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Overview
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Heat Shock Protein 20 Human Recombinant produced in E. Coli. Hsp20 is a mammalian small heat-shock protein family that is found most copiously in skeletal muscle and heart. The heat-shock proteins seem to act as chaperones that can protect other proteins against heat-induced denaturation and aggregation. The Hsp20 family is characterized structurally by the presence of a conserved C-terminal domain of about 100 residues and contains a beta-sandwich fold consisting of 8 strands in 2 beta-sheets in a Greek-key topology. Hsp20 proteins have a tendency to form dimers, through a disulphide linkage formed by an N-terminal cysteine, low heat stability and a poor chaperoning ability in comparison with other family members.
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Overview