
Recombinant Trypsin, GMP Grade
Description
Trypsin (EC 3.4.21.4) is a serine protease used for hydrolyzing peptide bonds formed at the C-terminal of lysine and arginine. Our recombinant porcine-derived trypsin is expressed in Pichia pastoris and purified using high-performance chromatography. Its amino acid sequence is identical to cationic trypsin derived from porcine pancreas, without any tags. It has a molecular weight of 24kDa, with an optimal enzymatic pH range of 7.0–9.0 and an optimal temperature of 30–37°C. Its activity is inhibited by serine protease inhibitors such as TLCK, PMSF, and EDTA.
Applications
- Biopharmaceuticals: Enzymatic cleavage or transpeptidation during the production of recombinant insulin and its analogs (e.g., aspart insulin, detemir, and glargine insulin), as well as peptide drug manufacturing processes.
- Biological Research: Protein digestion, peptide mapping, sequencing, cell culture digestion, tissue dissociation, and biochemical extractions.
Quality Parameters
- Appearance: White or off-white lyophilized powder
- Purity (SDS-PAGE): ≥95%
- Relative Molecular Weight: 23kDa ± 2.3kDa
- Specific Activity: ≥3800 USP/mg
- Endotoxin: <10 EU/mg
Notes:
① Additional tests, such as microbial limits, host protein residue, or host DNA residue, can be included in the CoA as per customer requirements.
② Enzyme activity definition: Using BAEE as the substrate, in a reaction system of 25mmol/L Tris, pH 7.6, at 25°C, in a 3.0ml reaction system with a 1cm optical path, the enzyme amount required to increase ΔA253nm by 0.001 per minute is defined as one unit of activity (USP).
Advantages
- Produced under GMP-compliant conditions with a batch production scale exceeding 200g and consistent quality across batches.
- High purity and activity with no residual contaminant enzymes. No animal-derived materials are used in the production process.
Storage
The lyophilized powder remains stable for 24 months when stored below -15°C. After reconstitution, it can be stored below -15°C and undergo up to three freeze-thaw cycles. The reconstituted solution remains stable at 2–8°C for up to five days.