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.
Zukerberg, L. R. (2000) Neuron 26:633.
Poon, R.Y.C. et al. (1997) J Biol. Chem. 272( 9):5703.
*For more information, see UniProt Accession P06493
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: