Anti-Cdk1 (Tyr-15) [conserved site], Phosphospecific Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P06493 |
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Reactivity | Bovine |
Host | Mouse |
Clonality | Mouse Monoclonal |
Isotype | IgG1 |
Clone Names | M231 |
Calculated MW | 34095 Da |
Gene ID | 983 |
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Other Names | Cdc2 |
Target/Specificity | Cyclin-dependent kinases (Cdks) are a family of serine/threonine kinases that require association with regulatory subunits known as cyclins for activation. In addition, post-translational phosphorylation and dephosphorylation events regulate Cdk activity. Phosphorylation of Thr-160 in the T loop by Cdk-activating kinase (CAK) is an obligatory step in kinase activation. By contrast, phosphorylation of the Thr-14 and Tyr-15 residues by the Wee1 family of dual specificity kinases is inhibitory for the Cdks, and dephosphorylation of these residues by the Cdc25 family of phosphatases coincides with Cdk activation. Alternatively, Cdk5 appears to require different mechanisms for activation. This Cdk is activated through association with specific activators, including p35, p39, and p67. Cdk5 is primarily activated in neuronal cells, and only c-Abl kinase, rather than Wee family members, have been shown to phosphorylate Tyr-15 to regulate its activity. |
Format | Protein A Purified |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Anti-Cdk1 (Tyr-15) [conserved site], Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |
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Background
Cyclin-dependent kinases (Cdks) are a family of serine/threonine kinases that require association with regulatory subunits known as cyclins for activation. In addition, post-translational phosphorylation and dephosphorylation events regulate Cdk activity. Phosphorylation of Thr-160 in the T loop by Cdk-activating kinase (CAK) is an obligatory step in kinase activation. By contrast, phosphorylation of the Thr-14 and Tyr-15 residues by the Wee1 family of dual specificity kinases is inhibitory for the Cdks, and dephosphorylation of these residues by the Cdc25 family of phosphatases coincides with Cdk activation. Alternatively, Cdk5 appears to require different mechanisms for activation. This Cdk is activated through association with specific activators, including p35, p39, and p67. Cdk5 is primarily activated in neuronal cells, and only c-Abl kinase, rather than Wee family members, have been shown to phosphorylate Tyr-15 to regulate its activity.
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