Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) ELISA Kits

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 (220) and CDC37 Proteins (19) and many more products for this protein.

list all ELISA KIts Gene Name GeneID UniProt
CDC37 11140 Q16543
CDC37 12539 Q61081
CDC37 114562 Q63692
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Top CDC37 ELISA Kits at antibodies-online.com

Showing 3 out of 3 products:

Catalog No. Reactivity Sensitivity Range Images Quantity Delivery Price Details
  2 x 96 Tests 2 to 3 Days
  96 Tests 21 to 31 Days
  96 Tests 21 to 31 Days

More ELISA Kits for CDC37 Interaction Partners

Fruit Fly (Drosophila melanogaster) Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) interaction partners

  1. loss of function leads to defects in mitosis and male meiosis

Human Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) interaction partners

  1. The results suggested that more complicated mechanisms might be necessary to explain the phosphorylation-activated interaction of Cdc37 with various kinases.

  2. results of this integrative computational study are compared with a wide range of structural, biochemical, and cell-based experiments, offering a robust network-centric model of allosteric regulation and client kinase recognition by the Hsp90-Cdc37 chaperone machine

  3. Results found that several disease-linked mutations convert FGFR3 to a stronger client of Hsp90/Cdc37. Enhanced interaction with Cdc37 is underpinned by a weakened N-lobe network. Cdc37 binding to unrelated kinases induces their common, extensive remodeling. Kinase remodeling and the kinase/Cdc37 architecture allow recognition by Hsp90.

  4. Study showed that Cdc37 gene was up-regulated in human colorectal adenocarcinoma (CRC). Furthermore, knockdown of Cdc37 effectively reduced cell proliferation activity, enhanced apoptosis, and inhibited G1-S transition in CRC cells, and vice versa. For the mechanism, Cdc37 increased CDK4 stability to promote the phosphorylation of RB1, which finally promoted the progression of CRC.

  5. 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 phosphorylation at Y197 and specifically regulate kinase chaperoning.

  6. findings suggested that this mechanism may be exploited by the Hsp90-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation

  7. 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.

  8. Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth.

  9. Cdc37 performs a quality control of protein kinases, including b-raf, where induced conformational instability acts as a "flag" for Hsp90 dependence and stable cochaperone association.

  10. Ulk1 promoted the degradation of Hsp90-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 in response to Hsp90 inhibition in cancer cells

  11. The authors find that the interaction between sB-Raf and the Hsp90 chaperone system is based on contacts with the M domain of Hsp90, which contributes in forming the ternary complex with Cdc37 as long as the kinase is not stabilized by nucleotide.

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

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

  14. RIP3 activation following the induction of necroptosis requires the activity of an HSP90 and CDC37 cochaperone complex.

  15. Correlation between PDZK1, Cdc37, Akt and breast cancer malignancy: the role of PDZK1 in cell growth through Akt stabilization by increasing and interacting with Cdc37

  16. 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 binding.

  17. 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, but requires HSP90 activity

  18. As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins.

  19. CDC37 is a crucial HSP90-cofactor for KIT oncogenic expression in gastrointestinal stromal tumors

  20. SGK3 stability and kinase activation are regulated by the Hsp90-Cdc37 chaperone complex.

Mouse (Murine) Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) interaction partners

  1. Results showed that Cdc37 acts as a bridge to direct Hsp90 to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90, with or without binding to Hsp90, the interaction between Cdc37 and Hsp90 appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90-mediated protein maturation.

  2. Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth.

  3. A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90, are minimally sufficient to provide directionality to the chaperone cycle.

  4. Hsp90-Cdc37 complex acta as an endogenous regulator of noncanonical p38alpha activity.

  5. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells

  6. The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase pull-down assay, and the possible interaction model was suggested.

  7. JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways

  8. This growth inhibition is partially rescued by expression of ectopic Gli1, suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells.

Cow (Bovine) Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) interaction partners

  1. Cdc37 has a direct regulatory interaction with endothelial nitric oxide synthase (eNOS) and may play an important role in mediating the eNOS protein complex formation.

CDC37 Antigen Profile

Antigen 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 CDC37

  • CG12019 gene product from transcript CG12019-RA (Cdc37) antibody
  • cell division cycle 37 homolog (Cdc37) antibody
  • Hsp90 co-chaperone Cdc37 (cdc37) antibody
  • Hsp90 co-chaperone Cdc37 (AFUA_4G10010) antibody
  • Cdc37p (CDC37) antibody
  • cell division cycle 37 (CDC37) antibody
  • cell division cycle 37 (Cdc37) antibody
  • Afu4g10010 antibody
  • cdc37 antibody
  • CG12019 antibody
  • CPDR-1 antibody
  • CPDR-2 antibody
  • Dmel\\CG12019 antibody
  • DROCPDR antibody
  • E(sev)3B antibody
  • p50 antibody
  • p50Cdc37 antibody

Protein level used designations for CDC37

CG12019-PA , Cdc37-PA , 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) , p50Cdc37 , CDC37 cell division cycle 37 protein , CDC37 homolog , cell division cycle 37 protein , cell division cycle control protein 37

38232 Drosophila melanogaster
724675 Apis mellifera
2541293 Schizosaccharomyces pombe 972h-
3509722 Aspergillus fumigatus Af293
3639210 Candida albicans SC5314
11140 Homo sapiens
12539 Mus musculus
114562 Rattus norvegicus
484955 Canis lupus familiaris
100141402 Sus scrofa
520883 Bos taurus
395430 Gallus gallus
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