, Cdk4 and Cdk6; and ( B ) the expression of Kip1/p27 and Cip1/p21. β-actin was used to verify equal loading of the samples. Representative blots are shown from three independent experiments with almost identical results. ( C ) In binding assay, Cip1/p21 and Kip1/p27 were immunoprecipitated using specific antibody from total protein lysates followed by SDS-PAGE and western blot analysis for Cdk2, Cdk4 and Ckd6 as detailed in . IP, immunoprecipitation; IB, immunoblotting.

    Techniques Used: SDS Page, Western Blot, Expressing, Binding Assay, Immunoprecipitation

    The A549 tumor xenograft tissues were harvested at the termination of the experiment, and tumor lysates were subjected to the analyses of cell cycle proteins of G1 phase using Western blot analysis, as described in . Effect of GSPs was determined on the following: ( A ) the expression of cyclin D1, cyclin D2 and cyclin E, and the expression levels of Cdk2, Cdk4 and Cdk6; and ( B ) the expression of Cdk inhibitory proteins, Kip1/p27 and Cip1/p21. β-actin was used to verify equal loading of the samples. Representative blots are presented from the independent experiments from at least six tumors from six different mice per group with identical expression levels of proteins.
    Figure Legend Snippet: The A549 tumor xenograft tissues were harvested at the termination of the experiment, and tumor lysates were subjected to the analyses of cell cycle proteins of G1 phase using Western blot analysis, as described in . Effect of GSPs was determined on the following: ( A ) the expression of cyclin D1, cyclin D2 and cyclin E, and the expression levels of Cdk2, Cdk4 and Cdk6; and ( B ) the expression of Cdk inhibitory proteins, Kip1/p27 and Cip1/p21. β-actin was used to verify equal loading of the samples. Representative blots are presented from the independent experiments from at least six tumors from six different mice per group with identical expression levels of proteins.

    Techniques Used: Western Blot, Expressing

    phospho cdk2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho cdk2
    Cancer cells harbouring CCNE1 gene amplification show increased sensitivity to <t>CDK2</t> silencing and chemical inhibition . (A) The fraction of cells in each phase of the cell cycle are shown following transfection with CCNE1 short interfering RNA (siRNA) and control (siCON) in cell lines with (HCC1569 and MDA-MB-157) and without (MDA-MB-231, ZR75.1, BT474 and JIMT1) CCNE1 amplification. (B) Bar plots illustrating the survival fraction of cells following transfection with CDK2 siRNA using individual duplex oligonucelotides (1 to 4) and a SMARTpool (SP) in cancer cells harbouring (red) or lacking (black) 19q12 amplification. Error bars represent the standard error of the mean of three replicates. Survival fractions are shown relative to those of siCON transfected cells. (* depicts significant t-test P values for the comparison of the survival fraction between cells with and without amplification of the target gene for an individual oligonucleotide). (C) Effects on <t>CDK2</t> <t>protein</t> expression of CDK2 siRNA silencing with Dharmacon individual oligonucelotides and SMARTpool (SP) in MDA-MB-157 cells. (D) Dose response curves of breast cancer cell lines with (red) or without (black) 19q12 amplification to the CDK1, CDK2, and CDK9 inhibitor ADZ5438.
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    1) Product Images from "Functional characterization of the 19q12 amplicon in grade III breast cancers"

    Article Title: Functional characterization of the 19q12 amplicon in grade III breast cancers

    Journal: Breast Cancer Research : BCR

    doi: 10.1186/bcr3154

    Cancer cells harbouring CCNE1 gene amplification show increased sensitivity to CDK2 silencing and chemical inhibition . (A) The fraction of cells in each phase of the cell cycle are shown following transfection with CCNE1 short interfering RNA (siRNA) and control (siCON) in cell lines with (HCC1569 and MDA-MB-157) and without (MDA-MB-231, ZR75.1, BT474 and JIMT1) CCNE1 amplification. (B) Bar plots illustrating the survival fraction of cells following transfection with CDK2 siRNA using individual duplex oligonucelotides (1 to 4) and a SMARTpool (SP) in cancer cells harbouring (red) or lacking (black) 19q12 amplification. Error bars represent the standard error of the mean of three replicates. Survival fractions are shown relative to those of siCON transfected cells. (* depicts significant t-test P values for the comparison of the survival fraction between cells with and without amplification of the target gene for an individual oligonucleotide). (C) Effects on CDK2 protein expression of CDK2 siRNA silencing with Dharmacon individual oligonucelotides and SMARTpool (SP) in MDA-MB-157 cells. (D) Dose response curves of breast cancer cell lines with (red) or without (black) 19q12 amplification to the CDK1, CDK2, and CDK9 inhibitor ADZ5438.
    Figure Legend Snippet: Cancer cells harbouring CCNE1 gene amplification show increased sensitivity to CDK2 silencing and chemical inhibition . (A) The fraction of cells in each phase of the cell cycle are shown following transfection with CCNE1 short interfering RNA (siRNA) and control (siCON) in cell lines with (HCC1569 and MDA-MB-157) and without (MDA-MB-231, ZR75.1, BT474 and JIMT1) CCNE1 amplification. (B) Bar plots illustrating the survival fraction of cells following transfection with CDK2 siRNA using individual duplex oligonucelotides (1 to 4) and a SMARTpool (SP) in cancer cells harbouring (red) or lacking (black) 19q12 amplification. Error bars represent the standard error of the mean of three replicates. Survival fractions are shown relative to those of siCON transfected cells. (* depicts significant t-test P values for the comparison of the survival fraction between cells with and without amplification of the target gene for an individual oligonucleotide). (C) Effects on CDK2 protein expression of CDK2 siRNA silencing with Dharmacon individual oligonucelotides and SMARTpool (SP) in MDA-MB-157 cells. (D) Dose response curves of breast cancer cell lines with (red) or without (black) 19q12 amplification to the CDK1, CDK2, and CDK9 inhibitor ADZ5438.

