HSP90 antibody

Catalog No. ABIN361712

This Mouse Monoclonal antibody specifically detects HSP90 in WB, IHC and AA. It exhibits reactivity toward Water Mold.

Quick Overview for HSP90 antibody (ABIN361712)

Target: HSP90 (Heat Shock Protein 90 (HSP90))

Reactivity: Water Mold

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP90 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), Antibody Array (AA)

Clone: AC-16

Product Details anti-HSP90 Antibody

Specificity: Detects 90 kDa. 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.

Cross-Reactivity: Chicken, Fusarium, Human, Insect, Mouse, Plant, Rabbit, Rat

Purification: Protein G Purified

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

Isotype: IgG2b

Application Details

Application Notes:

• WB (1:1000)
• IHC (1:2000)
• optimal dilutions for assays should be determined by the user.

Comment:

1 μg/ml of ABIN361711 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

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: -20°C

Target Details for HSP90

Target: HSP90 (Heat Shock Protein 90 (HSP90))

Alternative Name: HSP90

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). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Gene ID: 4768

UniProt: Q8LLI5

Pathways: M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals