Cell Division Cycle 37 Proteins (CDC37)

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 (5) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
CDC37 11140 Q16543
Rat CDC37 CDC37 114562 Q63692
Mouse CDC37 CDC37 12539 Q61081
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Catalog No. Origin Source Conjugate Quantity Supplier Delivery Price Details
Human Un-conjugated 2 μg Log in to see 6 Days
$168.54
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More Proteins for Cell Division Cycle 37 (CDC37) Interaction Partners

Human Cell Division Cycle 37 (CDC37) interaction partners

  1. Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 (show HSP90 Proteins) in hepatocellular carcinoma, reducing tumor growth.

  2. 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.

  3. 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

  4. 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.

  5. Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes.

  6. Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.

  7. RIP3 (show RIPK3 Proteins) activation following the induction of necroptosis requires the activity of an HSP90 (show HSP90 Proteins) and CDC37 cochaperone complex.

  8. 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

  9. 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 (show HSP90 Proteins) binding.

  10. CDC37 has an important role in chaperoning protein kinases; it stabilizes kinase clients by a mechanism that is not dependent on a substantial direct interaction between CDC37 and HSP90 (show HSP90 Proteins), but requires HSP90 (show HSP90 Proteins) activity

Mouse (Murine) Cell Division Cycle 37 (CDC37) interaction partners

  1. Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 (show HSP90 Proteins) in hepatocellular carcinoma, reducing tumor growth.

  2. 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.

  3. Hsp90 (show HSP90 Proteins)-Cdc37 complex acta (show ACTC1 Proteins) as an endogenous regulator of noncanonical p38alpha (show MAPK14 Proteins) activity.

  4. CDC37 binds to Akt (show AKT1 Proteins) and HSP90 (show HSP90 Proteins) in the signal transduction pathway in human tumor cells

  5. 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.

  6. 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

  7. 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 Protein Profile

Protein Summary

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.

Gene names and symbols associated with Cell Division Cycle 37 Proteins (CDC37)

  • cell division cycle 37 (CDC37)
  • cell division cycle 37 (Cdc37)
  • p50 protein
  • p50Cdc37 protein

Protein level used designations for Cell Division Cycle 37 Proteins (CDC37)

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 , hsp90 co-chaperone Cdc37 , CDC37 (cell division cycle 37 S. cerevisiae homolog) , p50Cdc37

GENE ID SPECIES
11140 Homo sapiens
114562 Rattus norvegicus
12539 Mus musculus
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