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Bulk\". Unit of measure is \"MU\".
06 369 880 103: Will be supplied as \"Trypsin, recombinant 1g\". Unit of measure is “piece”.", "Name": "CB - Order Information" }, { "Language": "en", "Value": "Use the animal component-free and DIN EN ISO 13485-manufactured Trypsin, recombinant, as critical raw material for the production of active pharmaceutical ingredients (API), i.e., insulin, vaccines and for cell dissociation.", "Name": "Applications" }, { "Language": "en", "Value": "Trypsin is a widely used serine protease, typically isolated from pancreas of different animals, that specifically cleaves at the C-terminus of arginine and lysine within a peptide chain. Roche has chemically synthesized a gene encoding for the amino acid sequence of Trypsin and has transformed the gene into the expression host Pichia pastoris, which expresses the recombinant Trypsin as active protease with identical properties compared to the native Trypsin.
The product is manufactured according to DIN EN ISO 13485. No animal-derived products are used in the fermentation, purification and final formulation. The production process is validated resulting in a very high lot-to-lot consistency.", "Name": "Product Description" }, { "Language": "en", "Value": "Intended for use in highly regulated production processes at pharmaceutical companies.", "Name": "Positioning" }, { "Language": "en", "Value": "For several years Roche has successfully pursued the strategy of replacing animal-derived enzymes, frequently used in pharmaceutical production processes with recombinant, animal component-free enzymes. Related products are recombinant Carboxypeptidase B, recombinant DNase I, and others.", "Name": "Background Information" }, { "Language": "en", "Value": "Trypsin, recombinant, is produced completely animal component-free and according to DIN EN ISO 13485.", "Name": "Quality Control" }, { "Language": "en", "Value": "CAS Number: 9002-07-7
Molecular weight: 23.5 kD
pH optimum: 8.0
Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin, α1-antitrypsin, APMSF, and antipain", "Name": "Properties" }, { "Language": "en", "Value": "Appearance: Clear, colorless to slightly yellowish solution
Storage buffer: HCl, 10 mmol/L; CaCl2, 20 mmol/L
pH value: 2±0.5
Activity (with chromozym TRY): ≥10,800 U/mL
Total activity (with chromozym TRY): 3.5 MU ±10%
Specific activity: ≥180 U/mg
Protein: 70±10 mg/mL
Purity (RP-HPLC): ≤20% α-trypsin, ≥70% β-trypsin, corresponds to master lot
Bioburden: ≤100 CFU/mL
Stability: At -15 to -25°C within specification range for 36 months.", "Name": "Specification" } ] } } ] }

Trypsin, recombinant

Expressed in Pichia pastoris

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Trypsin
Secure and efficient protein production

Supporting your manufacturing challenges with exceptional enzyme quality and reproducibility 

Trypsin is a serine protease widely used in biopharmaceutical manufacturing to specifically cleave the C-terminus of arginine and lysine in peptide chains. 

To address demands of high-quality protein production, Roche has synthesized a gene encoding for the amino acid sequence of Trypsin and has transformed the gene into the expression host Pichia pastoris. Recombinant Trypsin is expressed as active protease, with equivalent properties compared to native trypsin. 

  • Minimize the risk of virus contamination and the risk of animal-related cross-contamination.
  • Rely on high purity. Minimize the risk of host cell protein contamination in your final product.
  • Increase the safety of your production processes with reproducible performance and high lot-to-lot consistency.
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proteases

Proteases selection guide

Protein cleavage beyond Trypsin. Learn more about the Roche protease portfolio in this selection guide.

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