Anti-Cdc37 antibody [EPR4935]

Supplementary info

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

Activity summary

The Cdc37 protein also known as cell division cycle 37 homolog is a molecular chaperone that assists in the proper folding and stabilization of protein kinases. With a mass of approximately 44 kDa Cdc37 is widely expressed in mammalian tissues. It interacts directly with other proteins aiding in their stabilization and activity. Functioning closely with Hsp90 Cdc37 forms a chaperone complex critical for the maturation of several protein kinases.

Biological function summary

Cdc37 serves as a co-chaperone with Hsp90 in regulating protein kinase activity by maintaining their functional conformation and stability. This protein acts mainly as a kinase-specific adapter that recruits kinases to the Hsp90 chaperone system forming a protein complex essential for the proper functioning of key signaling molecules. Its role is vital in signal transduction and cellular growth regulation ensuring proper cell cycle progression and response to external stimuli.

Pathways

Cdc37 plays a significant role in the PI3K/AKT and MAPK signaling pathways. In these pathways Cdc37 assists in the proper activation and function of various kinases such as AKT and RAF which are important for cell growth survival and proliferation. Its partnership with Hsp90 in these pathways underlines its importance in maintaining kinase activity ensuring that signaling cascades proceed correctly for normal cellular function.

Associated diseases and disorders

Cdc37 has been implicated in cancer and neurodegenerative diseases like Alzheimer's. Overexpression or dysfunction of Cdc37 can lead to improper activation of oncogenic kinases contributing to tumor progression. Additionally the protein's association with Hsp90 highlights its potential involvement in Alzheimer's where protein misfolding and stability are disrupted making Cdc37 a target of interest for therapeutic intervention in these conditions.