CDC37 Human

CDC37 is known to form complexes with Heat Shock Protein 90 (Hsp90) and a variety of protein kinases, including CDK4, CDK6, SRC, RAF-1, MOK, and eIF2 alpha kinases . This interaction is critical for the proper functioning of these kinases, as CDC37 directs Hsp90 to its target kinases, thereby stabilizing them and promoting their activity . Additionally, CDC37 inhibits the ATPase activity of HSP90AA1, further contributing to the stabilization of the kinase-Hsp90 complex .

CDC37 is expressed in proliferative zones during embryonic development and in adult tissues, indicating its positive role in cell proliferation . It is required for cell division in budding yeast and is thought to play an important role in the establishment of signaling pathways that control cell growth and division . The protein’s ability to bind to numerous kinases and promote their interaction with the Hsp90 complex is essential for the regulation of cell cycle progression and signal transduction .

Mutations or dysregulation of CDC37 have been associated with various diseases, including Fanconi Anemia and Parkinson’s Disease . The protein’s involvement in multiple signaling pathways makes it a potential target for therapeutic interventions in diseases characterized by abnormal cell proliferation and signal transduction.

Recombinant human CDC37 protein is produced using recombinant DNA technology, which involves inserting the gene encoding CDC37 into a suitable expression system, such as bacteria or mammalian cells. This allows for the large-scale production of the protein, which can be used for research and therapeutic purposes. Recombinant CDC37 is used in various studies to understand its role in cell cycle regulation and to develop potential therapeutic strategies targeting its function .