AR03017PU-S Heat Shock Protein 90 alpha (hsp90a) antigen
see all 11 Heat Shock Protein 90 alpha products
50 µg / US$ 335
NOVUS BIOLOGICALS
PO Box 802 Littleton, CO 80160, USA
E-Mail: novus@novus-biologicals.com
Homepage: http://www.novus-biologicals.com
PO Box 802 Littleton, CO 80160, USA
E-Mail: novus@novus-biologicals.com
Homepage: http://www.novus-biologicals.com
Quick Overview
Human Heat Shock Protein 90 alpha (hsp90a)
Synonyms
Hsp90 alpha,
Product Description
Human Heat Shock Protein 90 alpha (hsp90a)
Properties
| Presentation | Purified |
| Species | Human |
| Purity | >90% |
| Source | E. coli |
| Catalog Number | AR03017PU-S |
| Quantity | 50 µg |
| Price | US$ 335 |
| Delivery | Worldwide |
| Manufacturer | Acris Antibodies GmbH |
| Datasheet | view  AR03017PU-S.pdf |
Datasheet Extract
| Concentration | 1.6 mg/ml |
| 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). |
| Source | E. coli |
| Format | State: Liquid protein Purity: >90% pure (determined by SDS-PAGE analysis and western blot analysis), purified by multy-step chromatography BufferSystem: 20 mM Tris pH 7.5, 150 mM NaCl, 10 % glycerol |
| Applications | WB control. |
| Description | Recombinant Hsp90α cloned from a human cDNA library |
| Storage | Store at 2 - 8 °C up to one week or (in aliquots) at -20 °C for longer. Avoid repeated freezing and thawing.
Centrifuge vial before opening. Shelf life: one year from despatch. |
| References | 1. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.
2. Pearl H, et al. (2001) Adv Protein Chem 59:157-186. 3. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 4. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 5. Pratt W, Toft D. (1997) Endocr Rev 18: 306â??360. 6. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420â??434. 7. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324â??8328. |
