Glu-C Protease

Endoproteinase Glu-C from Staphylococcus aureus V8 has been used for:

• obtaining proteolytic cleavage fragments of the S-layer protein (from Bacillus stearothermophilus ATCC 12980) to perform affinity studies.
• the enzymatic cleavage of native VSTx-3 (voltage sensor toxin 3) peptide for its sequence determination.
• limited proteolysis of recombinant purified PimA (phosphatidylinositol mannosyltransferase).
• the digestion of glycosylated hemoglobin for isotope dilution liquid chromatography-tandem mass spectrometry analysis.

Endoproteinase Glu-C from Staphylococcus aureus strain V8 is a serine endoprotease, which hydrolyzes peptide bonds at the carboxyl side of glutamyl and aspartyl residues. The specificity of Glu-C is dependent upon the buffer and pH employed as well as the structure around the potential cleavage site. In ammonium acetate (pH 4.0) or ammonium bicarbonate (pH 7.8), the enzyme preferentially cleaves glutamyl bonds; whereas, in phosphate buffer (pH 7.8) Glu-C will cleave at either site. Glu-C is reported to be active in the presence of 0.2% SDS (sodium dodecyl sulfate) and in 4.0M urea.