    Techniques Used: Amplification, Inhibition, Transfection, Small Interfering RNA, Expressing

    phospho cdk2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho cdk2
    Effect of roscovitine on cell proliferation and survival of endocrine-resistant cancer cells . (a) Total cellular lysates from control and therapy-resistant model cells were subjected to western blotting using phosphor cell cycle dependent kinase (CDK) 2 antibody. Graph shows densitometry measurements of phosCDK2 protein bands relative to total <t>CDK2</t> in each cell line. (b) Model cells were treated with or without roscovitine and cell proliferation was determined at indicated time points by using the Cell Titer Glo assay. (c) Model cells were treated with or without roscovitine and clonogenic survival was determined. Representative figures and quantitative analysis of survival was shown. Statistical significance was determined by student's t-test. P, P value; * P < 0.05; ** P < 0.01. Con, control; Phos, phospho; ROS, roscovitine.
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    1) Product Images from "Roscovitine confers tumor suppressive effect on therapy-resistant breast tumor cells"

    Article Title: Roscovitine confers tumor suppressive effect on therapy-resistant breast tumor cells

    Journal: Breast Cancer Research : BCR

    doi: 10.1186/bcr2929

    Effect of roscovitine on cell proliferation and survival of endocrine-resistant cancer cells . (a) Total cellular lysates from control and therapy-resistant model cells were subjected to western blotting using phosphor cell cycle dependent kinase (CDK) 2 antibody. Graph shows densitometry measurements of phosCDK2 protein bands relative to total CDK2 in each cell line. (b) Model cells were treated with or without roscovitine and cell proliferation was determined at indicated time points by using the Cell Titer Glo assay. (c) Model cells were treated with or without roscovitine and clonogenic survival was determined. Representative figures and quantitative analysis of survival was shown. Statistical significance was determined by student's t-test. P, P value; * P < 0.05; ** P < 0.01. Con, control; Phos, phospho; ROS, roscovitine.
    Figure Legend Snippet: Effect of roscovitine on cell proliferation and survival of endocrine-resistant cancer cells . (a) Total cellular lysates from control and therapy-resistant model cells were subjected to western blotting using phosphor cell cycle dependent kinase (CDK) 2 antibody. Graph shows densitometry measurements of phosCDK2 protein bands relative to total CDK2 in each cell line. (b) Model cells were treated with or without roscovitine and cell proliferation was determined at indicated time points by using the Cell Titer Glo assay. (c) Model cells were treated with or without roscovitine and clonogenic survival was determined. Representative figures and quantitative analysis of survival was shown. Statistical significance was determined by student's t-test. P, P value; * P < 0.05; ** P < 0.01. Con, control; Phos, phospho; ROS, roscovitine.

    Techniques Used: Western Blot, Glo Assay

    rabbit anti phospho cdk2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti phospho cdk2
    ( A ) Frequency of cells in the G0/G1, S, and G2/M phases of the cell cycle in each anagliptin concentration group (n = 3). Huh-7 cells were incubated with DNA dye (Hoechst 33342). Plates containing the cells were scanned with ImageXpress Micro Screening System. Classification of cell phases was based on the fluorescence intensity of the DNA dye. For the cell number and cell cycle analyses, the intensity of the integrated DNA dye was assessed using the cell-cycle application module. ( B ) Expression of p21, p27kip1, pCDK2, and pRb of Huh-7 cells in each anagliptin concentration group (n = 4). Immunoblots for p21, p27kip1, <t>CDK2,</t> and pRb were performed using Huh-7 cell lysates. Amounts of protein were normalized to β-actin. ( C ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing low dose of anagliptin [ L-A ] [0.7 g/kg diet], and diet containing high dose of anagliptin [ H-A ] [2 g/kg diet]) (n = 5 for each group). * P < .05 vs L-A, ** P < .01 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( D ) Li-7 cell xenograft tumors and growth curves in mice at 21 days feeding in the same 3 groups as described in ( D ) (n = 5 for each group). * P < .05 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( E ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing high dose of anagliptin [2 g/kg diet], and diet containing high dose of vildagliptin [2 g/kg diet]) (n = 5 for each group). * P < .05, ** P < .01 vs anagliptin group, # P < .05, ## P < .01 vs vildagliptin group.
    Rabbit Anti Phospho Cdk2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Dipeptidyl Peptidase 4 Inhibitors Reduce Hepatocellular Carcinoma by Activating Lymphocyte Chemotaxis in Mice"

    Article Title: Dipeptidyl Peptidase 4 Inhibitors Reduce Hepatocellular Carcinoma by Activating Lymphocyte Chemotaxis in Mice

    Journal: Cellular and Molecular Gastroenterology and Hepatology

    doi: 10.1016/j.jcmgh.2018.08.008

    ( A ) Frequency of cells in the G0/G1, S, and G2/M phases of the cell cycle in each anagliptin concentration group (n = 3). Huh-7 cells were incubated with DNA dye (Hoechst 33342). Plates containing the cells were scanned with ImageXpress Micro Screening System. Classification of cell phases was based on the fluorescence intensity of the DNA dye. For the cell number and cell cycle analyses, the intensity of the integrated DNA dye was assessed using the cell-cycle application module. ( B ) Expression of p21, p27kip1, pCDK2, and pRb of Huh-7 cells in each anagliptin concentration group (n = 4). Immunoblots for p21, p27kip1, CDK2, and pRb were performed using Huh-7 cell lysates. Amounts of protein were normalized to β-actin. ( C ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing low dose of anagliptin [ L-A ] [0.7 g/kg diet], and diet containing high dose of anagliptin [ H-A ] [2 g/kg diet]) (n = 5 for each group). * P < .05 vs L-A, ** P < .01 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( D ) Li-7 cell xenograft tumors and growth curves in mice at 21 days feeding in the same 3 groups as described in ( D ) (n = 5 for each group). * P < .05 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( E ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing high dose of anagliptin [2 g/kg diet], and diet containing high dose of vildagliptin [2 g/kg diet]) (n = 5 for each group). * P < .05, ** P < .01 vs anagliptin group, # P < .05, ## P < .01 vs vildagliptin group.
    Figure Legend Snippet: ( A ) Frequency of cells in the G0/G1, S, and G2/M phases of the cell cycle in each anagliptin concentration group (n = 3). Huh-7 cells were incubated with DNA dye (Hoechst 33342). Plates containing the cells were scanned with ImageXpress Micro Screening System. Classification of cell phases was based on the fluorescence intensity of the DNA dye. For the cell number and cell cycle analyses, the intensity of the integrated DNA dye was assessed using the cell-cycle application module. ( B ) Expression of p21, p27kip1, pCDK2, and pRb of Huh-7 cells in each anagliptin concentration group (n = 4). Immunoblots for p21, p27kip1, CDK2, and pRb were performed using Huh-7 cell lysates. Amounts of protein were normalized to β-actin. ( C ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing low dose of anagliptin [ L-A ] [0.7 g/kg diet], and diet containing high dose of anagliptin [ H-A ] [2 g/kg diet]) (n = 5 for each group). * P < .05 vs L-A, ** P < .01 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( D ) Li-7 cell xenograft tumors and growth curves in mice at 21 days feeding in the same 3 groups as described in ( D ) (n = 5 for each group). * P < .05 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( E ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing high dose of anagliptin [2 g/kg diet], and diet containing high dose of vildagliptin [2 g/kg diet]) (n = 5 for each group). * P < .05, ** P < .01 vs anagliptin group, # P < .05, ## P < .01 vs vildagliptin group.

    Techniques Used: Concentration Assay, Incubation, Fluorescence, Expressing, Western Blot

    phospho cdk2 thr160  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho cdk2 thr160
    <t>CDK2</t> inactivation mediates cell cycle arrest by MYC depletion and is not selectively lethal to MYC-dependent breast cancer cells. (A) Cells were transfected with either pooled MYC siRNA (siMYC) or Non-targeting siRNA control (siCON) at 2 nM or 10 nM. Cell lysates were collected at 72 hour post-transfection and then subjected to Western blotting. β-ACTIN was used as loading control for whole-cell lysates. (B) Cells were transfected with either pooled CDK2 siRNA (siCDK2) or Non-targeting siRNA control (siCON) at 10 nM. 72 hours after transfection, cell proliferation was measured by BrdU incorporation. Data are mean ± SEM analysed in triplicate experiments. (C) A panel of 17 human breast cancer cell lines were treated with CDK2 inhibitor SNS-032 at a series of concentrations for 48 hours followed by measurement of BrdU incorporation. The correlation between sensitivity to MYC siRNA and SNS-032 was assessed. Sensitivity to MYC siRNA was determined by inhibition of BrdU incorporation at 10 nM MYC siRNA and sensitivity to SNS-032 determined by the IC 50 value for each cell line shown in Additional file : Table S2 and S3, respectively. R = Pearson correlation coefficient, P = the corresponding P -value.
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    1) Product Images from "Targeting cyclin-dependent kinase 1 (CDK1) but not CDK4/6 or CDK2 is selectively lethal to MYC-dependent human breast cancer cells"

    Article Title: Targeting cyclin-dependent kinase 1 (CDK1) but not CDK4/6 or CDK2 is selectively lethal to MYC-dependent human breast cancer cells

    Journal: BMC Cancer

    doi: 10.1186/1471-2407-14-32

    CDK2 inactivation mediates cell cycle arrest by MYC depletion and is not selectively lethal to MYC-dependent breast cancer cells. (A) Cells were transfected with either pooled MYC siRNA (siMYC) or Non-targeting siRNA control (siCON) at 2 nM or 10 nM. Cell lysates were collected at 72 hour post-transfection and then subjected to Western blotting. β-ACTIN was used as loading control for whole-cell lysates. (B) Cells were transfected with either pooled CDK2 siRNA (siCDK2) or Non-targeting siRNA control (siCON) at 10 nM. 72 hours after transfection, cell proliferation was measured by BrdU incorporation. Data are mean ± SEM analysed in triplicate experiments. (C) A panel of 17 human breast cancer cell lines were treated with CDK2 inhibitor SNS-032 at a series of concentrations for 48 hours followed by measurement of BrdU incorporation. The correlation between sensitivity to MYC siRNA and SNS-032 was assessed. Sensitivity to MYC siRNA was determined by inhibition of BrdU incorporation at 10 nM MYC siRNA and sensitivity to SNS-032 determined by the IC 50 value for each cell line shown in Additional file : Table S2 and S3, respectively. R = Pearson correlation coefficient, P = the corresponding P -value.
    Figure Legend Snippet: CDK2 inactivation mediates cell cycle arrest by MYC depletion and is not selectively lethal to MYC-dependent breast cancer cells. (A) Cells were transfected with either pooled MYC siRNA (siMYC) or Non-targeting siRNA control (siCON) at 2 nM or 10 nM. Cell lysates were collected at 72 hour post-transfection and then subjected to Western blotting. β-ACTIN was used as loading control for whole-cell lysates. (B) Cells were transfected with either pooled CDK2 siRNA (siCDK2) or Non-targeting siRNA control (siCON) at 10 nM. 72 hours after transfection, cell proliferation was measured by BrdU incorporation. Data are mean ± SEM analysed in triplicate experiments. (C) A panel of 17 human breast cancer cell lines were treated with CDK2 inhibitor SNS-032 at a series of concentrations for 48 hours followed by measurement of BrdU incorporation. The correlation between sensitivity to MYC siRNA and SNS-032 was assessed. Sensitivity to MYC siRNA was determined by inhibition of BrdU incorporation at 10 nM MYC siRNA and sensitivity to SNS-032 determined by the IC 50 value for each cell line shown in Additional file : Table S2 and S3, respectively. R = Pearson correlation coefficient, P = the corresponding P -value.

