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.
序列
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来源宿主
大肠杆菌中重组表达
溶解建议
Sterile Filtered White lyophilized （freeze-dried） powder. HSP20 lyophilized from 20mM Tris-acetate， pH-7.6， 10mM NaCl， 0.1mM EDTA， 0.1mM PMSF and 15mM ?-mercaptoethanol.
保存建议
HSP20 although stable at 10℃ for 2 weeks， should be stored desiccated below -18℃. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）.
Please prevent freeze-thaw cycles.
