Glu-C Protease, MS Grade, is a highly specific endoproteinase use to improve sequence coverage in mass spectrometry protein identification applications, in-solution digestion of proteins and in-gel digestion of proteins. Store at -20 ˚C in a nonfrost-free freezer.

• Complementary to tryptic digests – hydrolyzes proteins specifically at the carboxyl side of glutamic acids
• Increased sequence coverage – better protein characterization results from overlapping peptides with complementary sequence coverage and chromatographic, ionization and fragmentation properties
• High specific activity – greater than 500 units/mg protein
• N-terminal arginine cleavage specificity – at least 90% for a complex protein sample
• Stable – provided in a lyophilized format

This Glu-C is a mass spectrometry (MS)-grade serine protease isolated from Staphylococcus aureus

The endoproteinase Glu-C, also referred to as V-8 Protease, specifically cleaves the carboxyl side of glutamic residues when reactions are carried out in ammonium bicarbonate and ammonium acetate buffers, generating a limited number of peptide fragments. Cleavage can also occur at both glutamic and aspartic residues in phosphate buffers. Glu-C can efficiently digest protein in 5 - 18 hours at 37 ˚C. Glu-C Protease remains active under denaturing conditions such as 2 M urea, 1 M guanidine∙HCl, 0.1% SDS, 2% CHAPS and 20% acetonitrile. Glu-C activity is optimal at pH 8. This lyophilized enzyme has a mass of 27 kDa and is stable for 1 year when stored at -20 ˚C.

Glu-C can be used alone or alongside trypsin or other proteases to produce complementary protein digests for peptide mapping and protein sequencing. Glu-C protease is suitable for either in-solution or in-gel digestion workflows. This Glu-C enzyme is packaged lyophilized (5 x 10 µg).