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anti-Hsp 90 antibody [H90-10]

ARG20503
Arigo Biolaboratories
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry
Product group Antibodies
ReactivityHuman
TargetHSP90AB1
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Overview

  • Supplier
    Arigo Biolaboratories
  • Product Name
    anti-Hsp 90 antibody [H90-10]
  • Delivery Days Customer
    23
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    H90-10
  • Concentration
    1 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID3326
  • Target name
    HSP90AB1
  • Target description
    heat shock protein 90 alpha family class B member 1
  • Target synonyms
    D6S182; heat shock 84 kDa; heat shock 90kD protein 1, beta; heat shock protein 90 kDa; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha family class B member 1; heat shock protein HSP 90-beta; HSP84; HSP90B; HSP90-beta; HSPC2; HSPCB
  • Host
    Mouse
  • Isotype
    IgG2a
  • Scientific Description
    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). 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 S.J.H., 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 W.B. (1998) Proc Soc Exptl Biol Med 217: 420-434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324-8328.
  • Reactivity
    Human
  • Storage Instruction
    -20°C
  • UNSPSC
    12352203