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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€
|
If you have any questions, please use our Contact Form.
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
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 |
Database Information
KEGG ID : | K04079 | Matching products |
UniProt ID : | P07900 | Matching products |
Gene ID | GeneID 3320 | Matching products |
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!
Our products are for laboratory research use only: Not for administration to humans!
Information about the product reference will follow.
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