Immobilized Trypsin, Agarose(T575-31AN)
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Description :Recombinant tag-free swine trypsin (10-end) was expressed in yeast cells.
Matrix: cross-linked agarose
Average Particle Size: 90 μm
Ligand Density: 1 mg protein / ml matrix
Maximum Flow Rate, Pressure: 100 cm/h, 0.5 bar
Species :Swine
Tag :tag-free
Expression System:Yeast cells
Sequence :10-end
Sample Data :
Enzyme Commission Number :EC 3.4.21.4
Gene Aliases :Trypsinogen
Storage, Stability, and Shipping :Store product at 2 - 4oC for up to 6 months.
Applications :In vitro Proteolysis
Digestion Conditions :Catalytic pH range: 8.0 ~ 10.0
Catalytic temperature range: 20 ~ 37oC
Enzyme : Substrate Ratio: 1:200 ~ 1:3,000
Scientific Background :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 an agarose matrix circumventing the need for enzyme removal after cleavage. The resin can be reused 10-20 times after regenerating when proper storage conditions are followed.
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