CDC37 is highly similar to the cell division cycle control protein found in Saccharomyces cerevisiae (yeast). The human CDC37 protein is composed of 388 amino acids and has a molecular weight of approximately 45.71 kDa . It is often tagged with a His (histidine) tag to facilitate purification and detection in laboratory experiments.
CDC37 forms a complex with Heat Shock Protein 90 (Hsp90) and several protein kinases, including CDK4, CDK6, SRC, RAF-1, MOK, and eIF2 alpha kinases . This complex is vital for directing Hsp90 to its target kinases, thereby stabilizing and promoting their activity . CDC37 also inhibits the ATPase activity of Hsp90, which is essential for its chaperone function .
Mutations or dysregulation of CDC37 have been associated with various diseases, including Fanconi Anemia and Parkinson’s Disease . Its role in stabilizing protein kinases makes it a critical player in cell cycle regulation and signal transduction pathways, which are often disrupted in cancer and other diseases.
Recombinant CDC37 tagged with a His tag is widely used in research to study its function and interactions with other proteins. The His tag allows for easy purification using nickel affinity chromatography, making it a valuable tool for biochemical and structural studies . Researchers can use recombinant CDC37 to investigate its role in various signaling pathways and its potential as a therapeutic target.