Protease Inhibitors

Trypsin is a proteolytic enzyme used to detach adherent cell from culture vessel surfaces. Typical use includes removing adherent cells from a culture surface.

Trypsin consists of a single chain polypeptide of 223 amino acid residues. Member of the serine protease family Dissolves blood clots in its microbial form Treats inflammation in its pancreatic form Trypsin cleaves peptides on the C-terminal side of

Trypsin consists of a single chain polypeptide of 223 amino acid residues. Member of the serine protease family Dissolves blood clots in its microbial form Treats inflammation in its pancreatic form Trypsin cleaves peptides on the C-terminal side of

Trypsin consists of a single chain polypeptide of 223 amino acid residues. Member of the serine protease family Dissolves blood clots in its microbial form Treats inflammation in its pancreatic form Trypsin cleaves peptides on the C-terminal side of

Trypsin consists of a single chain polypeptide of 223 amino acid residues. Member of the serine protease family Dissolves blood clots in its microbial form Treats inflammation in its pancreatic form Trypsin cleaves peptides on the C-terminal side of

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino