Heat Shock Protein 90 alpha, Recombinant, Human (HSP90a)

Heat Shock Protein 90 alpha, Recombinant, Human (HSP90a)
Item number Size Datasheet Manual SDS Delivery time Quantity Price
H1832-85B.50 50 µg - -

3 - 19 business days*

395.00€
H1832-85B.100 100 µg - -

3 - 19 business days*

482.00€
 
Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic... more
Product information "Heat Shock Protein 90 alpha, Recombinant, Human (HSP90a)"
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:, Recombinant Hsp90a cloned from a human cDNA library expressed in E.coli , Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20°C. Aliquots are stable for at least 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Keywords: HSP86, LAP-2, HSP90A, HSP 86, HSP90AA1, Heat shock 86 kDa, LPS-associated protein 2, Heat shock protein HSP 90-alpha, Renal carcinoma antigen NY-REN-38, Lipopolysaccharide-associated protein 2
Supplier: United States Biological
Supplier-Nr: H1832-85B

Properties

Application: WB
Conjugate: No
Species reactivity: human
Format: Highly Purified

Handling & Safety

Storage: -20°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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