||Recombinant fusion protein; human Hsp90 alpha fused to His-tag at N-terminus.Molecular Weight: 86.8 kDa (732 amino acids).
||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, an inducible form, and HSP90AB1 (MIM 140572), 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: 20mM Tris HCl, 100mM Sodium chloride, pH 7.4
||Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
||Belongs to the heat shock protein 90 family.