Phospho-cdc2 (Tyr15) Antibody detects endogenous levels of cdc2, CDK2 and CDK5 only when phosphorylated at tyrosine 15. The antibody does not cross-react with CDK4, CDK6 or CDK7. It does detect the yeast orthologue of cdc2 (cdc28) when phosphorylated at tyrosine 19
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr15 of human cdc2. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The entry of eukaryotic cells into mitosis is regulated by cdc2 kinase activation, a process controlled at several steps including cyclin binding and phosphorylation of cdc2 at Thr161 (1). However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of cdc2 at Thr14 and Tyr15 (2). Phosphorylation at Thr14 and Tyr15, resulting in inhibition of cdc2, can be carried out by Wee1 and Myt1 protein kinases (3,4). The cdc25 phosphatase may be responsible for removal of phosphates at Thr14 and Tyr15 and subsequent activation of cdc2 (1,5).