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phosphorylated cdk2 on thr160  (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc phosphorylated cdk2 on thr160
Figure 1. A synthetic peptide corresponding to the CaM- binding sequence of cyclin E inhibits CaM–cyclin E interac- tions and calcium-sensitive <t>CDK2</t> activity in VSMCs. A, Sequences of the CaM binding region of mouse and human cyclin E1 and of synthesized peptides. Hydrophobic residues are bold and underlined. 5A indicates control peptide with 5 alanine substi- tutions at every hydrophobic residue; NC, negative control peptide of identical length but randomly generated sequence. B, Histone H1 in vitro kinase assay on G1/S-synchronized mouse VSMC extracts at 500 nmol/L [Ca2] in the presence of peptides (each 100 mol/L). C, Co-IP analysis. Cyclin E/CDK2 complex formation and CaM–cyclin E interaction were examined in the presence of each peptide (100 mol/L). A representative blot is shown (N2). D, Histone H1 in vitro kinase assay on G1/S-synchronized mouse VSMC extracts at 0 or 500 nmol/L [Ca2] in the presence of CBS or NC (100 mol/L). For all in vitro kinase assay experiments, N3 for each condition, with experiments repeated at least twice. Results were normalized to the kinase activity of the untreated group (B) and the untreated group at 0 nmol/L [Ca2] (D). (**P0.01 vs no peptide by 1-way ANOVA and post hoc Student’s t test for multiple comparisons.)
Phosphorylated Cdk2 On Thr160, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Figure 1. A synthetic peptide corresponding to the CaM- binding sequence of cyclin E inhibits CaM–cyclin E interac- tions and calcium-sensitive CDK2 activity in VSMCs. A, Sequences of the CaM binding region of mouse and human cyclin E1 and of synthesized peptides. Hydrophobic residues are bold and underlined. 5A indicates control peptide with 5 alanine substi- tutions at every hydrophobic residue; NC, negative control peptide of identical length but randomly generated sequence. B, Histone H1 in vitro kinase assay on G1/S-synchronized mouse VSMC extracts at 500 nmol/L [Ca2] in the presence of peptides (each 100 mol/L). C, Co-IP analysis. Cyclin E/CDK2 complex formation and CaM–cyclin E interaction were examined in the presence of each peptide (100 mol/L). A representative blot is shown (N2). D, Histone H1 in vitro kinase assay on G1/S-synchronized mouse VSMC extracts at 0 or 500 nmol/L [Ca2] in the presence of CBS or NC (100 mol/L). For all in vitro kinase assay experiments, N3 for each condition, with experiments repeated at least twice. Results were normalized to the kinase activity of the untreated group (B) and the untreated group at 0 nmol/L [Ca2] (D). (**P0.01 vs no peptide by 1-way ANOVA and post hoc Student’s t test for multiple comparisons.)

Journal: Circulation Research

Article Title: Peptide-Mediated Disruption of Calmodulin–Cyclin E Interactions Inhibits Proliferation of Vascular Smooth Muscle Cells and Neointima Formation

doi: 10.1161/circresaha.110.239483

Figure Lengend Snippet: Figure 1. A synthetic peptide corresponding to the CaM- binding sequence of cyclin E inhibits CaM–cyclin E interac- tions and calcium-sensitive CDK2 activity in VSMCs. A, Sequences of the CaM binding region of mouse and human cyclin E1 and of synthesized peptides. Hydrophobic residues are bold and underlined. 5A indicates control peptide with 5 alanine substi- tutions at every hydrophobic residue; NC, negative control peptide of identical length but randomly generated sequence. B, Histone H1 in vitro kinase assay on G1/S-synchronized mouse VSMC extracts at 500 nmol/L [Ca2] in the presence of peptides (each 100 mol/L). C, Co-IP analysis. Cyclin E/CDK2 complex formation and CaM–cyclin E interaction were examined in the presence of each peptide (100 mol/L). A representative blot is shown (N2). D, Histone H1 in vitro kinase assay on G1/S-synchronized mouse VSMC extracts at 0 or 500 nmol/L [Ca2] in the presence of CBS or NC (100 mol/L). For all in vitro kinase assay experiments, N3 for each condition, with experiments repeated at least twice. Results were normalized to the kinase activity of the untreated group (B) and the untreated group at 0 nmol/L [Ca2] (D). (**P0.01 vs no peptide by 1-way ANOVA and post hoc Student’s t test for multiple comparisons.)

Article Snippet: Blots were blocked with 5% non-fat dry milk in TBS-T (10 mmol/L Tris (pH 8.0), 150 mmol/L NaCl, and 0.05 % Tween 20) overnight at 4°C and incubated for 3 h at 25°C in TBS-T plus 3% non-fat dry milk containing primary antibodies: anti-CDK2 (07-631, Upstate Biotech, Billerica, MA), -cyclin E (ab7959, Abcam, Cambridge, MA), -phosphorylated CDK2 on Thr160 (2561, Cell Signaling Technology, Danvers, MA), -CaM (sc-1989, Santa Cruz Biotechnology, Santa Cruz, CA), -phosphorylated CDK2 on Thr14/Tyr15 (sc-28435-R, Santa Cruz Biotechnology), and -actin (sc-7210, Santa Cruz Biotechnology).

Techniques: Binding Assay, Sequencing, Activity Assay, Synthesized, Control, Residue, Negative Control, Generated, In Vitro, Kinase Assay, Co-Immunoprecipitation Assay

Figure 3. CBS inhibits CDK2 phosphor- ylation and S-phase entry of serum- stimulated VSMCs. Primary mouse aortic SMCs were starved for 72 hours, nucleo- fected with peptides (1 mmol/L), serum- stimulated for 24 hours, and harvested for: Western blotting, representative blots shown with normalized band intensities (N3 for each experiment shown) (A); and FACS analysis with 10 000 cells per group (N3) (B) (*P0.05 vs no peptide by 1-way ANOVA and post hoc Student’s t test).

Journal: Circulation Research

Article Title: Peptide-Mediated Disruption of Calmodulin–Cyclin E Interactions Inhibits Proliferation of Vascular Smooth Muscle Cells and Neointima Formation

doi: 10.1161/circresaha.110.239483

Figure Lengend Snippet: Figure 3. CBS inhibits CDK2 phosphor- ylation and S-phase entry of serum- stimulated VSMCs. Primary mouse aortic SMCs were starved for 72 hours, nucleo- fected with peptides (1 mmol/L), serum- stimulated for 24 hours, and harvested for: Western blotting, representative blots shown with normalized band intensities (N3 for each experiment shown) (A); and FACS analysis with 10 000 cells per group (N3) (B) (*P0.05 vs no peptide by 1-way ANOVA and post hoc Student’s t test).

Article Snippet: Blots were blocked with 5% non-fat dry milk in TBS-T (10 mmol/L Tris (pH 8.0), 150 mmol/L NaCl, and 0.05 % Tween 20) overnight at 4°C and incubated for 3 h at 25°C in TBS-T plus 3% non-fat dry milk containing primary antibodies: anti-CDK2 (07-631, Upstate Biotech, Billerica, MA), -cyclin E (ab7959, Abcam, Cambridge, MA), -phosphorylated CDK2 on Thr160 (2561, Cell Signaling Technology, Danvers, MA), -CaM (sc-1989, Santa Cruz Biotechnology, Santa Cruz, CA), -phosphorylated CDK2 on Thr14/Tyr15 (sc-28435-R, Santa Cruz Biotechnology), and -actin (sc-7210, Santa Cruz Biotechnology).

Techniques: Western Blot