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Heat Shock Protein 20 Human Recombinant ( HSP20 Human )
DescriptionHeat Shock Protein 20 Human Recombinant produced in E.Coli.SourceEscherichia Coli.Physical AppearanceSterile Filtered White lyophilized (freeze-dried) powder.FormulationHSP20 lyophilized from 20mM Tris-acetate, pH-7.6, 10mM NaCl, 0.1mM
Data sheet
| Formulation | HSP20 lyophilized from 20mM Tris-acetate, pH-7.6, 10mM NaCl, 0.1mM EDTA, 0.1mM PMSF and 15mM b-mercaptoethanol. |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Inactivation | Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-4 as a Reference Standard. |
| Description | Heat Shock Protein 20 Human Recombinant produced in E.Coli. |
| Protein Background | 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. |
| Expression host | Escherichia Coli. |
| Synonyms | Heat Shock Protein 20, HSP20. |
| Reagent Appearance | Sterile Filtered White lyophilized (freeze-dried) powder. |
| Stability | HSP20 although stable at 10°C for 2 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles. |