Cdk1, also known as p34 [cdc2], is a ubiquitously expressed serine/threonine protein kinase. Cdk1/cdc2 has been identified as the catalytic subunit of the maturation-promoting factor (MPF), while cyclin B acts as the regulatory subunit. The binding of these two subunits is critical to the transition into M-phase of the mammalian cell cycle, and this factor's role is regulated by a series of phosphorylations and dephosphorylations. After binding to cyclin B, cdk1/cdc2 is phosphorylated on Thr-14, by Myt1, and Tyr-15, by wee1 or mik1, yielding an inactive pre-MPF complex. Phosphorylation of cdk1/cdc2 on Thr-161 is performed by a cdk7/cyclin H complex and is necessary for activation of the cdc2 complex. Dephosphorylation of Thr-14 and Tyr-15 by CDC25 occurs at the prophase/metaphase transition and completes activation of the cdc2/cyclin B complex, initiating the cell's entry into mitosis.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.