CDC37
CDC37 (cell division cycle 37, HSP90 cochaperone, also known as P50CDC37) is a molecular co-chaperone that binds numerous protein kinases and promotes their interaction with the Hsp90 complex. It has a specific role in cell signal transduction. Browse Assay Genie's current range of CDC37 research reagents below, or read on for the biology behind the target.
CDC37 is a co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex. This results in stabilisation of the kinases and promotion of their activity. CDC37 also inhibits the ATPase activity of HSP90AA1. The protein is described as a molecular chaperone with a specific function in cell signal transduction, and it is thought to play a critical role in directing Hsp90 to its target kinases.
The CDC37 protein has been shown to form complexes with Hsp90 and a variety of protein kinases, including CDK4, CDK6, SRC, RAF-1, MOK and the eIF2 alpha kinases. This breadth of client kinases makes it a useful focus for work on kinase folding, stability and signalling. The protein localises to the cytoplasm and belongs to the CDC37 family. Researchers studying the CDC37 gene or CDC37 protein often do so alongside Hsp90 and its kinase clients.
The human gene is highly similar to Cdc37, a cell division cycle control protein of Saccharomyces cerevisiae, which explains the name. Earlier HGNC names refer to it as the S. cerevisiae homologue, and P50CDC37 is a recognised alias. Mouse and rat both carry a Cdc37 ortholog. HGNC places the gene in the group of microRNA protein coding host genes.
CDC37 binds numerous kinases and promotes their interaction with the Hsp90 complex, stabilising them and promoting their activity.
CDC37 inhibits HSP90AA1 ATPase activity and is thought to direct Hsp90 to its target kinases, making it relevant to chaperone mechanism studies.
As a molecular chaperone with a specific role in signal transduction, CDC37 is studied in kinase-dependent signalling pathways.
CDC37 forms complexes with CDK4 and CDK6, linking this co-chaperone to the study of cell cycle kinases.
CDC37 is a co-chaperone that binds numerous kinases and promotes their interaction with the Hsp90 complex, stabilising them and promoting their activity. It also inhibits HSP90AA1 ATPase activity. It is thought to direct Hsp90 to its target kinases in cell signal transduction.
The HGNC full name is cell division cycle 37, HSP90 cochaperone, and UniProt calls the protein Hsp90 co-chaperone Cdc37. P50CDC37 is a recognised alias. Earlier names describe it as the S. cerevisiae homologue of cell division cycle 37.
Yes. The human protein is highly similar to Cdc37 of Saccharomyces cerevisiae, a cell division cycle control protein. Mouse and rat each have an ortholog named Cdc37. Check the datasheet of any product for its validated reactivity.
Other cell division cycle proteins and cell cycle regulators with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q16543; product specifications from Assay Genie datasheets.