    Techniques Used: Transfection, Western Blot, BrdU Incorporation Assay, Inhibition

    cdk 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cdk 2
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    Cell Signaling Technology Inc rabbit anti-human primary anti cdk2
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    Cell Signaling Technology Inc phospho cdk2 thr160 antibodies
    ( A ) Dose-dependent inhibition of Cdk7 kinase activity abolishes <t>Cdk2</t> phosphorylation in vivo . Asynchronous HCT116-Cdk7 +/+ and HCT116-Cdk7 as/as cells were incubated 14 h with the indicated concentrations of 1-NMPP1, and the cell lysates were analyzed by Western blotting using anti-phospho-Cdk2 <t>(P-Thr160)</t> antibody. The cellular protein lamin B serves as a loading control. ( B and C ) CAK inhibition does not affect the removal of CPD and 6-4PP from the genome. HCT116-Cdk7 as/as cells were starved in serum-free medium overnight and the cells were pretreated with 1-NMPP1 (10 µM) or DMSO (vehicle) for 14 h. The cells were then UV-irradiated with 20 J/m 2 and allowed to repair DNA in fresh medium with similar composition to the pretreatment for the indicated times. Identical amounts of genomic DNA were subjected to immuoslot-blot analysis of CPD and 6-4PP using the corresponding antibodies. The quantitative data presented in the graph indicate mean ± S.E. of the remaining CPD or 6-4PP from three independent experiments.
    Phospho Cdk2 Thr160 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phospho cdk2 thr160
    Protein expression of AR, Skp2, <t>Cdk2,</t> phospho-Cdk2 Tyr15, phospho-Cdk2 Thr14, phospho-Cdk2 <t>Thr160,</t> Cdk7, cyclin E, cyclinA, cyclin H, p21 cip , p27 Kip , c-Myc, and E2F-1 was determined by Western blotting assay in LNCaP 104-R1, PC-3 LNCX-2 , PC-3 AR , and PC-3 LNCaP-AR cells treated with different concentration of R1881 for 96 h. Protein abundance of α-tubulin was used as loading control.
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    Cell Signaling Technology Inc phospho cdk2
    Cancer cells harbouring CCNE1 gene amplification show increased sensitivity to <t>CDK2</t> silencing and chemical inhibition . (A) The fraction of cells in each phase of the cell cycle are shown following transfection with CCNE1 short interfering RNA (siRNA) and control (siCON) in cell lines with (HCC1569 and MDA-MB-157) and without (MDA-MB-231, ZR75.1, BT474 and JIMT1) CCNE1 amplification. (B) Bar plots illustrating the survival fraction of cells following transfection with CDK2 siRNA using individual duplex oligonucelotides (1 to 4) and a SMARTpool (SP) in cancer cells harbouring (red) or lacking (black) 19q12 amplification. Error bars represent the standard error of the mean of three replicates. Survival fractions are shown relative to those of siCON transfected cells. (* depicts significant t-test P values for the comparison of the survival fraction between cells with and without amplification of the target gene for an individual oligonucleotide). (C) Effects on <t>CDK2</t> <t>protein</t> expression of CDK2 siRNA silencing with Dharmacon individual oligonucelotides and SMARTpool (SP) in MDA-MB-157 cells. (D) Dose response curves of breast cancer cell lines with (red) or without (black) 19q12 amplification to the CDK1, CDK2, and CDK9 inhibitor ADZ5438.
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    ( A ) Frequency of cells in the G0/G1, S, and G2/M phases of the cell cycle in each anagliptin concentration group (n = 3). Huh-7 cells were incubated with DNA dye (Hoechst 33342). Plates containing the cells were scanned with ImageXpress Micro Screening System. Classification of cell phases was based on the fluorescence intensity of the DNA dye. For the cell number and cell cycle analyses, the intensity of the integrated DNA dye was assessed using the cell-cycle application module. ( B ) Expression of p21, p27kip1, pCDK2, and pRb of Huh-7 cells in each anagliptin concentration group (n = 4). Immunoblots for p21, p27kip1, <t>CDK2,</t> and pRb were performed using Huh-7 cell lysates. Amounts of protein were normalized to β-actin. ( C ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing low dose of anagliptin [ L-A ] [0.7 g/kg diet], and diet containing high dose of anagliptin [ H-A ] [2 g/kg diet]) (n = 5 for each group). * P < .05 vs L-A, ** P < .01 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( D ) Li-7 cell xenograft tumors and growth curves in mice at 21 days feeding in the same 3 groups as described in ( D ) (n = 5 for each group). * P < .05 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( E ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing high dose of anagliptin [2 g/kg diet], and diet containing high dose of vildagliptin [2 g/kg diet]) (n = 5 for each group). * P < .05, ** P < .01 vs anagliptin group, # P < .05, ## P < .01 vs vildagliptin group.
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    Cell Signaling Technology Inc cdk 2
    ( A ) Frequency of cells in the G0/G1, S, and G2/M phases of the cell cycle in each anagliptin concentration group (n = 3). Huh-7 cells were incubated with DNA dye (Hoechst 33342). Plates containing the cells were scanned with ImageXpress Micro Screening System. Classification of cell phases was based on the fluorescence intensity of the DNA dye. For the cell number and cell cycle analyses, the intensity of the integrated DNA dye was assessed using the cell-cycle application module. ( B ) Expression of p21, p27kip1, pCDK2, and pRb of Huh-7 cells in each anagliptin concentration group (n = 4). Immunoblots for p21, p27kip1, <t>CDK2,</t> and pRb were performed using Huh-7 cell lysates. Amounts of protein were normalized to β-actin. ( C ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing low dose of anagliptin [ L-A ] [0.7 g/kg diet], and diet containing high dose of anagliptin [ H-A ] [2 g/kg diet]) (n = 5 for each group). * P < .05 vs L-A, ** P < .01 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( D ) Li-7 cell xenograft tumors and growth curves in mice at 21 days feeding in the same 3 groups as described in ( D ) (n = 5 for each group). * P < .05 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( E ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing high dose of anagliptin [2 g/kg diet], and diet containing high dose of vildagliptin [2 g/kg diet]) (n = 5 for each group). * P < .05, ** P < .01 vs anagliptin group, # P < .05, ## P < .01 vs vildagliptin group.
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    ( A ) Dose-dependent inhibition of Cdk7 kinase activity abolishes Cdk2 phosphorylation in vivo . Asynchronous HCT116-Cdk7 +/+ and HCT116-Cdk7 as/as cells were incubated 14 h with the indicated concentrations of 1-NMPP1, and the cell lysates were analyzed by Western blotting using anti-phospho-Cdk2 (P-Thr160) antibody. The cellular protein lamin B serves as a loading control. ( B and C ) CAK inhibition does not affect the removal of CPD and 6-4PP from the genome. HCT116-Cdk7 as/as cells were starved in serum-free medium overnight and the cells were pretreated with 1-NMPP1 (10 µM) or DMSO (vehicle) for 14 h. The cells were then UV-irradiated with 20 J/m 2 and allowed to repair DNA in fresh medium with similar composition to the pretreatment for the indicated times. Identical amounts of genomic DNA were subjected to immuoslot-blot analysis of CPD and 6-4PP using the corresponding antibodies. The quantitative data presented in the graph indicate mean ± S.E. of the remaining CPD or 6-4PP from three independent experiments.

