Anti-HSP90

0.5mg/ml if reconstituted with 0.2ml sterile DI water. 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. Protein function: 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. 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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. [The UniProt Consortium]