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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. Zusätzlich bieten wir Ihnen CDC37 Proteine (19) und CDC37 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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Yeast (Saccharomyces cerevisiae) Polyclonal CDC37 Primary Antibody für 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
Human Polyclonal CDC37 Primary Antibody für 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
Study showed that Cdc37 gene was up-regulated in human colorectal adenocarcinoma (CRC (zeige CALR Antikörper)). Furthermore, knockdown of Cdc37 effectively reduced cell proliferation activity, enhanced apoptosis, and inhibited G1-S transition in CRC (zeige CALR Antikörper) cells, and vice versa. For the mechanism, Cdc37 increased CDK4 (zeige CDK4 Antikörper) stability to promote the phosphorylation of RB1 (zeige RB1 Antikörper), which finally promoted the progression of CRC (zeige CALR Antikörper).
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 (zeige HSP90 Antikörper) phosphorylation at Y197 and specifically regulate kinase chaperoning.
findings suggested that this mechanism may be exploited by the Hsp90 (zeige HSP90 Antikörper)-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 (zeige HSP90 Antikörper) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (zeige SNRPE Antikörper), where induced conformational instability acts as a "flag" for Hsp90 (zeige HSP90 Antikörper) dependence and stable cochaperone association.
Ulk1 (zeige ULK1 Antikörper) promoted the degradation of Hsp90 (zeige HSP90 Antikörper)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (zeige HSP90 Antikörper) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (zeige ULK1 Antikörper) in response to Hsp90 (zeige HSP90 Antikörper) inhibition in cancer cells
The authors find that the interaction between sB-Raf (zeige RAF1 Antikörper) and the Hsp90 chaperone (zeige HSP90 Antikörper) system is based on contacts with the M domain of Hsp90 (zeige HSP90 Antikörper), 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 (zeige HSP90 Antikörper) to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90 (zeige HSP90 Antikörper), with or without binding to Hsp90 (zeige HSP90 Antikörper), the interaction between Cdc37 and Hsp90 (zeige HSP90 Antikörper) appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90 (zeige HSP90 Antikörper)-mediated protein maturation.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (zeige HSP90 Antikörper), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (zeige HSP90 Antikörper)-Cdc37 complex acta (zeige ACTC1 Antikörper) as an endogenous regulator of noncanonical p38alpha (zeige MAPK14 Antikörper) activity.
CDC37 binds to Akt (zeige AKT1 Antikörper) and HSP90 (zeige HSP90 Antikörper) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (zeige GSTa2 Antikörper) 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 (zeige GLI1 Antikörper), 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 (zeige NOS3 Antikörper)) and may play an important role in mediating the eNOS (zeige NOS3 Antikörper) 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