Bio-Connect

Hsp90 Antibody (OASE00019)

Research Use Only
OASE00019
Aviva Systems Biology
ApplicationsWestern Blot, ImmunoHistoChemistry, Other Application
Product group Antibodies
ReactivityChicken, Fungus, Human, Insect, Mouse, Plant, Rabbit, Rat
TargetNF1P5
Price on request
Packing Size
Large volume orders?
Order with a bulk request

Overview

  • Supplier
    Aviva Systems Biology
  • Product Name
    Hsp90 Antibody (OASE00019)
  • Delivery Days Customer
    23
  • Applications
    Western Blot, ImmunoHistoChemistry, Other Application
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    AC-16
  • Concentration
    1 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID4768
  • Target name
    NF1P5
  • Target description
    neurofibromin 1 pseudogene 5
  • Target synonyms
    neurofibromin 1-like 5; NF1L5; Putative neurofibromin 1-like protein 5
  • Host
    Mouse
  • Isotype
    IgG2b
  • Scientific 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 (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 immuno-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 (7). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.
  • Reactivity
    Chicken, Fungus, Human, Insect, Mouse, Plant, Rabbit, Rat
  • Storage Instruction
    -20°C
  • UNSPSC
    12352203