HSP90
HSP90 (heat shock protein HSP 90-alpha, encoded by HSP90AA1) is an inducible molecular chaperone that works as a homodimer and helps specific target proteins fold correctly. It is also known as Hsp89, HSPC1 and HSPCA. Browse Assay Genie's current range of HSP90 research reagents below, or read on for the biology behind the target.
HSP90 is an inducible molecular chaperone that functions as a homodimer. It aids the proper folding of specific target proteins through an ATPase activity, and this activity is modulated by co-chaperones. The enzyme is classified under EC 3.6.4.10. The protein belongs to the heat shock protein 90 family, and the HGNC places its gene in the group of heat shock 90kDa proteins.
The HSP90AA1 gene encodes the alpha isoform, formally named heat shock protein 90 alpha family class A member 1. UniProt records the protein in the nucleus, cytoplasm, melanosome, cell membrane and mitochondrion. NCBI Gene reports two transcript variants that encode different isoforms. Orthologous genes, both named Hsp90aa1, are present in mouse and rat, which allows comparative work in rodent models.
The gene has carried several earlier names and symbols, including heat shock 90kD protein 1, alpha, as well as HSPCA, HSPC1, HSP90N, HSPCAL4 and FLJ31884. Searches of the literature may therefore return any of these terms. UniProt also notes a role in microbial infection: HSP90 appears to interfere with NadA-mediated invasion of human cells by N. meningitidis. Lowering HSP90 levels increases adhesion and entry of NadA-expressing E. coli into human Chang cells, whereas raising its levels reduces adhesion and invasion.
HSP90 folds specific target proteins using an ATPase activity modulated by co-chaperones, making it a core subject in chaperone mechanism studies.
As an inducible chaperone, HSP90 is studied in the heat shock response and in how cells regulate chaperone levels.
HSP90 levels influence adhesion and invasion of human cells by NadA-expressing bacteria, a link relevant to Neisseria meningitidis infection biology.
The ATPase activity of the HSP90 homodimer and its modulation by co-chaperones provide a basis for enzymology and regulation studies.
HSP90 is an inducible molecular chaperone that acts as a homodimer. It helps specific target proteins fold properly through an ATPase activity that co-chaperones modulate. UniProt also reports that it seems to interfere with NadA-mediated invasion of human cells by N. meningitidis.
HSP90AA1 is also called Hsp89, Hsp90, HSPC1, HSPCA, HSPCAL4, HSP90N and FLJ31884. Earlier names include heat shock 90kD protein 1, alpha. NCBI Gene reports two transcript variants encoding different isoforms of the protein.
Yes. Mouse and rat both carry an ortholog named Hsp90aa1, so the human HSP90 gene can be studied in rodent models. The protein belongs to the heat shock protein 90 family. Check the datasheet of any product for its validated reactivity.
Other heat shock proteins and chaperones, including HSP90 family, HSP70 family and small heat shock proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P07900; product specifications from Assay Genie datasheets.