High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu. Residues 27-43 and 178-184 both contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.
High-mobility group box 1 (HMGB1 or HMG1) human recombinant fused with 6X His tag produced in E. coli is a single, non-glycosylated, polypeptide chain containing 223 amino acids and having a molecular mass of 26 kDa. The HMGB1 is purified by proprietary chromatographic techniques. Purity is greater than 95.0% as determined by RP-HPLC and SDS-PAGE. The HMGB1 (1 mg/ml) was lyophilized after extensive dialyses against 1x PBS pH-7.4.
Amino acid sequence:
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