HSP90AA1
Reactivité: Humain, Souris, Rat, Lapin, Boeuf (Vache), Cobaye, Mouton, Cheval
WB, IHC
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
Optimal dilution of the HSP90 alpha antibody should be determined by the researcher.\. Western blot: 0.1-0.5 μg/mL,IHC (Paraffin): 0.5-1 μg/mL
Restrictions
For Research Use only
Buffer
0.5 mg/mL if reconstituted with 0.2 mL sterile DI water
Stock
-20 °C
Stockage commentaire
After reconstitution, the HSP90 alpha antibody can be stored for up to one month at 4°C. For long-term, aliquot and store at -20°C. Avoid repeated freezing and thawing.
Antigène
HSP90AA1
(Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
anticorps EL52, anticorps HSP86, anticorps HSP89A, anticorps HSP90A, anticorps HSP90N, anticorps HSPC1, anticorps HSPCA, anticorps HSPCAL1, anticorps HSPCAL4, anticorps HSPN, anticorps Hsp89, anticorps Hsp90, anticorps LAP2, anticorps Hsp86, anticorps Hspca, anticorps htpG, anticorps 86kDa, anticorps 89kDa, anticorps AL024080, anticorps AL024147, anticorps Hsp86-1, anticorps hsp4, anticorps HSP90, anticorps HSP90AA1, anticorps fb17b01, anticorps hsp90, anticorps hsp90a, anticorps hsp90a.1, anticorps hsp90alpha, anticorps wu:fb17b01, anticorps zgc:86652, anticorps Hsp90alpha, anticorps heat shock protein 90 alpha family class A member 1, anticorps heat shock protein 90, alpha (cytosolic), class A member 1, anticorps Heat Shock Protein 90, cytosolic, anticorps heat shock protein 90A, anticorps molecular chaperone, anticorps heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1, anticorps heat shock protein HSP 90-alpha, anticorps heat shock protein 90kDa alpha (cytosolic), class A member 1, anticorps HSP90AA1, anticorps Hsp90aa1, anticorps HSP90A, anticorps hsp90A, anticorps hsp90aa1.1, anticorps LOC108698781
Sujet
Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene. The gene, HSP90AA1, encodes the human stress-inducible 90- kDa heat shock protein alpha (Hsp90A). Complemented by the constitutively expressed paralog Hsp90B which shares over 85 % amino acid sequence identity, Hsp90A expression is initiated when a cell experiences proteotoxic stress. Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures. This molecular chaperoning ability of Hsp90A is driven by a cycle of structural rearrangements fueled by ATP hydrolysis. Current research on Hsp90A focuses in its role as a drug target due to its interaction with a large number of tumor promoting proteins and its role in cellular stress adaptation.