Mass spectrometry (MS) grade enzymes are ultra-pure proteases specifically engineered and rigorously standardized for protein sample preparation in mass spectrometry workflows. MS grade enzymes undergo extensive purification and chemical modifications, such as reductive methylation, to minimize digestion and eliminate contaminating proteolytic activities. This ensures high cleavage specificity and prevents the generation of unwanted background noise or artifact peaks during mass spectra analysis.
Trypsin is the most universally utilized MS grade enzyme, because of its highly specific and efficient cleavage at the carboxyl side of arginine and lysine residues. Other major types include alternative endoproteinases such as Lys-C, Glu-C, Asp-N, and Chymotrypsin, which provide different cleavage specificities and are often used sequentially or in combination with trypsin to maximize protein sequence coverage.
These high-fidelity enzymes are applied in modern proteomics, particularly in approaches where large proteins must be reliably digested into smaller, predictable peptide fragments prior to LC-MS/MS analysis. They are heavily relied upon for accurate protein identification, protein quantitation, and the comprehensive characterization of post-translational modifications (PTMs) such as phosphorylation, methylation, or glycosylation. Furthermore, in the biopharmaceutical industry, MS grade enzymes are crucial for peptide mapping and the structural validation of therapeutic proteins, ensuring reproducible, artifact-free data required for strict quality control. Amerigo Scientific offers a variety of MS grade enzymes to meet the application requirements of different fields.
Specific proteolytic enzymes comprise highly specific endopeptidases that selectively cleave peptide bonds at either the C-terminus or N-terminus of targeted amino acid residues. These enzymes serve as the foundational tools for effectively digesting complex proteins into predictable peptide fragments that fall within the optimal mass range for mass spectrometry identification and sequencing.
By utilizing engineered variants, alternative cleavage sites (such as GluC, AspN, or Chymotrypsin), and "mirror" proteases (Trypsin-N and LysN), researchers can significantly improve sequence coverage, mitigate digestion gaps, and precisely map challenging PTMs.
| Product | Description | Cleavage Site / Specificity | Applications |
|---|---|---|---|
| Trypsin Protease | Porcine-derived, TPCK-treated, and reductively methylated to prevent autolysis. High purity and activity. | C-terminus of R, K | Proteomics, peptide mapping, and protein identification. |
| Ultra-fast rTrypsin 3.0 Protease | Recombinant metalloproteinase with an engineered sequence and methylation; features ultra-fast digestion and zero autolysis. | C-terminus of R, K | Biopharmaceutical protein characterization, single-cell proteomics, and large-cohort proteomics. |
| rTrypsin-N Protease | Recombinant "mirror" protease of trypsin, specifically hydrolyzing peptide bonds at the N-terminus of lysine and arginine. | N-terminus of R, K | Research of R/K PTMs, neuroproteomics, Alzheimer's disease (AD) clinical diagnosis, and peptide therapeutics characterization. |
| rTrypsin/rLys C Complex Protease | An optimized combination of rTrypsin and LysC that addresses inconsistent digestion rates and missed cleavages. | C-terminus of R, K | Improving digestion efficiency and reducing missed cleavages in proteomics. |
| rLys-C Protease | Recombinant protease that specifically hydrolyzes the C-terminus of lysine residues. | C-terminus of K | Improving digestion of resilient proteins and characterization of biopharmaceuticals and antibodies. |
| rLys-N Protease | "Mirror" protease that specifically hydrolyzes peptide bonds at the N-terminus of lysine residues. | N-terminus of K | K-amino acid PTM analysis, neuroproteomics, AD clinical diagnosis, and peptide characterization. |
| rGlu-C Protease | Specifically cleaves C-terminus of E (in ammonium bicarbonate) or E/D (in phosphate buffer). Solution digestion recommended. | C-terminus of E, D | Proteomics, glycoproteomics, and biopharmaceutical peptide mapping to improve sequence coverage and analyze complex PTMs. |
| rArg C Protease | Endopeptidase specifically cleaving the C-terminus of arginine (including R next to proline). | C-terminus of R | Protein identification, PTM characterization, peptide mapping of biotherapeutics, and de novo sequencing. |
| Chymotrypsin Protease | Serine endoprotease with TLCK-inactivation of residual trypsin. Activated and stabilized by Ca2+. | C-terminus of Y, F, W, L | Proteomics research, peptide mapping, and structural analysis. |
| rAsp-N Protease | Recombinant metalloproteinase derived from Pseudomonas fragi, specifically cleaving N-terminus of D and C. | N-terminus of D, C | Protein sequencing characterization and proteomics research. |
Glycoproteomics and glycan analysis enzymes are designed for the targeted analysis of protein glycosylation, focusing explicitly on the removal, modification, or site-specific cleavage of N-linked and O-linked glycans. This group includes robust glycosidases and glycoproteases that can either strip complex oligosaccharides cleanly from the protein backbone or selectively digest peptide bonds adjacent to glycosylation sites without structural bias.
