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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae.
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Human Polyclonal CDC37 Primary Antibody for ICC, IF - ABIN4296941
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
Yeast (Saccharomyces cerevisiae) Polyclonal CDC37 Primary Antibody for IF, IP - ABIN2451938
Reed: The selection of S. cerevisiae mutants defective in the start event of cell division. in Genetics 1981
Show all 3 Pubmed References
Study showed that Cdc37 gene was up-regulated in human colorectal adenocarcinoma (CRC (show CALR Antibodies)). Furthermore, knockdown of Cdc37 effectively reduced cell proliferation activity, enhanced apoptosis, and inhibited G1-S transition in CRC (show CALR Antibodies) cells, and vice versa. For the mechanism, Cdc37 increased CDK4 (show CDK4 Antibodies) stability to promote the phosphorylation of RB1 (show RB1 Antibodies), which finally promoted the progression of CRC (show CALR Antibodies).
During the kinase chaperone cycle, Cdc37 phosphorylated at Y298 acts as a platform for docking of non-receptor tyrosine kinases through their regulatory domains to drive the coupled Hsp90 (show HSP90 Antibodies) phosphorylation at Y197 and specifically regulate kinase chaperoning.
findings suggested that this mechanism may be exploited by the Hsp90 (show HSP90 Antibodies)-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 Antibodies) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (show SNRPE Antibodies), where induced conformational instability acts as a "flag" for Hsp90 (show HSP90 Antibodies) dependence and stable cochaperone association.
Ulk1 (show ULK1 Antibodies) promoted the degradation of Hsp90 (show HSP90 Antibodies)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (show HSP90 Antibodies) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (show ULK1 Antibodies) in response to Hsp90 (show HSP90 Antibodies) inhibition in cancer cells
The authors find that the interaction between sB-Raf (show RAF1 Antibodies) and the Hsp90 chaperone (show HSP90 Antibodies) system is based on contacts with the M domain of Hsp90 (show HSP90 Antibodies), 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.
Results showed that Cdc37 acts as a bridge to direct Hsp90 (show HSP90 Antibodies) to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90 (show HSP90 Antibodies), with or without binding to Hsp90 (show HSP90 Antibodies), the interaction between Cdc37 and Hsp90 (show HSP90 Antibodies) appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90 (show HSP90 Antibodies)-mediated protein maturation.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (show HSP90 Antibodies), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (show HSP90 Antibodies)-Cdc37 complex acta (show ACTC1 Antibodies) as an endogenous regulator of noncanonical p38alpha (show MAPK14 Antibodies) activity.
CDC37 binds to Akt (show AKT1 Antibodies) and HSP90 (show HSP90 Antibodies) 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 Antibodies) pull-down assay, and the possible interaction model was suggested.
JAK1 (show JAK1 Antibodies)/2 are client proteins of Hsp90 alpha (show HSP90AA1 Antibodies) and beta; Hsp90 (show HSP90 Antibodies) and CDC37 play a critical role in types I and II interferon (show IFNA Antibodies) pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (show GLI1 Antibodies), 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 Antibodies)) and may play an important role in mediating the eNOS (show NOS3 Antibodies) 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