More info
Assay Range | 31.25-2000 pg/mL |
Sensitivity | 10 pg/mL |
Specificity | No cross-reaction with other related substances detected |
Size | 96T |
Storage | Store at 2 - 8ºC. Keep reconstituted standard and detection Ab at -20 ºC |
Assay Principle | Sandwich ELISA |
Sample Volume | 100 µL final volume, dilution factor varies on samples |
Sample Type | Cell lysates |
Detection Method | Chromogenic |
Kit Components
1. Recombinant Human Trypsin (Pan) standard: 2 vials
2. One 96-well plate coated with Human Trypsin (Pan) Ab
3. Sample diluent buffer: 12 mL - 1
4. Detection antibody: 1 vial
5. Streptavidin-HRP: 1 vial
6. Antibody diluent buffer: 12 mL x1
7. Streptavidin-HRP diluent buffer: 12 mL x1
8. Chromogenic solution A: 6 mlx1
9.Chromogenic solution B: 6 mlx1
10. Stop solution: 6 mL x1
11. Washing solution (20x): 25 mL x1
Background
Trypsin is a serine protease belonging to the PA clan superfamily. Trypsin is produced as the inactive zymogen trypsinogen in the pancreas. When the pancreas is stimulated by cholecystokinin, it is then secreted into the first part of the small intestine (the duodenum) via the pancreatic duct. Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream.