Chaperonin GroEL Proteine (GroEL)

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity). Zusätzlich bieten wir Ihnen Chaperonin GroEL Antikörper (26) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
Human GroEL GroEL 3329 P10809
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Katalog Nr. Origin Quelle Konjugat Bilder Menge Lieferzeit Preis Details
Escherichia coli (E. coli) REACT_Escherichia coli Unkonjugiert Figure annotation denotes ug of protein loaded and % gel used. 100 μg 9 bis 11 Tage
Hefe REACT_Escherichia coli His tag   1 mg 60 bis 71 Tage

GroEL Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Escherichia coli (E. coli) ,

Weitere Proteine zu Chaperonin GroEL (GroEL) Interaktionspartnern

Human Chaperonin GroEL (GroEL) Interaktionspartner

  1. both HSP60 knockdown and oxidative phosphorylation (OXPHOS) inhibition by metformin decreased Erk1/2 phosphorylation and induced apoptosis and cell cycle arrest.

  2. WHO GS was found to be significantly and negatively associated with ANX2, and positively with SPINK1/TATI and Hsp60 expression.

  3. HSP60 mediates microglial IL-1beta production by regulating NLRP3 inflammasome pathway and reduction of HSP60 leads to reduction of inflammation in JEV infection.

  4. Data demonstrated that HSPD1 expression was indirectly regulated by EHMT2, and an unknown target regulated by EHMT2 modulates the downregulation of HSPD1 in breast neoplasm.

  5. Helicobacter pylori (Hp)-positive patients with gastritis or coronary heart disease produce IgG autoantibodies to a specific epitope (P1 peptide) of human heat shock protein (Hsp)60 homologous to Hp Hsp60 (HspB) in the sera. Monocytes respond to P1 by production of proinflammatory cytokines. Upregulation of proinflammatory cytokines by P1 contributes to the pathogenesis of Hp infection.

  6. High HSP60 expression is associated with disease recurrence and progression in bladder cancer.

  7. When conditioned media was immuno-depleted of Hsp60, there was a significant reduction in the release of TNF-alpha from the human umbilical vein endothelial cells.

  8. The mechanism involved in the interaction of HSP60-Ass conjugate with HLA-DR-DRB allele considering the fact that Ass (1-42) is highly immunogenic in human and interactions evoked highly robust T-cell response through MHC class II binding predictions.

  9. HSP60 showed pro-inflammatory properties in bronchial epithelial cells mediated by activation of TLR-4-related molecules.

  10. HSP60 silencing deactivates the mTOR pathway to suppress glioblastoma progression

  11. the effect of Hsp60 on differentiation and invasion of hepatocellular carcinoma cells might be associated with mitochondrial biogenesis

  12. The results demonstrate that HSP60 participates in mitochondrial progesterone synthesis. These findings provide novel insights into progesterone synthesis in the human placenta and its role in maintaining pregnancy.

  13. Clinical data showed that upregulation of miR-382/3-NT and downregulation of HSPD1/Trx were also observed in IgA nephropathy patients with renal interstitial fibrosis. These data supported a novel mechanism in which miR-382 targets HSPD1 and contributes to the redox imbalance in the development of renal fibrosis.

  14. Low HSP60 expression is associated with beta-cell hypertrophy and dysfunction.

  15. high level of ROS is needed for tumorigenesis and progression in tumors with low HSP60 expression

  16. HSP60 regulation of SOX9 ubiquitination mitigates the development of knee osteoarthritis.

  17. These findings shed some light on how a tumor cell may avert apoptosis using Hsp60 and point to the anti-cancer potential of drugs, such as CubipyOXA, which interfere with Hsp60/pC3 complex formation, and thus allow the apoptotic cascade to proceed.

  18. The associations of diabetes, combined with the polymorphisms in the genes of fat mass and obesity-associated gene (FTO), interleukin 6 (IL-6), and heat shock protein 60 (HSPD1), with breast cancer risk and survival in a Chinese Han population, was evaluated.

  19. 27-Hydroxycholesterol upregulates the production of HSP60 in monocytic cells.

  20. data indicate that HSP65 suppresses cholesterol efflux and increases cellular cholesterol content through an Lck-mediated pathway in T cells

Chaperonin GroEL (GroEL) Protein Überblick

Protein Überblick

This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13.

Genbezeichner und Symbole assoziert mit Chaperonin GroEL Proteine (GroEL)

  • heat shock protein family D (Hsp60) member 1 (HSPD1)
  • chaperonin GroEL (groEL1)
  • chaperonin GroEL (groEL)
  • chaperonin (groEL)
  • GroEL (groEL)
  • groEL (groEL)
  • Cpn60; groEL (groEL)
  • molecular chaperone GroEL (APH_RS01055)
  • CPN60 Protein
  • cpn60_1 Protein
  • GROEL Protein
  • HLD4 Protein
  • HSP-60 Protein
  • HSP60 Protein
  • HSP65 Protein
  • HuCHA60 Protein
  • SPG13 Protein

Bezeichner auf Proteinebene für Chaperonin GroEL Proteine (GroEL)

60 kDa chaperonin , 60 kDa heat shock protein, mitochondrial , P60 lymphocyte protein , chaperonin 60 , heat shock protein 65 , mitochondrial matrix protein P1 , short heat shock protein 60 Hsp60s1 , chaperonin GroEL , molecular chaperone GroEL

3329 Homo sapiens
887877 Mycobacterium tuberculosis H37Rv
923783 Mycobacterium tuberculosis CDC1551
938045 Bacillus subtilis subsp. subtilis str. 168
1005835 Buchnera aphidicola str. Sg (Schizaphis graminum)
1021559 Bifidobacterium longum NCC2705
1037522 Escherichia coli CFT073
1040731 Mycoplasma penetrans HF-2
1091466 Mycobacterium bovis AF2122/97
2865623 Bartonella henselae str. Houston-1
2866615 Bartonella quintana str. Toulouse
3171347 Anaplasma marginale str. St. Maries
3429979 Haemophilus influenzae 86-028NP
3719842 Rhodobacter sphaeroides 2.4.1
3930333 Anaplasma phagocytophilum str. HZ
4119495 Yersinia pestis Antiqua
4190456 Escherichia coli 536
4207596 Shigella flexneri 5 str. 8401
4465649 Listeria welshimeri serovar 6b str. SLCC5334
6061450 Escherichia coli str. K-12 substr. DH10B
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