    Journal: PLoS ONE

    Article Title: Dissociation of CAK from Core TFIIH Reveals a Functional Link between XP-G/CS and the TFIIH Disassembly State

    doi: 10.1371/journal.pone.0011007

    Figure Lengend Snippet: ( A ) Dose-dependent inhibition of Cdk7 kinase activity abolishes Cdk2 phosphorylation in vivo . Asynchronous HCT116-Cdk7 +/+ and HCT116-Cdk7 as/as cells were incubated 14 h with the indicated concentrations of 1-NMPP1, and the cell lysates were analyzed by Western blotting using anti-phospho-Cdk2 (P-Thr160) antibody. The cellular protein lamin B serves as a loading control. ( B and C ) CAK inhibition does not affect the removal of CPD and 6-4PP from the genome. HCT116-Cdk7 as/as cells were starved in serum-free medium overnight and the cells were pretreated with 1-NMPP1 (10 µM) or DMSO (vehicle) for 14 h. The cells were then UV-irradiated with 20 J/m 2 and allowed to repair DNA in fresh medium with similar composition to the pretreatment for the indicated times. Identical amounts of genomic DNA were subjected to immuoslot-blot analysis of CPD and 6-4PP using the corresponding antibodies. The quantitative data presented in the graph indicate mean ± S.E. of the remaining CPD or 6-4PP from three independent experiments.

    Article Snippet: Rabbit phospho-p53 (Ser15) and phospho-Cdk2 (Thr160) antibodies were from Cell Signaling Technology (Danvers, MA).

    Techniques: Inhibition, Activity Assay, In Vivo, Incubation, Western Blot, Irradiation

    Protein expression of AR, Skp2, Cdk2, phospho-Cdk2 Tyr15, phospho-Cdk2 Thr14, phospho-Cdk2 Thr160, Cdk7, cyclin E, cyclinA, cyclin H, p21 cip , p27 Kip , c-Myc, and E2F-1 was determined by Western blotting assay in LNCaP 104-R1, PC-3 LNCX-2 , PC-3 AR , and PC-3 LNCaP-AR cells treated with different concentration of R1881 for 96 h. Protein abundance of α-tubulin was used as loading control.

    Journal: PLoS ONE

    Article Title: Androgen Suppresses the Proliferation of Androgen Receptor-Positive Castration-Resistant Prostate Cancer Cells via Inhibition of Cdk2, CyclinA, and Skp2

    doi: 10.1371/journal.pone.0109170

    Figure Lengend Snippet: Protein expression of AR, Skp2, Cdk2, phospho-Cdk2 Tyr15, phospho-Cdk2 Thr14, phospho-Cdk2 Thr160, Cdk7, cyclin E, cyclinA, cyclin H, p21 cip , p27 Kip , c-Myc, and E2F-1 was determined by Western blotting assay in LNCaP 104-R1, PC-3 LNCX-2 , PC-3 AR , and PC-3 LNCaP-AR cells treated with different concentration of R1881 for 96 h. Protein abundance of α-tubulin was used as loading control.

