Cell Division Cycle 37 Homolog (S. Cerevisiae) Proteine (CDC37)

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 Antikörper (185) und und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
CDC37 11140 Q16543
CDC37 12539 Q61081
Ratte CDC37 CDC37 114562 Q63692
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Top CDC37 Proteine auf antikoerper-online.de

Showing 10 out of 19 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
Insektenzellen Maus His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 50 Days
$6,749.58
Details
Insektenzellen Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 50 Days
$6,749.58
Details
Baculovirus infected Insect Cells Human GST tag 50 μg Anmelden zum Anzeigen 14 bis 16 Tage
$382.80
Details
Baculovirus infected Insect Cells Maus GST tag,His tag 100 μg Anmelden zum Anzeigen 14 bis 16 Tage
$382.80
Details
Escherichia coli (E. coli) Human Unkonjugiert Figure annotation denotes ug of protein loaded and % gel used. 100 μg Anmelden zum Anzeigen 9 bis 11 Tage
$364.64
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Escherichia coli (E. coli) Human His tag   100 μg Anmelden zum Anzeigen 3 bis 4 Tage
$486.20
Details
HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Anmelden zum Anzeigen Verfügbar
$547.80
Details
Wheat germ Human GST tag 10 μg Anmelden zum Anzeigen 11 bis 12 Tage
$414.29
Details
Hefe Rind (Kuh) His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$3,045.17
Details
Hefe Huhn His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$3,085.50
Details

CDC37 Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human , , , ,
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Mouse (Murine) ,
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Am meisten referenzierte CDC37 Proteine

  1. Human CDC37 Protein expressed in Baculovirus infected Insect Cells - ABIN2003178 : Roiniotis, Masendycz, Ho, Scholz: Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37. in Biochemistry 2005 (PubMed)
    Show all 2 Pubmed References

Weitere Proteine zu Cell Division Cycle 37 Homolog (S. Cerevisiae) (CDC37) Interaktionspartnern

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

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

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

  1. 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.

  2. 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.

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

  4. 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.

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

  6. 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.

  7. 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

  8. 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.

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

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

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

  12. 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

  13. 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.

  14. 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

  15. 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.

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

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

  18. Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.

  19. ERK5 interacts with the Hsp90-Cdc37 chaperone in resting cells, and inhibition of Hsp90 or Cdc37 results in ERK5 ubiquitylation and proteasomal degradation.

  20. analysis of a novel interaction between the co-chaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth

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

  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) Interaktionspartner

  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 Protein Überblick

Protein Überblick

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.

Genbezeichner und Symbole assoziert mit CDC37

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

Bezeichner auf Proteinebene für 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

GENE ID SPEZIES
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
Ausgewählte Anbieter für CDC37 Proteine (CDC37)
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