The 90-kDa heat shock protein (Hsp90) is a highly conserved, and abundant cytosolic homodimeric molecular chaperone (1). Hsp90 is distinguished from other chaperones in that most of its known substrates are signal transduction proteins, non activated steroid hormone receptors, several protooncogenic tyrosine and serine/threonine kinases and actin (2-3). Two isoforms which correspond to the major and minor isoform , (Hsp90 a and Hsp90 ß ) can be found in nearly equal amount in humans, and operates as part of a multichaperone machinery in the cytosol, which includes Hsp70, peptidyl-prolyl isomerases and other cochaperones (3).
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