This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI) and is suitable for Cancer, Immunology and Nuclear Signaling research. Hsp90 is a member of the heat shock protein 90 family, the members of which are highly conserved between isoforms and species. Hsp90 functions as a molecular chaperone and has ATPase activity. Hsp90 is a cytoplasmic protein that forms a homodimer in vivo and interacts with TOM34, AHSA1, HDAC6 and SMYD3. Several signal transduction pathways depend on Hsp90 function, including pathways involving erbB2, hypoxia sensitivity (Hif1 alpha), and steroid hormone receptors (for example, androgen, progesterone, glucocorticoid, and aryl-hydrocarbon). Recent reports show that Hsp90 from tumor cells has increased sensitivity to small molecule inhibitors (for example, 17AAG). The mechanism of the differential sensitivity of Hsp90 from normal versus tumor cells is unknown, although mutation has been ruled out. One possible mechanism may be differences in post-translational modification of tumor Hsp90. K294 was found to be acetylated in purified Hsp90 from SkBr3 cells, a breast cancer cell line.
This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids surrounding K294 of human Hsp90.