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Rc Trypsin standard

Rc Trypsin standard

Trypsin, a single chain protein of 223 amino acids, is a member of the Serine protease S1 family. It is 223 amino acids long — expressed in Pichia Pastoris — and is produced by the removal of N-terminal hexapeptide from Trypsinogen. The native form of Trypsin is termed as β –Trypsin and α-Trypsin results from its hydrolysis. The protease cleaves peptides at Lysine and Arginine residues on the C-terminal end, with an optimal activity at pH 7-9.

  • Insulin and vaccine manufacturing
  • Cell culture applications
  • Food industry
  • Cosmetic industry
  • 100% AOF
  • Zero risk of contamination by adventitious agents
  • High purity; free of contaminating proteases such as Amylase, Chymotrypsin and Carboxypeptidases
  1. Description: Clear, colorless to pale greenish brown,and odorless liquid
  2. pH: 2.0-3.0
  3. Protein content by UV 280 : >60 mg/ml
  4. Purity: >98%
  5. Specific activity: >3800 USP units/mg of protein
  6. Microbial limit tests:
    • TVAC: <100 cfu/ml
    • TYMC: <10 cfu/ml
  7. Pathogens:
    • E. Coli: Shall be absent
    • Salmonella sp: Shall be absent
    • Pseudomonas aeruginosa: Shall be absent
    • Staphylococcus aureus: Shall be absent
  1. Description: White to off white odourless powder
  2. Solubility: Shall comply to the test for solubility
  3. Enzyme activity by USP method: >2500 USP units/mg of powder
  4. Protein content by UV 280 :  >60 mg/mg of powder
  5. Purity: >98%
  6. Specific activity: >3800 USP units/mg of protein
  7. Loss of Drying: NMT 5.0%
  8. Residue on ignition: NMT 2.5%
  9. Microbial limit tests:
    • TVAC: <10,000 cfu/gm
    • TYMC: <100 cfu/ml
  10. Pathogens:
    • E. Coli: Shall be absent
    • Salmonella sp: Shall be absent
    • Pseudomonas aeruginosa: Shall be absent
    • Staphylococcus aureus: Shall be absent
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