Description
Description: Recombinant Human HSP-90 produced in E Coli is a single, non-glycosylated polypeptide chain (aa 1-732) containing 752 amino acids and having a molecular mass of 86.8kDa. HSP90 is expressed with a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Introduction: HSP90 has been identified in the cytosol, nucleus and endoplasmic reticulum, and is reported to exist in many tissue types. In several tissues, including smooth muscle, HSP90 comprises up to 2% of total cellular protein. HSP90 functions as a dimer, assembled as part of heterocomplex. It possesses ATP-binding site and low ATPase activity. HSP90 is able to associate with actin filaments in certain conditions. Another important property of HSP90 is the binding of unoccupied steroid hormone receptors. HSP90 has been characterized as a molecular chaperone able to keep the target protein in a folding-competent state. It has an enhanced chaperone activity in oligomeric form at high temperatures. HSP90 function is sensitive to bivalent cations concentration