HSP90AA1 / HSP90 alpha Mouse Monoclonal Antibody [Clone ID: Hyb-K41009]

CAT#: AM03143PU-N

HSP90AA1 / HSP90 alpha mouse monoclonal antibody, clone Hyb-K41009, Purified

Specifications

Product Data

• Clone Name: Hyb-K41009
• Applications: ELISA, IHC, IP, WB
• Recommended Dilution: ELISA (Ref.10).
  Immunoprecipitation.
  Immunohistochemistry (Ref.10).
  Western blot (Ref.1): 1 µg/ml was sufficient for detection of HSP90-alpha in 20 µg of HeLa lysate.
• Reactivities: Human, Rat
• Host: Mouse
• Isotype: IgG2a
• Clonality: Monoclonal
• Immunogen: Recombinant Human HSP90 alpha.
• Specificity: Detects 90kD proteins corresponding to the molecular mass of HSP90alpha.
• Formulation: PBS pH 7.2 containing 50% Glycerol as stabilizer and 0.09% Sodium Azide as preservative.
  State: Purified
  State: Liquid purified Ig fraction.
• Concentration: lot specific
• Purification: Affinity Chromatography on Protein G.
• Storage: Store the antibody (in aliquots) at -20°C.
• Stability: Shelf life: one year from despatch.
• 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, HSP90A exists predominantly as a homodimer while HSP90B 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-hhaperones 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).
• Synonyms: HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, HSP86, NY-REN-38, Heat shock protein HSP 90-alpha
• Note: Predicted molecular weight: 95 kDa.