Recombinant tag-free swine trypsin (10-end) was expressed in yeast cells.
Matrix: cross-linked silica
Average Particle Size: 200 μm
Ligand Density: 10 mg protein / ml matrix
Maximum Flow Rate, Pressure: 300 cm/h, 3 bar
Catalog No. T575-31SN
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Silica immobilized proteases are amenable to large-scale proteolysis processes. Trypsin is a serine protease that is produced in the acinar exocrine cells of the pancreas. The enzyme cleaves peptides at the C-terminal side of lysine and arginine amino acid residues. Recombinant pancreatic trypsin is a widely biochemical tool used in processes, which include: recombinant insulin production, cell culture, cell fermentation, protein peptide mapping, proteomic sequencing and cell dissociation. Trypsin function is inhibited by serine protease inhibitors (e.g. TLCK, PMSF), and metal chelating agents (e.g. EDTA).
Immobilized trypsin is covalently cross-linked to a silica matrix circumventing the need for enzyme removal after cleavage. The resin can be reused ~20 times after regenerating when proper storage conditions are followed.
Enzyme Commission Number:
Storage, Stability, and Shipping:
Store product at 2 - 4oC for up to 6 months.
Catalytic pH Range: 8.0 ~10.0
Catalytic Temperature Range: 20 ~ 37oC
Enzyme : Substrate Ratio: 1:200 ~ 1:3,000
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