Product Name: HSP90
Product Number: AB-NN061-17
Size: 50 µg      Price:89.00
      $US
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: Heat shock/stress protein pan-specific antibody

Antibody Code: NN061-17

Antibody Target Type: Pan-specific

Protein UniProt: P08238

Protein SigNET: P08238

Antibody Type: Monoclonal

Antibody Host Species: Mouse

Antibody Ig Isotype Clone: IgG2b

Antibody Immunogen Source: Heat shock protein 90 from the water mold Achyla ambisexualis

Production Method: Protein G purified

Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.

Antibody Concentration: 1 mg/ml

Storage Buffer: Phosphate buffered saline pH7.4, 50% glycerol, 0.09% sodium azide

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 | Immunohistochemistry

Antibody Dilution Recommended: WB (1:1000); optimal dilutions for assays should be determined by the user.

Antibody Potency: Detects a 90 kDa protein in cell and tissue lysates by Western blotting. This antibody is reactive with both the constitutive and the inducible form of HSP90. It does not bind to the native form and does not recognize HSP90 from E.coli or yeast.

Antibody Species Reactivity: Human | Mouse | Rat | Rabbit | Chicken | Achyla | Wheat Germ | Spodoptera frugiperda

Antibody Positive Control: 1 µg/ml of SMC-112 was sufficient for detection of HSP90 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody

Related Product 1: HSP90 complex pan-specific antibody (Cat. No.: AB-NN061-18)

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 immuno-adsorption 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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.