Anti-?acetyl-?Heat Shock Protein HSP90 alpha (Lys294)

Anti-Heat Shock Protein HSP 90-alpha acetyl specific K294 antibody is directed against human Hsp90 protein acetylated at K294. The product was affinity purified from monospecific antiserum by immunoaffinity chromatography using acetyl-peptide coupled to agarose beads followed by solid phase adsorption against non-acetyl peptide.  While ELISA data show strong reactivity with the acetylated form of the immunizing peptide and minimal reactivity with the non-acetylated form, to date western blotting data are not definitive for acetyl K294 specificity as blots show equivalent staining of lysates from cells either treated or untreated with Trichostatin A (an HDAC inhibitor).  A BLAST analysis was used to suggest cross-reactivity with Hsp90 from human, mouse, rat, monkey, chicken and Drosophila based on 100% homology with the immunizing sequence.  Reactivity of this antibody with Hsp90 from other species is unknown. 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. [The UniProt Consortium]