Peptide-affinity Purified Polyclonal Antibody to Hsp90b (Ser254)

Background
The 90 kDa molecular chaperone family comprises several proteins including the 90 kDa heat shock protein, Hsp90 and the 94 kDa glucose-regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90 alpha and Hsp90 beta which are encoded by separate genes. Hsp90 is part of the cell’s powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steroid receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways. Recent studies indicate that when Drosophila Hsp90 buffering is compromised by e.g., temperature, cryptic variants are expressed and selection can lead to the continued expression of these traits, even if Hsp90 function is restored.

Antigen
This antibody was generated by immunizing rabbits with a synthetic phosphopeptide corresponding to human HSP90B around the phosphorylation site of serine 254 (V-G-SP-D-E).

Reference
1. Scheibel, T. et al. PNAS. 96:1297-1302 (1999).
2. Nemoto, T. et al.  J. Biol. Chem. 272:26179-26187 (1997).
3. Nemoto, T. et al. Biochem. J. 330:989-995 (1998).