Hsp90 (total) Antibody
Cat# OASE00068
Size : 50ug
Marca : Aviva Systems Biology
Contatta il distributore locale :
Telefono : +1 850 650 7790
| Datasheets/Manuals | Printable datasheet for OASE00068 |
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| Predicted Species Reactivity | Human, Mouse, Rat, Plant |
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| Product Format | Liquid. In PBS pH7.2, 50% glycerol, 0.09% sodium azide. |
| Clonality | Monoclonal |
| Clone | 4F3.E8 |
| Isotype | IgG2a |
| Host | Mouse |
| Conjugation | Unconjugated |
| Application | WB, IHC, ICC, IF, IP, ELISA |
| :: | Certificate of Analysis: 0.5 ug/mL was sufficient for detection of Hsp90alpha in 20ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody. |
| Reconstitution and Storage | Store at -20C. Shipping with Blue Ice or 4C. |
| Immunogen | Recombinant Human HSP90 purified from E.coli |
| Purification | Protein G Purified |
| Concentration | 1 mg/ml |
| Specificity | Detects ~90kDa. This antibody detects both α and β forms of HSP90 equally well. |
| Dilution | WB (1:2000), IHC (1:100), ICC/IF (1:100); optimal dilutions for assays should be determined by the user. |
| Application Info | 1:2000 (Western Blot) |
| Storage Buffer | PBS pH7.2, 50% glycerol, 0.09% sodium azide |
| Description | HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 â€â -regulated proteins that have been discovered to date are involved in cell signaling (7-8). 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 (9). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca. |
| Reference | 1. Nemoto, T. et al. (1997) J.Biol Chem. 272, 26179-26187. 2. Minami, Y, et al. (1991), J.Biol Chem. 266, 10099-10103. 3. Arlander SJH, et al. (2003) J Biol Chem 278, 52572-52577. 4. Pearl H, et al. (2001) Adv Protein Chem 59,157-186. 5. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 6. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 7. Pratt W, Toft D. (1997) Endocr Rev 18,306–360. 8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217, 420–434. 9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91, 8324–8328. 10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5), 881-889. |
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| Gene Symbol | HSP90 |
| Gene Full Name | heat shock protein 90kDa alpha (cytosolic), class A member 1 |
| Alias Symbols | HSP84, HSP86, HSP90A, HSP90AA1, HSP90AB1, HSP90B, HSPC1, HSPC2, HSPCAL1, HSPCAL4 |
| NCBI Gene Id | 3320 |
| Description of Target | HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). 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 (9). |
| Uniprot ID | P07900 |
| Protein Accession # | NP_001017963.2 |
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What is the species homology for "Hsp90 (total) Antibody (OASE00068)"?
The tested species reactivity for this item is "". This antibody is predicted to have homology to "Human, Mouse, Rat, Plant".
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How long will it take to receive "Hsp90 (total) Antibody (OASE00068)"?
This item is available "Domestic: within 1-2 weeks delivery | International: 1-2 weeks".
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What buffer format is "Hsp90 (total) Antibody (OASE00068)" provided in?
This item is provided in "Liquid. In PBS pH7.2, 50% glycerol, 0.09% sodium azide.".
Additional format options may be available. For more information please contact info@avivasysbio.com. -
What are other names for "Hsp90 (total) Antibody (OASE00068)"?
This target may also be called "HSP84, HSP86, HSP90A, HSP90AA1, HSP90AB1, HSP90B, HSPC1, HSPC2, HSPCAL1, HSPCAL4" in publications.
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What is the shipping cost for "Hsp90 (total) Antibody (OASE00068)"?
The shipping cost for this item is within the US. Please contact us for specific shipping for international orders.
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What is the guarantee for "Hsp90 (total) Antibody (OASE00068)"?
All Aviva products have been through rigorous validations and carry 100% satisfaction guarantee.
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Can I get bulk pricing for "Hsp90 (total) Antibody (OASE00068)"?
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 (total) Antibody (OASE00068)"?
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.