PhosphoPlus® Cdc2 (Tyr15) Western Detection Kit offers an efficient way of detecting cdc2 (Tyr15) phosphorylation by western blotting. The kit contains enough primary and secondary antibodies to perform 10 western blots, as well as a set of pre-stained and biotinylated markers, control proteins and LumiGLO® reagent.
When used in conjunction with our Phototope®-HRP Western Detection Kit, Phospho-cdc2 (Tyr15) Antibody detects less than 10 ng of tyrosine phosphorylated cdc2 yet will not react with up to 1 µg of non-tyrosine phosphorylated cdc2. Similarly, Phospho-cdc2 (Tyr15) Antibody detects phosphorylated tyrosine 15 of cdk2 but demonstrates no cross reactivity to cdk4, cdk6 and cdk7 or other phospho-tyrosine proteins.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the phsphorylation site. Antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibody is produced by immunizing animals with a recombinant human cdc2 fusion protein.
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).
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