Heat shock protein 90 is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. Inhibitors of it are investigated as anti-cancer drugs. Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species. HSP90 acts as a capacitor for morphologic evolution through epigenetic and genetic mechanisms. It is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including HER2/ERBB2, AKT, RAF1, BCR-ABL, and mutated p53. Although it is highly expressed in most cells, HSP90 inhibitors selectively kill cancer cells compared to normal cells, and the the inhibitor 17-allylaminogeldanamycin (17-AAG) exhibited antitumor activity in preclinical models.
Formulation
0.5mg/ml if reconstituted with 0.2ml sterile DI water
Host
Rabbit
Immunogen Region
Human partial recombinant protein (AA 2-365) was used as the immunogen for this HSP90 antibody.
Isotype
IgG
Predicted Reactivity
Human, Mouse, Rat
Reactivity
Human, Mouse, Rat
Recombinant
No
Gene Id
3320
Format
Antigen affinity purified
Purification
Antigen affinity
Storage
After reconstitution, the HSP90 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.
Applications
WB, IHC-P, ICC
Dilution
Western blot: 0.5-1ug/ml,Immunohistochemistry (FFPE): 0.5-1ug/ml,Immunocytochemistry: 0.5-1ug/ml