Selected Proteases for Peptide Mapping Analysis
UA BIOSCIENCE Has Selected Proteases for Peptide Mapping Analysis
- Recent Advances
- Product Information

The Process of Peptide Coverage by Mass Spectrometry/Determination of the Complete Peptide Map Sequence:
• Use proteases such as PNGase F, Trypsin, Chymotrypsin, Asp-N, Glu-C, Lys-C, and Lys-N to respectively digest and identify the target protein.
• Analyze the samples by nano LC-MS/MS or UV LC-MS/MS.
• Compare the obtained peptide coverage/complete peptide map sequence with the theoretical sequence you provided.
• The comparison results
Data Sharing:
Recombinant Trypsin (Mass Spectrometry Grade):

The sequence coverage of the BSA sample after digestion by Trypsin and analysis by LC-MS/MS is 99.7%.
Recombinant Endoproteinase Lys-C:

Compared with the imported brand of Lys-C, the peptide map is basically the same, and there are basically no differences in common post-translational modifications (PTMs).
V8 Protease (Glu-C):

The sequence coverage of the BSA sample after digestion by Glu-C and analysis by LC-MS/MS is 98.3%.
Recombinant α-Chymotrypsin:

After proteolytic digestion, compared with the chymotrypsin of mainstream brands, the peptide map and sequence coverage are basically the same.
Metalloprotease (Asp-N):

The sequence coverage of the BSA sample after digestion by AspN-1 and analysis by LC-MS/MS is 91.8%.
Glycerol-free PNGase F:













