HSP90 antibody (HRP)

Catalog No. ABIN2486692

The Rabbit Polyclonal anti-HSP90 antibody has been validated for WB, IP, IHC, ELISA, IF and ICC. It is suitable to detect HSP90 in samples from Human.

Quick Overview for HSP90 antibody (HRP) (ABIN2486692)

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

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This HSP90 antibody is conjugated to HRP

Application: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)

Product Details anti-HSP90 Antibody (HRP)

Specificity: Detects ~90 kDa.

Cross-Reactivity: Human, Mouse, Rat

Purification: Protein A Purified

Immunogen: Full length protein HSP90

Application Details

Application Notes:

• WB (1:500)
• IHC (1:100)
• ICC/IF (1:100)
• optimal dilutions for assays should be determined by the user.

Comment:

A 1:500 dilution of ABIN2486692 was sufficient for detection of 0.2 mg of purified HSP90 by ECL immunoblot analysis.

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: 4 °C

Storage Comment: Conjugated antibodies should be stored at 4°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 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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Gene ID: 3326

NCBI Accession: NP_031381

UniProt: P08238

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