Sortase A from Staphylococcus aureus is a bacterial transpeptidase that covalently attaches 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.

This chemistry has been exploited as a molecular "stapler" to site-specifically link proteins with the C-terminal LPETGX motif to other proteins or molecules possessing a glycine or aminomethylene motif.

Sortase A (26-206 aa) was overexpressed and purified from E.coli strain as His-tagged form at N-terminal.

Applications
- in vitro protein ligation reactions

Concentration & Storage Condition
- 1 ㎍/㎕. Store at -20℃.

10X reaction buffer
- 500 mM Tris-HCl (pH 7.5), 1.5 M NaCl, 50 mM CaCl₂

Storage Buffer

- 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 50% glycerol.