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HSP90AA1 antibody

The Mouse Monoclonal anti-HSP90AA1 antibody is suitable to detect HSP90AA1 in samples from Human and Rat. It has been validated for WB, IP, EIA and IHC (fro).
Catalog No. ABIN263945
$470.40
Plus shipping costs $50.00
25 μg
Shipping to: United States
Delivery in 1 to 2 Business Days

Quick Overview for HSP90AA1 antibody (ABIN263945)

Target

See all HSP90AA1 Antibodies
HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

Reactivity

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Human, Rat

Host

  • 62
  • 39
  • 5
Mouse

Clonality

  • 55
  • 51
Monoclonal

Conjugate

  • 95
  • 7
  • 2
  • 2
This HSP90AA1 antibody is un-conjugated

Application

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Western Blotting (WB), Immunoprecipitation (IP), Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro))

Clone

Hyb-K41009
  • Specificity

    Detects 90 kDa proteins corresponding to the molecular mass of HSP90alpha.

    Characteristics

    Synonyms: HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, HSP86, NY-REN-38, Heat shock protein HSP90-alpha

    Purification

    Affinity Chromatography on Protein G.

    Immunogen

    Recombinant Human HSP90 alpha.

    Isotype

    IgG2a
  • Application Notes

    ELISA (Ref.10). Immunoprecipitation. Immunohistochemistry (Ref.10). Western blot : 1 μg/mL was sufficient for detection of HSP90-alpha in 20 μg of HeLalysate.
    Other applications not tested.
    Optimal dilutions are dependent on conditions and should be determined by the user.

    Restrictions

    For Research Use only
  • Concentration

    1.0 mg/mL

    Buffer

    PBS pH 7.2 containing 50 % Glycerol as stabilizer and 0.09 % Sodium Azide as preservative.

    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

    -20 °C

    Storage Comment

    Store the antibody (in aliquots) at -20 °C.
    Shelf life: one year from despatch.

    Expiry Date

    12 months
  • Target

    HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

    Alternative Name

    HSP90AA1 / HSP90 alpha

    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: HSP86, HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, Heat shock protein HSP 90-alpha, NY-REN-38

    UniProt

    P07900

    Pathways

    M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
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