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| Product Name | Mass-Spectrometry-Grade Recombinant Porcine Trypsin |
| Catalog No. | IVDRM-0303 |
| Description | A serine endopeptidase that cleaves on the carboxyl side of lysine and arginine residues, produced as a recombinant porcine trypsin in the yeast Pichia pastoris under GMP controls. The preparation is filtered to sterility, contains no animal-derived impurities and therefore carries no risk of animal-origin viral contamination such as porcine parvovirus or swine influenza virus. Chymotryptic activity is naturally absent, and published comparisons report missed-cleavage rates in proteomic digests roughly 50% below those of imported reference materials. |
| Intended Use | Digestion of protein extracts ahead of LC-MS/MS identification, and protease treatment steps inside protein purification workflows. |
| Principle / Technology | Hydrolyses peptide bonds C-terminal to Lys or Arg; the resulting peptide mixture is matched against databases for protein identification. |
| Detection Method | Peptide bonds on the carboxyl side of lysine and arginine |
| Sample Type | Reduced, alkylated and denatured protein extracts prepared for bottom-up proteomics |
| Performance Range / Specifications | Specific activity above 6800 USP U/mg; beta-trypsin content above 80% by HPLC with alpha-trypsin below 20%; missed-cleavage rate approximately 50% lower than imported benchmarks |
| Specificity | Single-site specificity for Lys/Arg carboxyl peptide bonds; no detectable chymotrypsin contamination |
| Reaction Conditions / Protocol | Denature, reduce and alkylate the sample, add the enzyme at the recommended enzyme-to-substrate ratio and incubate until digestion is complete; quench with acid before desalting and LC-MS analysis. |
| Components / Formulation | Supplied as a sterile-filtered aqueous solution with hydrochloric acid as preservative |
| Storage Conditions | -25 to -15 °C; protect from repeated freeze-thaw cycles |
| Shelf Life | 24 months from the release date |
| Package Specifications | 1 mg and 100 microgram packs |
| Product Form | Sterile-filtered solution, 2.0 mg/mL |
| Quality Control | Released against activity, purity and beta-trypsin proportion specifications; manufactured and sterile-filtered under GMP conditions |
| Key Features | Animal-component-free GMP production; chymotryptic activity naturally absent; USP-based activity assignment that exceeds imported equivalents; high storage stability and low missed-cleavage rate in proteomic workflows |
| Purity | Greater than 95% by HPLC |
| Concentration | 2.0 mg/mL |
| Activity / Unit Definition | Above 6800 USP Unit/mg |
| Source / Origin | Recombinant porcine sequence expressed in Pichia pastoris (yeast) |
| pH Range / Optimal pH | Acidic formulation preserved in 1 mM HCl |
| Shipping Conditions | Dry ice or cold pack |
| Expiration Date / Stability | Two years at -25 to -15 °C with high retained activity |
| Regulatory / Compliance | Produced under GMP regulations |
| Compatibility | Inhibited by serine-protease inhibitors such as PMSF and TLCK and by the metal chelator EDTA; compatible with standard denaturation and reduction reagents used before digestion |
| Recommended Buffer System | 1 mM hydrochloric acid |
| Application Notes / Precautions | Avoid chelating agents and serine-protease inhibitors during digestion; aliquot to prevent repeated freeze-thaw; handle as a biologically active protease with appropriate PPE. |
| Batch-to-Batch Consistency | Lot-controlled GMP material; lot number printed on every vial |
| Model Type | Recombinant trypsin, mass-spectrometry grade |
| Starting Material / Tissue Site | Protein lysates from cells, tissues or biofluids prepared for bottom-up proteomic identification |
| Delivery Standard | Supplied as a ready-to-use sterile solution; pack sizes as listed |
| Readouts / Downstream Assays | Peptide mapping by LC-MS/MS, sequence coverage and missed-cleavage statistics |
For in vitro diagnostic use.
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