CDK1 Protein, Human (Biotinylated, sf9, Avi)

The CDK1/CDC2-cyclin-B complex is a key regulator of the cell cycle. It plays an important control role in the interphase fertilized egg and is crucial for the early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates the CDK1/cyclin complex. This complex phosphorylates multiple substrates, triggering centrosome dissociation, Golgi dynamics, nuclear envelope disruption, and chromosome condensation. After chromosomes are condensed and aligned on the metaphase plate, CDK1 activity is turned off by WEE1- and PKMYT1-mediated phosphorylation, allowing sister chromatid separation, chromosome decondensation, nuclear envelope remodeling, and cytokinesis. When DNA is damaged, CDK1 will be inactivated by phosphorylation mediated by PKR/EIF2AK2 and WEE1, thereby stopping the cell cycle and genome replication and promoting DNA repair. After repair is completed, CDK1 is reactivated by WIP1-dependent signaling to resume cell cycle progression. In proliferating cells, CDK1-mediated phosphorylation can inhibit FOXO1 interactions and promote FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. In addition, phosphorylation of CDK1 can also regulate microtubule dynamics, spindle formation and other processes.