Sortase A, S. aureus, His-tag

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This product is suitable for in vitro ligation of proteins and peptides to other. Sortase A has been shown to create circularized proteins ^[1], as well as couple polypeptides to a wide range of substituents including polymers ^[2], lipids ^[3], fluorophores ^[4], sugars ^[5], microspheres ^[3], peptide nucleic acids ^[6], among others.

Staphylococcal Sortase A is a bacterial transpeptidase that covalently links proteins to the bacterial cell wall by cleaving between threonine and glycine at an LPXTG recognition motif and catalyzes the formation of an amide bond between the carboxyl-group of threonine and the amino-group of the cell-wall peptidoglycan ^[7]. This chemistry can be exploited to site-specifically link proteins/peptides with the C-terminal LPETGX motif to other proteins or molecules possessing a glycine or aminomethylene motif ^[8].

Aqueous buffered solution containing: 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 8 mM imidazole, 0.04% Tween-20, and 20% glycerol

Analysis of this product can be performed in a reaction buffer (50 μl) containing 50 mM HEPES (pH=7.4), 150 mM NaCl, 5 mM CaCl2, 5 mM (Gly)3, 25 mM Abz/Dnp substrate, and Sortase A for 30 min at 30°C. Fluorescence intensity is measured at Ex320nm/Em420nm.