||Recombinant full length human Hsp90 beta, cloned from a human cDNA library and expressed in Hi5 cells using baculovirus expression.
||HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1 (MIM 140571), an inducible form, and HSP90AB1, a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al.
||>90% by SDS-PAGE
||Preservative: NoneConstituents: 10% Glycerol, 20mM Tris, 175mM Sodium chloride, 1mM DTT, 0.1mM EDTA, pH 7.5
||Store at -20°C. Stable for 12 months at -20°C
||Belongs to the heat shock protein 90 family.