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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. De plus, nous expédions CDC37 Protéines (19) et CDC37 Kits (2) et beaucoup plus de produits pour cette protéine.
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Yeast (Saccharomyces cerevisiae) Polyclonal CDC37 Primary Antibody pour IF, IP - ABIN2451938
Reed: The selection of S. cerevisiae mutants defective in the start event of cell division. dans Genetics 1981
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Human Polyclonal CDC37 Primary Antibody pour 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. dans Nature methods 2013
Study showed that Cdc37 gene was up-regulated in human colorectal adenocarcinoma (CRC (Montrer CALR Anticorps)). Furthermore, knockdown of Cdc37 effectively reduced cell proliferation activity, enhanced apoptosis, and inhibited G1-S transition in CRC (Montrer CALR Anticorps) cells, and vice versa. For the mechanism, Cdc37 increased CDK4 (Montrer CDK4 Anticorps) stability to promote the phosphorylation of RB1 (Montrer RB1 Anticorps), which finally promoted the progression of CRC (Montrer CALR Anticorps).
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 (Montrer HSP90 Anticorps) phosphorylation at Y197 and specifically regulate kinase chaperoning.
findings suggested that this mechanism may be exploited by the Hsp90 (Montrer HSP90 Anticorps)-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 (Montrer HSP90 Anticorps) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (Montrer SNRPE Anticorps), where induced conformational instability acts as a "flag" for Hsp90 (Montrer HSP90 Anticorps) dependence and stable cochaperone association.
Ulk1 (Montrer ULK1 Anticorps) promoted the degradation of Hsp90 (Montrer HSP90 Anticorps)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (Montrer HSP90 Anticorps) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (Montrer ULK1 Anticorps) in response to Hsp90 (Montrer HSP90 Anticorps) inhibition in cancer cells
The authors find that the interaction between sB-Raf (Montrer RAF1 Anticorps) and the Hsp90 chaperone (Montrer HSP90 Anticorps) system is based on contacts with the M domain of Hsp90 (Montrer HSP90 Anticorps), 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 (Montrer HSP90 Anticorps) to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90 (Montrer HSP90 Anticorps), with or without binding to Hsp90 (Montrer HSP90 Anticorps), the interaction between Cdc37 and Hsp90 (Montrer HSP90 Anticorps) appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90 (Montrer HSP90 Anticorps)-mediated protein maturation.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (Montrer HSP90 Anticorps), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (Montrer HSP90 Anticorps)-Cdc37 complex acta (Montrer ACTC1 Anticorps) as an endogenous regulator of noncanonical p38alpha (Montrer MAPK14 Anticorps) activity.
CDC37 binds to Akt (Montrer AKT1 Anticorps) and HSP90 (Montrer HSP90 Anticorps) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (Montrer GSTa2 Anticorps) pull-down assay, and the possible interaction model was suggested.
JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (Montrer GLI1 Anticorps), 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 (Montrer NOS3 Anticorps)) and may play an important role in mediating the eNOS (Montrer NOS3 Anticorps) 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