HSP90AA2 Protein (full length)

Catalog No. ABIN1686664

Product Details

Target: HSP90AA2 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2))

Protein Type: Recombinant

Protein Characteristics: full length

Origin: Human

Source: Escherichia coli (E. coli)

Application: Western Blotting (WB), SDS-PAGE (SDS), Surface Plasmon Resonance (SPR), Activity Assay (AcA), Drug Affinity Responsive Target Stability Assay (DARTS), Southern Blotting (SB)

Specificity: ~90 kDa

Purification: Affinity Purified

Purity: >90%

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

This product has been certified >90% pure using SDS-PAGE analysis.

Restrictions: For Research Use only

Handling

Concentration: Lot specific

Buffer: 50 mM Tris/HCl pH 7.5, 5 mM Bme, 0.3M NaCl, 10 % glycerol

Storage: -20 °C

References

Bartolini, Wainer, Bertucci, Andrisano: "The rapid and direct determination of ATPase activity by ion exchange chromatography and the application to the activity of heat shock protein-90." in: Journal of pharmaceutical and biomedical analysis, Vol. 73, pp. 77-81, (2012) (PubMed).

Gilbert, Rowley, Gomez-Acevedo, Blossom: "Coexposure to mercury increases immunotoxicity of trichloroethylene." in: Toxicological sciences : an official journal of the Society of Toxicology, Vol. 119, Issue 2, pp. 281-92, (2011) (PubMed).

Rateb, Houssen, Arnold, Abdelrahman, Deng, Harrison, Okoro, Asenjo, Andrews, Ferguson, Bull, Goodfellow, Ebel, Jaspars: "Chaxamycins A-D, bioactive ansamycins from a hyper-arid desert Streptomyces sp." in: Journal of natural products, Vol. 74, Issue 6, pp. 1491-9, (2011) (PubMed).

Target Details

Target: HSP90AA2 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2))

Alternative Name: Hsp90 alpha (HSP90AA2 Products)

Synonyms: HSP90ALPHA Protein, HSPCA Protein, HSPCAL3 Protein, heat shock protein 90 alpha family class A member 2, pseudogene Protein, HSP90AA2P Protein

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.

Molecular Weight: approx. 90 kDa

Gene ID: 3320

NCBI Accession: NP_001017963

UniProt: P07900