Amerigo Scientific offers specific enzymes for high-throughput glycoproteomics, characterization of intact glycoprotein mass, and precise mapping of glycosylation sites, which are critical workflows in evaluating biopharmaceutical quality control and therapeutic efficacy.
| Product | Description | Cleavage Site / Specificity | Applications |
|---|---|---|---|
| O-Glycoprotease | Recombinant immune metalloproteinase (IMPa) from P. aeruginosa; cleaves N-terminus of S/T in O-glycosylated proteins/peptides without sialic acid bias. | N-terminus of S, T (O-glycosylated) | Characterization and analysis of O-glycosylated proteins. |
| rEndo S2 Glycosidase | Specifically cleaves the N-glycan after the core GlcNAc of native IgG Fc, leaving the core GlcNAc intact (with or without fucose). | IgG Fc N-glycans (after core GlcNAc) | Studying antibody afucosylation, deglycosylated antibody affinity, ADCC effects, site-specific ADC conjugation, and serum IgG fucosylation levels. |
| rPNGase F Glycosidase | Recombinant amidase that cleaves the beta-aspartylglucosamine bond of complex, hybrid, and high-mannose N-glycans, converting Asn to Asp. (Does not cleave core alpha(1→3) fucose). | N-glycans on Asn (N) | Intact mass analysis, glycosylation site identification, free glycan profiling, proteomics, and biopharma quality control. |
This group consists of specialized tool enzymes for the structural characterization, site-specific labeling, and modification of therapeutic antibodies and fusion proteins. It features highly precise proteases capable of generating homogenous antibody fragments via single-site cleavage, as well as transferases and transpeptidases engineered for precise molecular conjugation and protein cyclization via click chemistry.
In addition, we offer specific proteases dedicated to the seamless removal of recombinant fusion tags (such as SUMO or DDDDK tags), ensuring that the final protein products retain their native, unmodified sequences.
| Product | Description | Cleavage Site / Specificity | Applications |
|---|---|---|---|
| rIdeS Protease / rIdeZ Protease | Immunoglobulin IgG-specific degrading enzyme that cleaves a single site below the hinge region. | Single site below the IgG hinge region | Generating homogeneous F(ab')2 and Fc fragments for antibody characterization. |
| B4GALT1 (Y289L) Transferase | Recombinant human-derived enzyme engineered for transferring specific sugar or tags onto proteins. | GlcNAc sites | Conjugation/labeling of O-GlcNAcylated proteins; enzymatic attachment of azido-modified sugars (UDP-GalNAz) to GlcNAc for subsequent click chemistry (SPAAC) labeling (e.g., fluorophores, ADCs). |
| SUMO Protease | Highly active cysteine protease from S. cerevisiae. Recognizes the tertiary structure of SUMO tag rather than amino acid sequence, yielding native C-terminus (cleaves after QIGG). | C-terminus of SUMO tag (QIGG sequence) | Cleaving SUMO fusion tags during recombinant protein expression and purification process optimization. |
| Enterokinase (EK) | Recombinant serine protease that specifically recognizes the DDDDK sequence and cleaves at the C-terminus of Lys. | C-terminus of K in DDDDK | Cleavage of fusion proteins or recombinant peptides in biopharmaceuticals, synthetic biology, and molecular biology. |
| Sortase A | Tool enzyme for protein conjugation and modification. Transpeptidase recognizing N-terminal GGG and C-terminal LPXTG. | Recognizes LPXTG and GGG | Chemical modification of proteins, molecular conjugation, and protein N-/C-terminal cyclization. |
In upstream sample preparation, the elimination of nucleic acid contamination is essential, as it often interferes with downstream mass spectrometry workflows. Amerigo Scientific provides high-efficiency, recombinant endonucleases capable of digesting all forms of DNA and RNA into small, uniform oligonucleotide fragments. By rapidly reducing sample viscosity and eliminating background interference from nucleic acids, these enzymes significantly enhance overall protein recovery, improve sample purity, and ensure stable, reproducible mass spectrometry analysis for complex biological matrices.
| Product | Description | Cleavage Site / Specificity | Applications |
|---|---|---|---|
| BenzoNuclease | Recombinant endonuclease that digests all forms of DNA and RNA into 5'-monophosphate oligonucleotides of 2-5 bases. | Non-specific (DNA/RNA) | Removal of nucleic acid contamination to improve protein purity and sample quality during pre-treatment in proteomics and mass spec. |
Note: If you don't receive our verification email, do the following: