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Datasheets/Manuals | Printable datasheet for OASE00053 |
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Predicted Species Reactivity | Human, Mouse, Rat, Bovine, Pig, Rabbit, Chicken |
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Clonality | Monoclonal |
Clone | D7A |
Isotype | IgG1 |
Host | Mouse |
Conjugation | Unconjugated |
Application | WB, IHC, IP, ELISA, AM |
Additional Information | Background Info: Recognizes 90kDa proteins corresponding to the molecular mass of Hsp90. Hsp90alpha specific for human samples. Can isolate complexes of Hsp90, Src kinase and cec37. |
:: | Scientific 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 (4-7). 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 (8-9). The number of proteins now known 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(6). 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 immune-adsorption 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 (10). |
:: | Certificate of Analysis: 2ug/ml was sufficient for detection of Hsp90alpha in 20ug of heat shocked HeLa cell lysate as well as in 100ng oh human Hsp90alpha protein by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary. |
Reconstitution and Storage | Store at -20C. Shipping with Blue Ice or 4C. |
Immunogen | Full length protein HSP90 purified from chicken brain |
Purification | Protein G Purified |
Concentration | 1 mg/ml |
Specificity | Recognizes 90kDa. Can isolate complexes of HSP90, Src kinase and cec37. |
Dilution | WB (1:500), IP (5ug) ; optimal dilutions for assays should be determined by the user. |
Storage Buffer | PBS pH7.2, 50% glycerol, 0.09% sodium azide |
Reference | 1. Schuh S. et al. (1985) J Biol Chem. 260 (26): 14292-14296. 2. Lipsich L.A., Cutt J.R. and Brugge J.S. (1982) Mol. Cell Biol. 2(7): 875-880. 3. Brugge J.S., Yonemoto W., and Darrow D. (1983) Mol. Cell. Biol. 3(1): 9-19. 4. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577. 5. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186. 6. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 7. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 8. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360. 9. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434. 10. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328. |
Description | 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 (4-7). 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 (8-9). The number of proteins now known 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(6). 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 immune-adsorption 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 (10). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca. |
Gene Symbol | HSP90 |
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Gene Full Name | bromodomain adjacent to zinc finger domain, 1B |
Alias Symbols | HSP86, HSP89A, HSP90A, HSP90AA1, HSPC1, HSPCA, HsoCAL3 |
NCBI Gene Id | 9031 |
Uniprot ID | P11501 |
Protein Accession # | NP_001103255.1 |
- Protocol:
- Reconstitution & Storage Instructions
- Western Blotting/Immunoblotting (WB/IB) Protocol
- Immunohistochemistry (IHC) Protocol
- Immunocytochemistry (ICC) Protocol
- Enzyme-Linked ImmunoSorbent Assay (ELISA) Protocol
- Blocking Peptide Competition Protocol (BPCP)
- Immunoprecipitation (IP) Protocol
- Antibody Array (AA) Protocol
- Tips Information:
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See our General FAQ page.
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What is the species homology for "Hsp90 Antibody (OASE00053)"?
The tested species reactivity for this item is "". This antibody is predicted to have homology to "Human, Mouse, Rat, Bovine, Pig, Rabbit, Chicken".
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How long will it take to receive "Hsp90 Antibody (OASE00053)"?
This item is available "Domestic: within 1-2 weeks delivery | International: 1-2 weeks".
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What buffer format is "Hsp90 Antibody (OASE00053)" provided in?
This item is provided in "".
Additional format options may be available. For more information please contact info@avivasysbio.com. -
What are other names for "Hsp90 Antibody (OASE00053)"?
This target may also be called "HSP86, HSP89A, HSP90A, HSP90AA1, HSPC1, HSPCA, HsoCAL3" in publications.
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What is the shipping cost for "Hsp90 Antibody (OASE00053)"?
The shipping cost for this item is $40 within the US. Please contact us for specific shipping prices for international orders.
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What is the guarantee for "Hsp90 Antibody (OASE00053)"?
All Aviva products have been through rigorous validations and carry 100% satisfaction guarantee.
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Can I get bulk pricing for "Hsp90 Antibody (OASE00053)"?
You can get bulk pricing for this item by going here.
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What is the molecular weight of the protein?
The molecular weight reported by Uniprot for this item is "".
Please note observed molecular weights in western blot applications may differ depending on a variety of protein characteristics. -
What protocols are available for "Hsp90 Antibody (OASE00053)"?
We may have detailed protocol data avaialble for this item. To learn more, please view the "Protocols & Data" tab on the product page.
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What are positive controls for "HSP90"?
We have listed RNA Seq and gene expression data in the "Target Info" tab. You may be able to find adequate positive controls there.
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What are negative controls for "HSP90"?
We have listed RNA Seq and gene expression data in the "Target Info" tab. You may be able to find adequate positive controls there.
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What other proteins interact with "HSP90"?
This protein has been reported to interact with "Protein Interactions". Please view the "Related Categories" tab on the product page for more information.
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What biological processes are associated with "HSP90"?
This protein has been associated with "Biological Processes". Please view the "Related Categories" tab on the product page for more information.
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What cellular components are associated with "HSP90"?
This protein has been associated with "Cellular Components". Please view the "Related Categories" tab on the product page for more information.
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What protein functions are associated with "HSP90"?
This protein has been associated with "Protein Functions". Please view the "Related Categories" tab on the product page for more information.