Anti-HSP90α [Clone 2G5.G3] - 100 μg

Hsp90 is an abundantly and ubiquitously expressed heat shock protein found in all eukaryotic cells. It exists in two principal forms, α and β, which share 85% sequence homology. Both forms are expressed in the cytosol. Hsp90α exists primarily as a homodimer while Hsp90β exists mainly as a monomer. Hsp90 plays a role in folding, assembly, maturation, and stabilization of specific proteins as a key component of a chaperone complex. Most of the Hsp90-regulated proteins that have been identified are involved in cell signaling; kinases, v-Src, Wee1, c-Raf, and p53 are some examples. When bound to ATP, Hsp90 interacts with co- chaperones Cdc37, p23, and various immunophilin-like proteins to form complexes that stabilize and protect target proteins from proteasomal degradation.