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HSP90AA1 antibody (HRP)

HSP90AA1 Reactivity: Human, Mouse WB, IHC (p) Host: Mouse Monoclonal 3H7 HRP
Catalog No. ABIN5004954
  • Target See all HSP90AA1 Antibodies
    HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
    Reactivity
    • 69
    • 50
    • 41
    • 14
    • 13
    • 12
    • 12
    • 9
    • 9
    • 7
    • 7
    • 6
    • 5
    • 5
    • 4
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    Human, Mouse
    Host
    • 50
    • 16
    • 5
    Mouse
    Clonality
    • 49
    • 22
    Monoclonal
    Conjugate
    • 54
    • 8
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    This HSP90AA1 antibody is conjugated to HRP
    Application
    • 61
    • 22
    • 20
    • 14
    • 14
    • 13
    • 9
    • 4
    • 3
    • 2
    • 1
    • 1
    • 1
    Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
    Cross-Reactivity
    Human, Mouse
    Purification
    Purified by Protein G.
    Immunogen
    Recombinant human HSP90A Protein
    Clone
    3H7
    Isotype
    IgG
    Top Product
    Discover our top product HSP90AA1 Primary Antibody
  • Application Notes
    WB 1:300-5000
    IHC-P 1:200-400
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    1 μg/μL
    Buffer
    Aqueous buffered solution containing 0.01M TBS ( pH 7.4) with 1 % BSA, 0.03 % Proclin300 and 50 % Glycerol.
    Preservative
    ProClin
    Precaution of Use
    This product contains ProClin: a POISONOUS AND HAZARDOUS SUBSTANCE, which should be handled by trained staff only.
    Storage
    -20 °C
    Storage Comment
    Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.
    Expiry Date
    12 months
  • Target
    HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
    Alternative Name
    HSP90A (HSP90AA1 Products)
    Synonyms
    EL52 antibody, HSP86 antibody, HSP89A antibody, HSP90A antibody, HSP90N antibody, HSPC1 antibody, HSPCA antibody, HSPCAL1 antibody, HSPCAL4 antibody, HSPN antibody, Hsp89 antibody, Hsp90 antibody, LAP2 antibody, Hsp86 antibody, Hspca antibody, htpG antibody, 86kDa antibody, 89kDa antibody, AL024080 antibody, AL024147 antibody, Hsp86-1 antibody, hsp4 antibody, HSP90 antibody, HSP90AA1 antibody, fb17b01 antibody, hsp90 antibody, hsp90a antibody, hsp90a.1 antibody, hsp90alpha antibody, wu:fb17b01 antibody, zgc:86652 antibody, Hsp90alpha antibody, heat shock protein 90 alpha family class A member 1 antibody, heat shock protein 90, alpha (cytosolic), class A member 1 antibody, Heat Shock Protein 90, cytosolic antibody, heat shock protein 90A antibody, molecular chaperone antibody, heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 antibody, heat shock protein HSP 90-alpha antibody, heat shock protein 90kDa alpha (cytosolic), class A member 1 antibody, HSP90AA1 antibody, Hsp90aa1 antibody, HSP90A antibody, hsp90A antibody, hsp90aa1.1 antibody, LOC108698781 antibody
    Background

    Synonyms: Heat shock protein HSP 90-alpha, HSP90AA1, Heat shock 86 kDa, HSP 86, HSP86, Lipopolysaccharide-associated protein 2, LAP-2, LPS-associated protein 2, Renal carcinoma antigen NY-REN-38, HSP90A, HSPC1, HSPCA, HSP90AA1

    Background: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).

    Gene ID
    3320
    UniProt
    P07900
    Pathways
    M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
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