85-1450-45　［取扱停止］Heat Shock Protein 90, Recombinant, Human (HSP90) 20ug　H1831-57R

特徴

• 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, HSP-90 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.
• Recombinant HSP-90 produced in E. coli is a single non-glycosylated polypeptide chain containing 732 amino acids and having a molecular mass of 86.8kD. Recombinant HSP-90 is expressed with a 20aa His tag at the N-terminus and purified by proprietary chromatographic techniques.
• Storage and Stability:May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add 0.1% HSA or BSA, aliquot and store at -20°C. Aliquots are stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.