||Recombinant fragment, corresponding to amino acids 577-732 of Human Hsp90 alpha with N terminal His tag; MWt 18kDa.
||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.
||Lyophilised:Reconstitute with 103 μl aqua dest.
||Preservative: NoneConstituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5
||Shipped at 4°C. Upon delivery aliquot and store at -80oC. Avoid freeze / thaw cycles.
|Sequences of amino acids:
||DILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKA QALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADK NDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMI KLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEE VD
||Belongs to the heat shock protein 90 family.