Hsp90 alpha Antibody (OASE00066)

Catalog No: OASE00066 (Formerly GWB-D79D81)

Size:50ug

Western Blot analysis of Rat tissue lysate showing detection of Hsp90 alpha protein using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone 2G5.G3. Load: 15 ug. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.

Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone 2G5.G3. Tissue: HaCaT cells. Species: Human. Fixation: Cold 100% methanol for 10 minutes at -20C. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT.

Product Info

• Predicted Species Reactivity: Human, Mouse, Rat
• Clonality: Monoclonal
• Clone: 2G5.G3
• Isotype: IgG1
• Host: Mouse
• Conjugation: Unconjugated
• Application: WB, IHC, ICC, IF, IP, ELISA
• Additional Information: Background Info: Hsp90alpha-specific (>96% alpha-specific by ELISA)
  Scientific Background: 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).
  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 Full Length Human HSP90alpha Protein
• Purification: Protein G Purified
• Concentration: 1 mg/ml
• Specificity: Detects ~90kDa. HSP90α-specific (>96% α-specific by ELISA)
• Dilution: WB (1:2000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.
• Storage Buffer: PBS pH7.2, 50% glycerol, 0.09% sodium azide
• 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.
• 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 – 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). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Target Info

• Gene Symbol: HSP90 alpha
• Gene Full Name: heat shock protein 90kDa alpha (cytosolic), class A member 1
• Alias Symbols: HSP86, HSP89A, HSP90AA1, HSP90Alpha, HSPC1, HSPCA, HSPCAL3
• NCBI Gene Id: 3320
• Uniprot ID: P07900
• Protein Accession #: NP_001017963.2