产品
编 号：F294755
分子式：C35H57N15O9
分子量：831.92
分子式：C35H57N15O9
分子量：831.92
产品类型
规格
价格
是否有货
1mg
询价
询价
5mg
询价
询价
10mg
询价
询价
结构图
CAS No: 255064-79-0
产品详情
生物活性：
CDK2 is a member of the eukaryotic S/T protein kinase family and its function is to catalyze the phosphoryl transfer of ATP γ-phosphate to serine or threonine hydroxyl (denoted as S0/T0) in a protein substrate.
体外研究：
CDK2 (Cyclin-dependent kinase 2) is a member of the eukaryotic S/T protein kinase family and its function is to catalyze the phosphoryl transfer of ATP γ-phosphate to serine or threonine hydroxyl (denoted as S0/T0) in a protein substrate. The fully active CDK2 is in complex with HHASPRK (an optimal peptide substrate), namely interactions of CDK2 with peptide substrate and the dynamics of the G-loop. CDK2 participates in eukaryotic cell cycle regulation at the G1/S boundary. CDK2 deregulation has been proved to occur in tumor cells, evoking a strong interest in artificial and native inhibitors. CDK2 activity is tightly regulated by a complex mechanism, including a positive regulatory subunit binding, and phosphorylations at positive and/or negative regulatory sites.
CDK2 is a member of the eukaryotic S/T protein kinase family and its function is to catalyze the phosphoryl transfer of ATP γ-phosphate to serine or threonine hydroxyl (denoted as S0/T0) in a protein substrate.
体外研究：
CDK2 (Cyclin-dependent kinase 2) is a member of the eukaryotic S/T protein kinase family and its function is to catalyze the phosphoryl transfer of ATP γ-phosphate to serine or threonine hydroxyl (denoted as S0/T0) in a protein substrate. The fully active CDK2 is in complex with HHASPRK (an optimal peptide substrate), namely interactions of CDK2 with peptide substrate and the dynamics of the G-loop. CDK2 participates in eukaryotic cell cycle regulation at the G1/S boundary. CDK2 deregulation has been proved to occur in tumor cells, evoking a strong interest in artificial and native inhibitors. CDK2 activity is tightly regulated by a complex mechanism, including a positive regulatory subunit binding, and phosphorylations at positive and/or negative regulatory sites.
产品资料
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