Anti-Cdc25B (phospho S323) antibody

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Cdc25B phosphatase also known as M-phase inducer phosphatase 2 or CDC25B2 plays an important role in cell cycle regulation by activating cyclin-dependent kinases (CDKs). It weighs approximately 62 kDa. Researchers observe its expression in normal and cancerous tissues with higher levels found in proliferating cells. Cdc25B localizes to the nucleus during the cell cycle where it exerts control over cell division by removing inhibitory phosphates on CDKs.

Biological function summary

This protein accelerates the transition through various phases of the cell cycle. It does not function alone but forms part of a complex regulatory network ensuring timely CDK activation. By promoting the G1/S and G2/M transitions Cdc25B enables cells to progress through the cell cycle. Additionally Cdc25B is involved in DNA damage checkpoints helping cells respond to genotoxic stress thereby ensuring genomic stability through complex regulatory interactions.

Pathways

Several key cell cycle pathways include Cdc25B. It acts prominently in the cell cycle checkpoint control pathway and the DNA damage response pathway. The protein directly activates CDC2/CDK1 through dephosphorylation contributing to cell cycle progression. Cdc25B interacts with regulatory proteins like ATM/ATR which modulate Cdc25B activity in response to DNA damage further integrating it into critical checkpoint pathways.

Researchers link Cdc25B to cancer and neurological disorders. Overexpression of Cdc25B often associates with various cancers where it may contribute to unchecked cell proliferation through its influence on CDK activity. In this context it connects with oncogenic proteins like Cyclin B1 providing potential targets for therapeutic intervention. Additionally malfunction in Cdc25B activity associates with neurodegenerative diseases due to its role in cell cycle regulation and DNA repair mechanisms. Scientists are exploring its relationship with proteins such as p53 in these diseases offering insights into potential treatment strategies.