Heat shock protein 90 (Hsp90α) gene is mapped to human chromosome 14q32.31. Hsp90α is an isoform of Hsp90 and is a cytoplasmic protein that comprises three domains, namely C-terminal, middle domain, and N-terminal nucleotide-binding domain. This protein is associated with membrane microdomains and lipid rafts.
Immunogen
Synthetic peptide from human HSP90AA1 / Hsp90.
Application
Anti-HSP90AA1 antibody produced in rabbit has been used in immunohistochemistry at a dilution of 1:400.
Biochem/physiol Actions
Heat shock protein 90 alpha family class A member 1 (HSP90AA1 or Hsp90α) is upregulated during stress and helps in survival from membrane stress, especially during drug targeting. It elicits cytoprotective function and mediates protein homeostasis in the cytoplasm. An elevated level of Hsp90α is observed during chronic obstructive pulmonary disease (COPD). Hsp90α also favors spermatocyte maturation and human ether-a-go-go-related gene (hERG) ion channel maturation.
Features and Benefits
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Physical form
0.02 M potassium phosphate, 0.15 M sodium chloride, pH 7.2, 0.01% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Biochimica et biophysica acta. Biomembranes, 1861(2), 457-465 (2018-12-06)
During heat shock conditions, structural changes in cellular membranes may lead to cell death. Hsp90AA1 and other heat shock proteins involved in membranes are responsible for protecting membrane stabilization. However, the membrane binding mechanism of Hsp90AA1 remains largely uncharacterized. In
Heat shock protein 90α (Hsp90α), encoded by the HSP90AA1 gene, is the stress inducible isoform of the molecular chaperone Hsp90. Hsp90α is regulated differently and has different functions when compared to the constitutively expressed Hsp90β isoform, despite high amino acid
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