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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 (22) und CDC37 Kits (3) und viele weitere Produktgruppen zu diesem Protein an.
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Dog (Canine) Monoclonal CDC37 Primary Antibody für IF, IP - ABIN968047
Grammatikakis, Lin, Grammatikakis, Tsichlis, Cochran: p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function. in Molecular and cellular biology 1999
Zeige alle 3 Referenzen für 968047
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
Human Polyclonal CDC37 Primary Antibody für ELISA, WB - ABIN1534319
Lamphere, Fiore, Xu, Brizuela, Keezer, Sardet, Draetta, Gyuris: Interaction between Cdc37 and Cdk4 in human cells. in Oncogene 1997
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.
RIP3 (zeige RIPK3 Antikörper) activation following the induction of necroptosis requires the activity of an HSP90 (zeige HSP90 Antikörper) and CDC37 cochaperone complex.
Correlation between PDZK1 (zeige PDZK1 Antikörper), Cdc37, Akt (zeige AKT1 Antikörper) and breast cancer malignancy: the role of PDZK1 (zeige PDZK1 Antikörper) in cell growth through Akt (zeige AKT1 Antikörper) stabilization by increasing and interacting with Cdc37
The N-terminal tail serves as an intramolecular chaperone ensuring that CDC37 assumes one of two interconvertible states in a manner impacting the interaction of the client binding N-domain and the MC-domains, involved in dimerization and HSP90 (zeige HSP90 Antikörper) binding.
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 (zeige JAK1 Antikörper)/2 are client proteins of Hsp90 alpha (zeige HSP90AA1 Antikörper) and beta; Hsp90 (zeige HSP90 Antikörper) and CDC37 play a critical role in types I and II interferon (zeige IFNA Antikörper) 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