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HSP90 Antibody

     
  •  - HSP90 Antibody ASM10358
    Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-Hsp90 Polyclonal Antibody (ASM10358). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Hsp90 Polyclonal Antibody (ASM10358) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp90 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.
    detail
  • WB - HSP90 Antibody ASM10358
    Western blot analysis of Human Cell line lysates showing detection of HSP90 protein using Rabbit Anti-HSP90 Polyclonal Antibody (ASM10358). Load: 2 µg Hsp90beta. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Rabbit Anti-HSP90 Polyclonal Antibody (ASM10358) at 1:10000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.
    detail
  • IHC - HSP90 Antibody ASM10358
    Immunohistochemistry analysis using Rabbit Anti-HSP90 Polyclonal Antibody (ASM10358). Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative Solution. Primary Antibody: Rabbit Anti-HSP90 Polyclonal Antibody (ASM10358) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:50 for 1 hour at RT. Localization: Cytoplasm.
    detail
  •  - HSP90 Antibody ASM10358
    Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-Hsp90 Polyclonal Antibody (ASM10358). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Hsp90 Polyclonal Antibody (ASM10358) at 1:100 for 12 hours at 4°C. Secondary Antibody: APC Goat Anti-Rabbit (red) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp90 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.
    detail
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
WB, IHC, IP, ICC
Primary Accession P08238
Other Accession NP_031381.2
Host Rabbit
Reactivity Human, Mouse, Rat
Clonality Polyclonal
Description Rabbit Anti-Human HSP90 Polyclonal
Target/Specificity Detects ~90kDa.
Other Names HSP84 Antibody, HSP86 Antibody, HSP90A Antibody, HSP90AA1 Antibody, HSP90AB1 Antibody, HSP90B Antibody, HSPC1 Antibody, HSPC2 Antibody, HSPCAL1 Antibody, HSPCAL4 Antibody, HSP90N Antibody
Immunogen Full length protein HSP90
Purification Protein A Purified
Storage -20ºC
Storage Buffer PBS pH 7.4, 50% glycerol, 0.09% sodium azide
Shipping Temperature Blue Ice or 4ºC
Certificate of Analysis A 1:500 dilution of SPC-104 was sufficient for detection of 0.2 mg of purified HSP90 by ECL immunoblot analysis.
Cellular Localization Cytoplasm | Melanosome
Research Areas
Citations (0)
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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 (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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.

References

1. Arlander S.J.H., et al. (2003) J Biol Chem 278: 52572-52577.
2. Pearl H., et al. (2001) Adv Protein Chem 59:157-186.
3. Neckers L., et al. (2002) Trends Mol Med 8:S55-S61.
4. Pratt W., Toft D. (2003) Exp Biol Med 228:111-133.
5. Pratt W., Toft D. (1997) Endocr Rev 18: 306–360.
6. Pratt W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434.
7. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328.

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Cat# ASM10358
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