HSP90 antibody (APC)

Catalog No. ABIN2481300

This anti-HSP90 antibody is a Mouse Monoclonal antibody detecting HSP90 in WB, IP, IHC, ELISA, IF and ICC. Suitable for Human.

Quick Overview for HSP90 antibody (APC) (ABIN2481300)

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

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP90 antibody is conjugated to APC

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

Clone: 4F3-E8

Product Details anti-HSP90 Antibody (APC)

Specificity: Detects ~90 kDa. This antibody detects both α and β forms of HSP90 equally well.

Cross-Reactivity: Human, Mouse, Plant, Rat

Purification: Protein G Purified

Immunogen: Recombinant Human HSP90 purified from E.coli

Isotype: IgG2a

Application Details

Application Notes:

• WB (1:2000)
• IHC (1:100)
• ICC/IF (1:100)
• optimal dilutions for assays should be determined by the user.

Comment:

0.5 μg/ml of ABIN2481300 was sufficient for detection of HSP90alpha 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 7.2, 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 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). 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. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). 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 (9). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Gene ID: 3320

NCBI Accession: NP_001017963

UniProt: P07900

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