    Article Snippet: Antibodies for cyclin E, Cdk2, and phospho-Cdk2 Thr160 were from Cell Signaling (Danvers, MA, U.S.A.).

    Techniques: Expressing, Western Blot, Concentration Assay

    (A) Gene expression of CDKN1B was determined in LNCaP 104-R1 cells treated with 0, 0.1, or 10 nM R1881 for 96 h using qRT-PCR. LNCaP 104-R1 cells treated with 10 n m R1881 in the presence or absence of 5 µ m anti-androgen Casodex for 96 h. Asterisk * denotes significant difference p <0.05 of the treated cells as compared to control cells. (B) Relative cell number was determined by fluorometric DNA assay. (C) Percentage of cell population in S phase was determined by flow cytometry analysis. Asterisk * denotes a significant difference ( p <0.05) of the treated cells as compared to control cells. (D) Histone H1 phosphorylation was assayed using Cdk2 immunoprecipitated from cell lysate containing 2 mg protein. Relative radioactivity was determined by scanning with a Storm 860 phosphoimager (Molecular Dynamics, Sunnyvale, CA, U.S.A.). Protein expression level of Cdk2, p27 Kip1 , and β-actin were determined by Western blotting from the same cell lysates. Abundance of β-actin protein was used as loading control.

    Journal: PLoS ONE

    Article Title: Androgen Suppresses the Proliferation of Androgen Receptor-Positive Castration-Resistant Prostate Cancer Cells via Inhibition of Cdk2, CyclinA, and Skp2

    doi: 10.1371/journal.pone.0109170

    Figure Lengend Snippet: (A) Gene expression of CDKN1B was determined in LNCaP 104-R1 cells treated with 0, 0.1, or 10 nM R1881 for 96 h using qRT-PCR. LNCaP 104-R1 cells treated with 10 n m R1881 in the presence or absence of 5 µ m anti-androgen Casodex for 96 h. Asterisk * denotes significant difference p <0.05 of the treated cells as compared to control cells. (B) Relative cell number was determined by fluorometric DNA assay. (C) Percentage of cell population in S phase was determined by flow cytometry analysis. Asterisk * denotes a significant difference ( p <0.05) of the treated cells as compared to control cells. (D) Histone H1 phosphorylation was assayed using Cdk2 immunoprecipitated from cell lysate containing 2 mg protein. Relative radioactivity was determined by scanning with a Storm 860 phosphoimager (Molecular Dynamics, Sunnyvale, CA, U.S.A.). Protein expression level of Cdk2, p27 Kip1 , and β-actin were determined by Western blotting from the same cell lysates. Abundance of β-actin protein was used as loading control.

    Article Snippet: Antibodies for cyclin E, Cdk2, and phospho-Cdk2 Thr160 were from Cell Signaling (Danvers, MA, U.S.A.).

    Techniques: Expressing, Quantitative RT-PCR, Flow Cytometry, Immunoprecipitation, Radioactivity, Western Blot

    (A) Protein expression level of Skp2 and p27 Kip1 in LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 was determined by Western blotting. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Cdk2 activity was measured by in vitro phosphorylation of histone H1 using Cdk2 immunoprecipitates. Abundance of β-actin protein was used as loading control. (B) Cell proliferation of LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 treated with or without 10 nM R1881 for 96 hours was determined using the fluorometric DNA assay and was normalized to the cell number of control group (no treatment). (C) Percentage of LNCaP 104-R1 cells in S phase was determined by flow cytometry. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Asterisk denotes a significant difference ( p <0.05) from control cells. (D) LNCaP 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Fusion proteins of control GST (lanes 1–3) and bacterially-expressed GST-Skp2 (lanes 4–6) bound to glutathione-agarose beads was incubated with 200 µg whole cell lysates from untreated and androgen-treated 104-R1 cells in the presence of 10 µCi [ 32 P]-ATP for 30 min at room temperature. “nl” represents as no lysate. Phosphorylated proteins were eluted in Laemmli gel loading buffer and separated on a 10% SDS-PAGE gel that was then dried and exposed to Kodak X OMAT AR film for 3 days. (E) 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Phosphorylation of eluted GST (lanes 1–3) and GST-Skp2 (lanes 4–6) fusion proteins was determined by immunoprecipitated Cdk2. Cdk2 was immunoprecipitated from aliquots of lysate containing 1 mg protein prepared from untreated (lanes 2, 5 and 8) or R1881-treated (lanes 3, 6 and 9) 104-R1 cells. Control lanes (lanes 1, 4, and 7) labeled “ni” indicated no immunoprecipitated Cdk2. Cdk2 activity was determined by methods described in .

    Journal: PLoS ONE

    Article Title: Androgen Suppresses the Proliferation of Androgen Receptor-Positive Castration-Resistant Prostate Cancer Cells via Inhibition of Cdk2, CyclinA, and Skp2

    doi: 10.1371/journal.pone.0109170

    Figure Lengend Snippet: (A) Protein expression level of Skp2 and p27 Kip1 in LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 was determined by Western blotting. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Cdk2 activity was measured by in vitro phosphorylation of histone H1 using Cdk2 immunoprecipitates. Abundance of β-actin protein was used as loading control. (B) Cell proliferation of LNCaP 104-R1 cells infected with pMV7 empty retrovirus (control) or pMV7 retrovirus containing Skp2 treated with or without 10 nM R1881 for 96 hours was determined using the fluorometric DNA assay and was normalized to the cell number of control group (no treatment). (C) Percentage of LNCaP 104-R1 cells in S phase was determined by flow cytometry. Cells were grown for 3 days in the presence or absence of 10 n m R1881. Asterisk denotes a significant difference ( p <0.05) from control cells. (D) LNCaP 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Fusion proteins of control GST (lanes 1–3) and bacterially-expressed GST-Skp2 (lanes 4–6) bound to glutathione-agarose beads was incubated with 200 µg whole cell lysates from untreated and androgen-treated 104-R1 cells in the presence of 10 µCi [ 32 P]-ATP for 30 min at room temperature. “nl” represents as no lysate. Phosphorylated proteins were eluted in Laemmli gel loading buffer and separated on a 10% SDS-PAGE gel that was then dried and exposed to Kodak X OMAT AR film for 3 days. (E) 104-R1 cells were treated with or without 10 nM R1881 for 3 days. Phosphorylation of eluted GST (lanes 1–3) and GST-Skp2 (lanes 4–6) fusion proteins was determined by immunoprecipitated Cdk2. Cdk2 was immunoprecipitated from aliquots of lysate containing 1 mg protein prepared from untreated (lanes 2, 5 and 8) or R1881-treated (lanes 3, 6 and 9) 104-R1 cells. Control lanes (lanes 1, 4, and 7) labeled “ni” indicated no immunoprecipitated Cdk2. Cdk2 activity was determined by methods described in .

    Article Snippet: Antibodies for cyclin E, Cdk2, and phospho-Cdk2 Thr160 were from Cell Signaling (Danvers, MA, U.S.A.).

    Techniques: Expressing, Infection, Western Blot, Activity Assay, In Vitro, Flow Cytometry, Incubation, SDS Page, Immunoprecipitation, Labeling

    Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for CCNA2, CDK2, and SKP2 were 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1943_at, 1792_at, and 39449_at in Singh prostate dataset.

    Journal: PLoS ONE

    Article Title: Androgen Suppresses the Proliferation of Androgen Receptor-Positive Castration-Resistant Prostate Cancer Cells via Inhibition of Cdk2, CyclinA, and Skp2

    doi: 10.1371/journal.pone.0109170

    Figure Lengend Snippet: Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for CCNA2, CDK2, and SKP2 were 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1943_at, 1792_at, and 39449_at in Singh prostate dataset.

    Article Snippet: Antibodies for cyclin E, Cdk2, and phospho-Cdk2 Thr160 were from Cell Signaling (Danvers, MA, U.S.A.).

    Techniques:

    Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for Cdk7, CCNA2, CDK2, and SKP2 were 1969_s_at, 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1969_s_at, 1943_at, 1792_at, and 39449_at in Singh prostate dataset.

    Journal: PLoS ONE

    Article Title: Androgen Suppresses the Proliferation of Androgen Receptor-Positive Castration-Resistant Prostate Cancer Cells via Inhibition of Cdk2, CyclinA, and Skp2

    doi: 10.1371/journal.pone.0109170

    Figure Lengend Snippet: Scatter plots showing correlation of indicated genes in GSE6919 (A) and Singh prostate datasets (B). The r value indicated correlation coefficient. Probe ID for Cdk7, CCNA2, CDK2, and SKP2 were 1969_s_at, 40697_at, 1792_g_at, and 1941_at in GSE6919, and 1969_s_at, 1943_at, 1792_at, and 39449_at in Singh prostate dataset.

    Article Snippet: Antibodies for cyclin E, Cdk2, and phospho-Cdk2 Thr160 were from Cell Signaling (Danvers, MA, U.S.A.).

    Techniques:

    Cancer cells harbouring CCNE1 gene amplification show increased sensitivity to CDK2 silencing and chemical inhibition . (A) The fraction of cells in each phase of the cell cycle are shown following transfection with CCNE1 short interfering RNA (siRNA) and control (siCON) in cell lines with (HCC1569 and MDA-MB-157) and without (MDA-MB-231, ZR75.1, BT474 and JIMT1) CCNE1 amplification. (B) Bar plots illustrating the survival fraction of cells following transfection with CDK2 siRNA using individual duplex oligonucelotides (1 to 4) and a SMARTpool (SP) in cancer cells harbouring (red) or lacking (black) 19q12 amplification. Error bars represent the standard error of the mean of three replicates. Survival fractions are shown relative to those of siCON transfected cells. (* depicts significant t-test P values for the comparison of the survival fraction between cells with and without amplification of the target gene for an individual oligonucleotide). (C) Effects on CDK2 protein expression of CDK2 siRNA silencing with Dharmacon individual oligonucelotides and SMARTpool (SP) in MDA-MB-157 cells. (D) Dose response curves of breast cancer cell lines with (red) or without (black) 19q12 amplification to the CDK1, CDK2, and CDK9 inhibitor ADZ5438.

