Anti-Hsp90 Antibody

Immunoblotting: use at 1ug/mL. A band of ~88 kDa is detected. <br><br>These are recommended concentrations. User should determine optimal concentrations for their application. <br><br>Positive control: Heat shocked HeLa cell lysate.

This antibody is reactive with both the constitutive and the inducible forms of human, mouse, rat, rabbit, chicken, Sf9 cell, Achlya, and wheat germ Hsp90. However, it does not bind to the native form of Hsp90 and does not recognize E. coli and yeast Hsp90.

Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. It participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of chaperone complexes. Hsp90 is relatively abundant in unstressed cells of most prokaryotic and eukaryotic systems and can be induced by heat shock in some systems. It exists in a dimeric form and has been observed to bind to several other cellular proteins such as retrovirus kinases, steroid receptors, hemeregulated protein kinase, actin, and tubulin. When bound to ATP, Hsp 90 interacts with co-chaperones cdc37, p23, and various immunophilin-like proteins, forming complexes that stabilize and protect target proteins from proteasomal degradation.