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HSP90AA2 antibody (Atto 390)

This Mouse Monoclonal antibody specifically detects HSP90AA2 in WB, IHC, ELISA, IF, ICC and IP. It exhibits reactivity toward Human.
Catalog No. ABIN2481715
$698.75
Plus shipping costs $50.00
200 μg
Shipping to: United States
Delivery in 3 to 5 Business Days

Quick Overview for HSP90AA2 antibody (Atto 390) (ABIN2481715)

Target

See all HSP90AA2 Antibodies
HSP90AA2 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2))

Reactivity

  • 94
  • 74
  • 43
  • 2
  • 2
  • 2
  • 2
  • 2
  • 1
Human

Host

  • 73
  • 20
  • 2
Mouse

Clonality

  • 58
  • 37
Monoclonal

Conjugate

  • 20
  • 8
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 3
  • 3
  • 3
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
This HSP90AA2 antibody is conjugated to Atto 390

Application

  • 88
  • 38
  • 31
  • 31
  • 27
  • 26
  • 26
  • 20
  • 10
  • 6
  • 4
  • 1
Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC), Immunoprecipitation (IP)

Clone

2G5-G3
  • Specificity

    Detects ~90 kDa. HSP90α-specific (>96 % α-specific by ELISA)

    Cross-Reactivity

    Human, Mouse, Rat

    Purification

    Protein G Purified

    Immunogen

    Recombinant Full Length Human HSP90alpha Protein

    Isotype

    IgG1
  • Application Notes

    • WB (1:2000)
    • ICC/IF (1:100)
    • optimal dilutions for assays should be determined by the user.

    Comment

    0.5 μg/ml of ABIN2481715 was sufficient for detection of HSP90alpha in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

    Restrictions

    For Research Use only
  • Format

    Liquid

    Concentration

    1 mg/mL

    Buffer

    PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

    Preservative

    Sodium azide

    Precaution of Use

    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Storage

    4 °C

    Storage Comment

    Conjugated antibodies should be stored at 4°C
  • Target

    HSP90AA2 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2))

    Alternative Name

    HSP90 alpha

    Background

    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.

    Gene ID

    3320

    NCBI Accession

    NP_001017963

    UniProt

    P07900
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