Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 Proteins (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. Additionally we are shipping HSP90AA2 Antibodies (174) and many more products for this protein.

list all proteins Gene Name GeneID
HSP90AA2 3324
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Top HSP90AA2 Proteins at antibodies-online.com

Showing 4 out of 5 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Escherichia coli (E. coli) Human Un-conjugated   100 μg Log in to see 2 to 3 Days
Escherichia coli (E. coli) Human GST tag   0.1 mg Log in to see 2 to 3 Days
Escherichia coli (E. coli) Human Un-conjugated   50 μg Log in to see 5 to 8 Days
Baculovirus infected Insect Cells Human His tag   50 μg Log in to see 10 to 12 Days

HSP90AA2 Proteins by Origin and Source

Origin Expressed in Conjugate
Human ,

Top referenced HSP90AA2 Proteins

  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

More Proteins for Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2) Interaction Partners

Zebrafish Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2) interaction partners

  1. The transcriptional up-regulation of unc45b, hsp90aa1.1 and smyd1b is specific to zebrafish mutants with myosin folding defects, and is not triggered in other zebrafish myopathy models

  2. Data indicate that heat shock protein 90alpha (Hsp90alpha1) function in myosin thick filament organization is potentially regulated by post-translational modification (PTM) involving phosphorylation and acetylation.

  3. The chaperone proteins Ahsa1 (show AHSA1 Proteins) and Hsp90 (show HSP90 Proteins) promote severe craniofacial phenotypes in zebrafish model of HDR (show GATA3 Proteins) syndrome.

  4. Perturbation of the HSP70 (show HSPA1A Proteins)-HSP90 (show HSP90 Proteins) heat-shock protein axis stimulates degradation of endothelial VEGFR2 (show KDR Proteins).

  5. studies indicate that the hsp90alpha1 mutant phenotype is not simply due to disruption of myosin folding and assembly, suggesting that Hsp90alpha1 may play a role in the assembly and organization of other sarcomeric structures

  6. Mild perturbation of Hsp90 (show HSP90 Proteins) function at critical developmental stages may underpin the variable penetrance and expressivity of many developmental anomalies where the interaction between genotype and environment plays a major role.

  7. Steif/Unc-45b (show UNC45B Proteins) interacts with the chaperone Hsp90a (show HSP90AA1 Proteins) in vitro. The two genes are co-expressed in the skeletal musculature.

  8. Embryonic heat shock reveals latent hsp90 (show HSP90 Proteins) translation in zebrafish.

  9. Loss of Hsp90a (show HSP90AA1 Proteins) function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a (show HSP90AA1 Proteins) and several other genes encoding proteins that may act with Hsp90a (show HSP90AA1 Proteins) during sarcomere assembly.

  10. In response to stress or damage to the myofiber, Unc45b and Hsp90a dissociate from the Z line and transiently associate with myosin.

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

  1. Knocking out Hsp90beta (show HSP90AB1 Proteins) leads to tumour cell death. Extracellular supplementation with recombinant Hsp90alpha, but not Hsp90beta (show HSP90AB1 Proteins), protein recovers tumourigenicity of the Hsp90alpha-knockout cells. Sequential mutagenesis identifies two evolutionarily conserved lysine residues, lys (show LYZ Proteins)-270 and lys (show LYZ Proteins)-277, in the Hsp90alpha subfamily that determine the extracellular Hsp90alpha function.

  2. We revealed that Hsp90A (show HSP90AA1 Proteins) and Hsp90B (show HSP90AB1 Proteins) are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.

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

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

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

  6. Increased expression of nucleated RBC (show CACNA1C Proteins), HSP90alpha and corresponding decreased expression of HO-2 (show HMOX2 Proteins) in such hypoxic condition may play a protective role; to prevent cord blood RBC (show CACNA1C Proteins) against stress induced damage during preeclampsia.

  7. STAT5b (show STAT5B Proteins) pathway regulates Hsp90alpha expression under hypoxic conditions

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

  9. extracellular HSP90alpha transactivates EGFR/ErbB1 (show EGFR Proteins) through TLR4 (show TLR4 Proteins) and a PKCdelta (show PKCd Proteins)/c-Src (show SRC Proteins) pathway, which induces ATP release and cytosolic Ca(2 (show CA2 Proteins)+) increase and finally favors glioblastoma cell migration.

  10. High gene expression of Hsp90 alpha (show HSP90AA1 Proteins) is associated with leukemia.

HSP90AA2 Protein Profile

Protein Summary

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.

Gene names and symbols associated with HSP90AA2

  • heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 (hsp90aa1.1)
  • heat shock protein 90 alpha family class A member 2, pseudogene (HSP90AA2P)
  • fb17b01 protein
  • hsp90 protein
  • hsp90a protein
  • hsp90a.1 protein
  • HSP90ALPHA protein
  • HSPCA protein
  • HSPCAL3 protein
  • wu:fb17b01 protein
  • zgc:86652 protein

Protein level used designations for HSP90AA2

akineto , heat shock protein 90-alpha 1 , heat shock protein HSP 90-alpha 1 , slo , sloth

30591 Danio rerio
3324 Homo sapiens
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