Product Name:
HSP90
Product Number:
ab-nn061-16
Target Full Name: Heat shock protein HSP 90-beta
Target Alias: HSP84; HSP86; HSP90; HSP89; HSP90Beta; HSP90A; HSP90AA1; HSP90AB1; HSP90B; HSP90N; HSPC1; HSPC2; HSPCA; HSPCAL1; HSPCAL4; HSPCB; HSPN; LAP2
Product Type Specific: HSP90 heat shock/stress protein pan-specific antibody
Antibody Code: NN061-16
Antibody Target Type: Pan-specific
Protein UniProt: P08238
Protein SigNET: HSP90
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Immunogen Source: Full length human protein Hsp90
Production Method: Rabbit antiserum
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Storage Buffer: Rabbit antiserum
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting, ELISA, Immunoprecipitation, Immunohistochemistry, Immunofluorescence
Antibody Dilution Recommended: 1:20,000-40,000 (ECL) (WB)
Antibody Potency: Detects a ~90 kDa proteins corresponding to the molecular mass of Hsp90α/β.
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Rat | Mouse.
Antibody Positive Control: A 1:40000 dilution of SPC-104 was sufficient for detection of 0.2mg of purified hsp90 by ECL immunoblot analysis.
Related Product 1: HSP90 complex pan-specific antibody (Cat. No.: AB-NN061-18)
Related Product 2: HSP90 alpha pan-specific antibody (Cat. No.: AB-NN061-19)
Related Product 3: HSP90 alpha/beta pan-specific antibody (Cat. No.: AB-NN061-2)
Related Product 4: HSP90 pan-specific antibody (Cat. No.: AB-NN061-3)
Related Product 5: HSP90 pan-specific antibody (Cat. No.: AB-NN061-4)
Related Product 6: HSP90 (total) pan-specific antibody (Cat. No.: AB-NN061-9)
Related Product 7: HSP90 alpha pan-specific antibody (Cat. No.: AB-NN164)
Related Product 8: HSP90 beta pan-specific antibody (Cat. No.: AB-NN165)
Related Product 9: Hsp90 beta pan-specific antibody (Cat. No.: AB-NN165-1)
Related Product 10: HSP90AB1-pY484 phosphosite-specific antibody (Cat. No.: AB-PN520)
Scientific Background: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer (2). They feature three main domains: an amino-terminal domain (NTD) for ATP binding, a middle domain (MD) for client protein binding, and a carboxy-terminal domain (CTD) for dimerization. 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. Despite its 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 signalling (7-8). The number of identified proteins known to interact with HSP90 is over 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 signalling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Its activity is regulated by numerous co-chaperones (such as p60/Hop, p50Cdc37, p23) that assist in the chaperoning process. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). HSP90 is essential for cancer cell survival by stabilizing mutated or overexpressed proteins. This description may include information annotated by UniProt and/or Google AI.