Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. Additionally we are shipping CDC37 Antibodies (149) and CDC37 Kits (3) and many more products for this protein.
Showing 10 out of 19 products:
Human CDC37 Protein expressed in Baculovirus infected Insect Cells - ABIN2003178
Roiniotis, Masendycz, Ho, Scholz: Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37. in Biochemistry 2005
Show all 2 Pubmed References
findings suggested that this mechanism may be exploited by the Hsp90 (show HSP90 Proteins)-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation
The results suggest a re-evaluation of the role of Cdc37 in the kinase lifecycle, and suggest that such interactions potentially allow kinases to more rapidly respond to key signals while simultaneously protecting unstable kinases from degradation and suppressing unwanted basal activity.
Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 (show HSP90 Proteins) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (show SNRPE Proteins), where induced conformational instability acts as a "flag" for Hsp90 (show HSP90 Proteins) dependence and stable cochaperone association.
Ulk1 (show ULK1 Proteins) promoted the degradation of Hsp90 (show HSP90 Proteins)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (show HSP90 Proteins) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (show ULK1 Proteins) in response to Hsp90 (show HSP90 Proteins) inhibition in cancer cells
The authors find that the interaction between sB-Raf (show RAF1 Proteins) and the Hsp90 chaperone (show HSP90 Proteins) system is based on contacts with the M domain of Hsp90 (show HSP90 Proteins), which contributes in forming the ternary complex with Cdc37 as long as the kinase is not stabilized by nucleotide.
Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes.
Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.
RIP3 (show RIPK3 Proteins) activation following the induction of necroptosis requires the activity of an HSP90 (show HSP90 Proteins) and CDC37 cochaperone complex.
Correlation between PDZK1 (show PDZK1 Proteins), Cdc37, Akt (show AKT1 Proteins) and breast cancer malignancy: the role of PDZK1 (show PDZK1 Proteins) in cell growth through Akt (show AKT1 Proteins) stabilization by increasing and interacting with Cdc37
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (show HSP90 Proteins), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (show HSP90 Proteins)-Cdc37 complex acta (show ACTC1 Proteins) as an endogenous regulator of noncanonical p38alpha (show MAPK14 Proteins) activity.
CDC37 binds to Akt (show AKT1 Proteins) and HSP90 (show HSP90 Proteins) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (show GSTa2 Proteins) pull-down assay, and the possible interaction model was suggested.
JAK1 (show JAK1 Proteins)/2 are client proteins of Hsp90 alpha (show HSP90AA1 Proteins) and beta; Hsp90 (show HSP90 Proteins) and CDC37 play a critical role in types I and II interferon (show IFNA Proteins) pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (show GLI1 Proteins), suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells.
Cdc37 has a direct regulatory interaction with endothelial nitric oxide synthase (eNOS (show NOS3 Proteins)) and may play an important role in mediating the eNOS (show NOS3 Proteins) protein complex formation.
The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.
, cdc37 protein
, hsp90 co-chaperone Cdc37
, Hsp90 co-chaperone Cdc37
, hypothetical protein
, CDC37 (cell division cycle 37, S. cerevisiae, homolog)
, CDC37 cell division cycle 37 homolog
, cell division cycle 37 homolog
, hsp90 chaperone protein kinase-targeting subunit
, CDC37 (cell division cycle 37 S. cerevisiae homolog)
, CDC37 cell division cycle 37 protein
, CDC37 homolog
, cell division cycle 37 protein
, cell division cycle control protein 37