Wee1 (D10D2) Rabbit mAb recognizes endogenous levels of total Wee1 protein.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala54 of human Wee1 protein.

Entry of all eukaryotic cells into mitosis is regulated by activation of cdc2 kinase. The critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of Tyr15 and Thr14 (1,2). Phosphorylation at Tyr15 and Thr14 and inhibition of cdc2 is carried out by Wee1 and Myt1 protein kinases, while Tyr15 dephosphorylation and activation of cdc2 is carried out by the cdc25 phosphatase (1,3,4). Hyperphosphorylation and inactivation of Myt1 in mitosis suggests that one or more kinases activated at the G2/M transition negatively regulates Myt1 activity. Kinases shown to phosphorylate Myt1 include cdc2, p90RSK, Akt, and Plk1 (5-7).

Wee1 is inactivated upon mitotic entry by phosphorylation at Ser53 and Ser123 by Plk1 and cdc2, followed by β-TrCP-mediated ubiquitination and degradation (1,9,10).