HSP90AA1 antibody

Catalog No. ABIN7540485

Supplier Product No.: 200-301-f75

Product Details anti-HSP90AA1 Antibody

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

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP90AA1 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF)

Supplier Product No.: 200-301-f75

Supplier: Rockland

Purpose: HSP90 alpha/beta Antibody

Cross-Reactivity (Details): A BLAST analysis was used to suggest cross-reactivity with Hsp90αβ from Human, Rat, Liver, S.

Purification: Anti-Hsp90αβ Antibody was purified by Protein G chromatography.

Sterility: Sterile filtered

Immunogen: Hsp90 alpha beta Antibody was produced in mice by repeated immunizations raised against recombinant human Hsp90alpha.

Clone: Hyb-K41220A

Isotype: IgG2a

Application Details

Application Notes:

ELISA_Dilution: 1:200

Western_Blot_Dilution: 1 μg/mL

Comment:

Anti-Hsp90αβ Antibody is tested for WB, ELISA, IF, and IHC. Expect a band approximately 90kD proteins corresponding to the molecular mass of hsp90 α or β on SDS Page immunoblots. Specific conditions for reactivity should be optimized by the end user.

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer:

Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

Stabilizer: 50 % (v/v) Glycerol

Preservative: 0.09 % (w/v) Sodium Azide

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 vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.

Expiry Date: 12 months

Target Details for HSP90AA1

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

Alternative Name: HSP90AA1 (HSP90AA1 Products)

Background: Anti-Hsp90αβ, Hsp86, Hsp89A, Hsp90AA1, Hsp90Alpha, HspC1, HSPCA, HspCAL3, Heat shock protein HSP 90-alpha, Heat shock 86 kDa, HSP 86, HSP86, Renal carcinoma antigen NY-REN-38, HSP90AA1, HSP90A, HSPC1, HSPCA,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. Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. 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. 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. 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.

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