    Journal: Breast Cancer Research : BCR

    Article Title: Functional characterization of the 19q12 amplicon in grade III breast cancers

    doi: 10.1186/bcr3154

    Figure Lengend Snippet: Cancer cells harbouring CCNE1 gene amplification show increased sensitivity to CDK2 silencing and chemical inhibition . (A) The fraction of cells in each phase of the cell cycle are shown following transfection with CCNE1 short interfering RNA (siRNA) and control (siCON) in cell lines with (HCC1569 and MDA-MB-157) and without (MDA-MB-231, ZR75.1, BT474 and JIMT1) CCNE1 amplification. (B) Bar plots illustrating the survival fraction of cells following transfection with CDK2 siRNA using individual duplex oligonucelotides (1 to 4) and a SMARTpool (SP) in cancer cells harbouring (red) or lacking (black) 19q12 amplification. Error bars represent the standard error of the mean of three replicates. Survival fractions are shown relative to those of siCON transfected cells. (* depicts significant t-test P values for the comparison of the survival fraction between cells with and without amplification of the target gene for an individual oligonucleotide). (C) Effects on CDK2 protein expression of CDK2 siRNA silencing with Dharmacon individual oligonucelotides and SMARTpool (SP) in MDA-MB-157 cells. (D) Dose response curves of breast cancer cell lines with (red) or without (black) 19q12 amplification to the CDK1, CDK2, and CDK9 inhibitor ADZ5438.

    Article Snippet: Total protein lysates (40 μg) from treated and untreated cells were separated by SDS-PAGE according to standard protocols, and immunoblotting was carried out using primary antibodies directed against CCNE1 (HE-12, Abcam ab3927, Cambridge, UK), CDK2 (2546, Cell Signaling Technology, Danvers, MA, USA), phospho-CDK2 (2561, Cell Signaling), PLEKHF1 (20389-1-AP, Proteintech, Chicago, IL, USA), POP4 (Rpp29, sc-23048, Santa Cruz Biotechnology, Santa Cruz, CA, USA), TSHZ3 (sc-134132, Santa Cruz), and CCNB1 (4135, Cell Signaling), and against β-tubulin as loading control (5346, Cell Signaling).

    Techniques: Amplification, Inhibition, Transfection, Small Interfering RNA, Expressing

    ( A ) Frequency of cells in the G0/G1, S, and G2/M phases of the cell cycle in each anagliptin concentration group (n = 3). Huh-7 cells were incubated with DNA dye (Hoechst 33342). Plates containing the cells were scanned with ImageXpress Micro Screening System. Classification of cell phases was based on the fluorescence intensity of the DNA dye. For the cell number and cell cycle analyses, the intensity of the integrated DNA dye was assessed using the cell-cycle application module. ( B ) Expression of p21, p27kip1, pCDK2, and pRb of Huh-7 cells in each anagliptin concentration group (n = 4). Immunoblots for p21, p27kip1, CDK2, and pRb were performed using Huh-7 cell lysates. Amounts of protein were normalized to β-actin. ( C ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing low dose of anagliptin [ L-A ] [0.7 g/kg diet], and diet containing high dose of anagliptin [ H-A ] [2 g/kg diet]) (n = 5 for each group). * P < .05 vs L-A, ** P < .01 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( D ) Li-7 cell xenograft tumors and growth curves in mice at 21 days feeding in the same 3 groups as described in ( D ) (n = 5 for each group). * P < .05 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( E ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing high dose of anagliptin [2 g/kg diet], and diet containing high dose of vildagliptin [2 g/kg diet]) (n = 5 for each group). * P < .05, ** P < .01 vs anagliptin group, # P < .05, ## P < .01 vs vildagliptin group.

    Journal: Cellular and Molecular Gastroenterology and Hepatology

    Article Title: Dipeptidyl Peptidase 4 Inhibitors Reduce Hepatocellular Carcinoma by Activating Lymphocyte Chemotaxis in Mice

    doi: 10.1016/j.jcmgh.2018.08.008

    Figure Lengend Snippet: ( A ) Frequency of cells in the G0/G1, S, and G2/M phases of the cell cycle in each anagliptin concentration group (n = 3). Huh-7 cells were incubated with DNA dye (Hoechst 33342). Plates containing the cells were scanned with ImageXpress Micro Screening System. Classification of cell phases was based on the fluorescence intensity of the DNA dye. For the cell number and cell cycle analyses, the intensity of the integrated DNA dye was assessed using the cell-cycle application module. ( B ) Expression of p21, p27kip1, pCDK2, and pRb of Huh-7 cells in each anagliptin concentration group (n = 4). Immunoblots for p21, p27kip1, CDK2, and pRb were performed using Huh-7 cell lysates. Amounts of protein were normalized to β-actin. ( C ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing low dose of anagliptin [ L-A ] [0.7 g/kg diet], and diet containing high dose of anagliptin [ H-A ] [2 g/kg diet]) (n = 5 for each group). * P < .05 vs L-A, ** P < .01 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( D ) Li-7 cell xenograft tumors and growth curves in mice at 21 days feeding in the same 3 groups as described in ( D ) (n = 5 for each group). * P < .05 vs L-A, # P < .05 vs H-A, ## P < .01 vs H-A. ( E ) Huh-7 cell xenograft tumors and growth curves in mice at 21 days after feeding in 3 groups (control diet, diet containing high dose of anagliptin [2 g/kg diet], and diet containing high dose of vildagliptin [2 g/kg diet]) (n = 5 for each group). * P < .05, ** P < .01 vs anagliptin group, # P < .05, ## P < .01 vs vildagliptin group.

    Article Snippet: The samples were subsequently incubated overnight at 4°C with a rabbit anti-CD26 monoclonal antibody (Abcam), a rabbit anti-p21 monoclonal antibody (Cell Signaling Technology), a rabbit anti-p27-kip1 monoclonal antibody (Cell Signaling Technology), a rabbit anti-phospho-CDK2 (Thr 160) polyclonal antibody (Cell Signaling Technology), or a rabbit anti-phospho-Rb (Ser807/811) monoclonal antibody (Cell Signaling Technology).

    Techniques: Concentration Assay, Incubation, Fluorescence, Expressing, Western Blot