Recombinant human trypsin has the same amino acid sequence and properties as human trypsin. Comply with the provisions of Article 3 of Article 17, Animals for Production and Identification of the 2010 Chinese Pharmacopoeia: “Trypsin used to digest cells shall be proven free of exogenous or endogenous virus contamination” (Chinese Pharmacopoeia III (2010 Edition) ) Page XII)
1) Recombinant production, no animal-derived virus contamination, such as swine flu virus, porcine parvovirus, etc.
2) Special process, no endogenous virus pollution, no bacteria, fungi, mycoplasma pollution
3) Freeze-dried powder, safe to transport and store, not easy to lose activity
4) Does not contain any protease inhibitors, such as PMSF, etc.
1) HPLC purification, electrophoresis pure
2) Specific activity, no other protease activity
The specific activity is not less than 2500 USP u/mg pro.
Trypsin is an endopeptidase that can be used to cleave peptide bonds at the C-terminus of lysine and arginine, thereby cleaving large molecular proteins into small peptides. Trypsin is widely used in various biotechnological processes, such as:
1) Cell separation of various tissues in cell culture
2) Degradation of denatured protein
3) Enzymatic hydrolysis and sequencing of proteins
4) Cell therapy for tumors, etc.
Source: Recombinant Escherichia coli
Product properties: white or almost white freeze-dried powder
Electrophoresis identification and Coomassie brilliant blue staining
12% SDS-PAGE: non-reducing SDS-PAGE protein electrophoresis, molecular weight 24kD, single main band.
Specific activity: is not less than 2500 USP u/mg pro.
Other enzyme content: No chymotrypsin, carboxypeptidase A and other pollution and activity.
Does not contain any protease inhibitors: No PMSF, EDTA and other protease inhibitors
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