HSP90 alpha protein-HIS Epitope

Recombinant full length human HSP90alpha was expressed by baculovirus in Sf9 insect cells using a C-Terminal his epitope. The purity was determined to be >85% by densitometry. 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]