HSP90AA1 antibody

Catalog No. ABIN263946

The Mouse Monoclonal anti-HSP90AA1 antibody (Clone 8D3) (ABIN263946) specifically detects HSP90AA1 in IP. The antibody is reactive with Human, Mouse, Rat and Rabbit samples.

Quick Overview for HSP90AA1 antibody (ABIN263946)

Target: HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

Reactivity: Human, Mouse, Rat, Rabbit

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP90AA1 antibody is un-conjugated

Application: Immunoprecipitation (IP)

Clone: 8D3

Product Details anti-HSP90AA1 Antibody

Specificity: Immunoprecipitates 90 kDa proteins corresponding to the molecular mass of hsp90. Coimmunoprecipitates hsp90 complexes, including hsp70, Hop, Ah receptors (8), glucocorticoid receptors (9), heme-regulated eukaryotic initiation factor 2alpha (eIF- 2alpha) kinase (HRI) (10).

Characteristics: Synonyms: Hsp90 complex

Purification: PEG purified

Immunogen: Ah receptor (Aryl hydrocarbon receptor) (8)

Isotype: IgM

Application Details

Application Notes: Immunoprecipitation (Best results associated with use of goat anti-mouse IgM beads).

Restrictions: For Research Use only

Handling

Concentration: 1.0 mg/mL

Buffer: PBS in 0.09 % sodium azide in 50 % glycerol

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/-20 °C

Storage Comment: Store the antibody at 2 - 8 °C up to one month or (in aliquots) at -20 °C for longer. Avoidrepeated freezing and thawing.
Shelf life: one year from despatch.

Expiry Date: 12 months

Target Details for HSP90AA1

Target: HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

Alternative Name: HSP90AA1 / HSP90 alpha

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).Synonyms: Hsp90 complex

Gene ID: 3320

UniProt: P07900

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