Mass spectrometry grade trypsin - 'cut' to obtain good data
Mass spectrometry trypsin is a serine peptide endonuclease produced through genetic engineering technology. It can specifically cleave the carboxyl terminal peptide bonds of lysine (K) and arginine (R)
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Product Characteristics
Mass spectrometry-grade trypsin is a serine endopeptidase produced through genetic engineering technology. It specifically cleaves peptide bonds at the carboxyl terminus of lysine (K) and arginine (R), exhibiting the following key properties:
Animal Origin-Free: Manufactured without any animal-derived raw materials, eliminating the risk of exogenous viral contamination.
High Purity and Activity: Exhibits high purity, specific activity, and low levels of host protein residues.
Batch-to-Batch Consistency: Ensures stable and reproducible quality across production lots.
Application Scenarios
Post-Translational Modification (PTM) Analysis: Under low pH conditions, recombinant trypsin suppresses non-enzymatic modifications (e.g., deamidation, disulfide bond scrambling) while efficiently cleaving proteolysis-resistant sites, enabling accurate PTM localization.
Protein Identification and Quantification: By specifically cleaving lysine (K) and arginine (R) residues, it digests complex protein samples into peptides detectable by mass spectrometry, facilitating precise protein identification via database matching.
Exosome and Single-Cell Proteomics: Exosomes, as intercellular communication carriers, require highly sensitive digestion protocols. Combining recombinant trypsin with Lys-C significantly improves peptide recovery from exosome samples, advancing liquid biopsy technologies.
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Trypsin, Mass Spectrometry Grade (Product Code: UA070130)
In terms of sequence coverage, UA070130 demonstrates a slight advantage, with enzyme P and enzyme Y exhibiting coverage values that are 1.3% and 2.3% lower, respectively. However, when considering peptides with no more than three missed cleavage sites, a different trend emerges. Enzyme Y yields the highest proportion, followed by enzymes UA070130 and P, which show marginally lower values. These results indicate that the three enzymes display comparable efficacy in protein digestion.
This article is reviewed and published by the technical expert team of UA
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