Product Name:
HSP90
Product Number:
ab-nn061-16
Target Full Name: Heat shock protein HSP 90-beta
Target Alias: Hsp84; Hsp86; Hsp90A; Hsp90AA1; Hsp90AB1; Hsp90B; HspC1; HspC2; HspCAL1; HspCAL4; Hsp90N
Product Type Specific: Heat shock/stress protein pan-specific antibody
Antibody Code: NN061-16
Antibody Target Type: Pan-specific
Protein UniProt: P08238
Protein SigNET: P08238
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Immunogen Source: Full length human protein Hsp90
Antibody Modification: Heat shock/stress protein pan-specific antibody
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: 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 a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). 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 signaling (5-6). 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 (7).
