Recombinant Human CDK1 protein

CDK1 (Cyclin-Dependent Kinase 1), also known as cell division control protein 2 (CDC2), is a serine/threonine kinase that plays a central role in regulating cell cycle progression, particularly the G2/M phase transition. As a member of the cyclin-dependent kinase family, CDK1 requires binding to cyclin B for activation, forming the maturation-promoting factor (MPF) complex. This complex triggers critical events such as nuclear envelope breakdown, chromosome condensation, and spindle assembly, ensuring proper mitotic entry and progression. CDK1 activity is tightly controlled by phosphorylation/dephosphorylation events (e.g., inhibitory phosphorylation at Thr14/Tyr15 by WEE1 and activating dephosphorylation by CDC25) and cyclin degradation during cell cycle checkpoints.

Recombinant CDK1 protein is produced through genetic engineering techniques, typically expressed in prokaryotic (e.g., E. coli) or eukaryotic systems (e.g., insect cells) to maintain proper folding and kinase activity. The purified protein retains functional domains, including the catalytic kinase domain and cyclin-binding regions, enabling researchers to study its biochemical properties, substrate interactions, and regulatory mechanisms in vitro. Its molecular weight ranges between 34-37 kDa depending on post-translational modifications.

In research, recombinant CDK1 serves as a vital tool for investigating cell cycle dysregulation in cancers, where CDK1 overexpression frequently correlates with uncontrolled proliferation and poor prognosis. It is widely used in drug discovery for screening CDK1 inhibitors, analyzing kinase activity assays, and modeling cell cycle-related diseases. Studies using recombinant CDK1 have also elucidated its non-mitotic roles in DNA damage response and apoptosis. As a conserved regulator of cell division, CDK1 remains a key therapeutic target and a fundamental subject in cell biology research.