|The Hsp90 alpha hsp90aa1 (Catalog #MBS809355) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The Hsp90 alpha Antibody, Clone M10E3R: ATTO 680 reacts with Human and may cross-react with other species as described in the data sheet. MyBioSource\'s Hsp90 alpha can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), ELISA (EIA).
WB: 1:1000. Researchers should empirically determine the suitability of the Hsp90 alpha hsp90aa1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The Hsp90 alpha hsp90aa1 product has the following accession number(s) (GI #153792590) (NCBI Accession #NP_001017963.2) (Uniprot Accession #P07900). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
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HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively.
HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it\'s label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions - including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation.
In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9).