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
Beschränkungen
Nur für Forschungszwecke einsetzbar
Buffer
0.5 mg/mL if reconstituted with 0.2 mL sterile DI water
Lagerung
-20 °C
Informationen zur Lagerung
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.
Target
HSP90AA1
(Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
EL52 antikoerper, HSP86 antikoerper, HSP89A antikoerper, HSP90A antikoerper, HSP90N antikoerper, HSPC1 antikoerper, HSPCA antikoerper, HSPCAL1 antikoerper, HSPCAL4 antikoerper, HSPN antikoerper, Hsp89 antikoerper, Hsp90 antikoerper, LAP2 antikoerper, Hsp86 antikoerper, Hspca antikoerper, htpG antikoerper, 86kDa antikoerper, 89kDa antikoerper, AL024080 antikoerper, AL024147 antikoerper, Hsp86-1 antikoerper, hsp4 antikoerper, HSP90 antikoerper, HSP90AA1 antikoerper, fb17b01 antikoerper, hsp90 antikoerper, hsp90a antikoerper, hsp90a.1 antikoerper, hsp90alpha antikoerper, wu:fb17b01 antikoerper, zgc:86652 antikoerper, Hsp90alpha antikoerper, heat shock protein 90 alpha family class A member 1 antikoerper, heat shock protein 90, alpha (cytosolic), class A member 1 antikoerper, Heat Shock Protein 90, cytosolic antikoerper, heat shock protein 90A antikoerper, molecular chaperone antikoerper, heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 antikoerper, heat shock protein HSP 90-alpha antikoerper, heat shock protein 90kDa alpha (cytosolic), class A member 1 antikoerper, HSP90AA1 antikoerper, Hsp90aa1 antikoerper, HSP90A antikoerper, hsp90A antikoerper, hsp90aa1.1 antikoerper, LOC108698781 antikoerper
Hintergrund
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.