Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 Proteine (HSP90AA2)

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Zusätzlich bieten wir Ihnen HSP90AA2 Antikörper (169) und viele weitere Produktgruppen zu diesem Protein an.

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HSP90AA2 3324
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Showing 4 out of 6 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Lieferzeit Preis Details
Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 30 bis 35 Tage
Escherichia coli (E. coli) Human Unkonjugiert   100 μg 3 bis 4 Tage
Escherichia coli (E. coli) Human GST tag   0.1 mg 2 bis 3 Tage
Baculovirus infected Insect Cells Human His tag   20 μg 1 bis 2 Tage

HSP90AA2 Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human , ,

Am meisten referenzierte HSP90AA2 Proteine

  1. Human HSP90AA2 Protein expressed in Escherichia coli (E. coli) - ABIN1686664 : Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. in The Journal of biological chemistry 2003 (PubMed)
    Show all 10 Pubmed References

Weitere Proteine zu Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2) Interaktionspartnern

Human Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2) Interaktionspartner

  1. Study suggests that HSP90AA2 gene polymorphisms are associated with SLE susceptibility in Chinese population.

  2. The Hsp90alpha binds human recombinant p23 about three times stronger than Hsp90beta but with significantly smaller exothermic enthalpy as determined by isothermal titration calorimetry of direct binding between the purified proteins.

  3. Knocking out Hsp90beta leads to tumour cell death. Extracellular supplementation with recombinant Hsp90alpha, but not Hsp90beta, protein recovers tumourigenicity of the Hsp90alpha-knockout cells. Sequential mutagenesis identifies two evolutionarily conserved lysine residues, lys-270 and lys-277, in the Hsp90alpha subfamily that determine the extracellular Hsp90alpha function.

  4. We revealed that Hsp90A and Hsp90B are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.

  5. Heat shock protein 90 stimulates rat mesenchymal stem cell migration via PI3K/Akt and ERK1/2 pathways

  6. Studied the serum prolactin, cortisol, and ACTH stress response of intensive care unit (ICU) patients with severe sepsis/septic shock (SS) or systemic inflammatory response syndrome (SIRS) compared to healthy subjects.

  7. These results indicate that cytoplasmic HSP90alpha may serve as a biomarker for perineural invasion in pancreatic cancer

  8. Increased expression of nucleated RBC, HSP90alpha and corresponding decreased expression of HO-2 in such hypoxic condition may play a protective role; to prevent cord blood RBC against stress induced damage during preeclampsia.

  9. Heat shock protein 90alpha is a substrate and chaperone of DNA-PK necessary for the apoptotic response.

  10. STAT5b pathway regulates Hsp90alpha expression under hypoxic conditions

  11. HSP90alpha was an IMH-2 epitope-associated protein. Tumor HSP90alpha overexpression was correlated with the metastasis and poor prognosis of colorectal cancer patients.

  12. extracellular HSP90alpha transactivates EGFR/ErbB1 through TLR4 and a PKCdelta/c-Src pathway, which induces ATP release and cytosolic Ca(2+) increase and finally favors glioblastoma cell migration.

  13. High gene expression of Hsp90 alpha is associated with leukemia.

  14. extracellular Hsp90alpha promotes angiogenesis in an MMP-2-dependent manner.

  15. that Hsp90alpha can be secreted by activated endothelial cells and is a positive regulator of angiogenesis, suggesting the potential application of Hsp90alpha as a stimulator for wound repair.

  16. Promoter activity analysis revealed that hepatitis B virus X protein is directly involved in the c-Myc-mediated transcriptional activation of HSP90alpha.

  17. The hsp90 alpha isoform, but not hsp90 beta, is expressed extracellularly where it interacts with the matrix metalloproteinase 2 (MMP2). Inhibition of extracellular hsp90 alpha decreases both MMP2 activity and invasiveness.

  18. The reciprocal interactions of HSP90 and NF-kappa B activities are likely to constitute a regulatory loop, able to influence cell survival and response to stressful agents

  19. These findings provide a rationale for targeting HSP90alpha protein as a therapeutic candidate for glioma.

  20. C-terminal tail and determinants in the alphaE-helix of the catalytic domain allows the chaperones Hsp90 and Cdc37 to bind newly synthesized PKC beta II, a required event in the processing of PKC by phosphorylation

HSP90AA2 Protein Überblick

Protein Überblick

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.

Genbezeichner und Symbole assoziert mit HSP90AA2

  • heat shock protein 90 alpha family class A member 2, pseudogene (HSP90AA2P)
  • HSP90ALPHA Protein
  • HSPCA Protein
  • HSPCAL3 Protein
3324 Homo sapiens
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