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.
应用类型
ELISA， Western blot and immunohistochemistry
免疫原
Anti-human HSP90A mAb， is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSP90A amino acids 1-732 purified from E. coli.
