Description
Key facts
Detection method:Colorimetric,
Sample types:Urine, Plasma, Tissue Extracts, Cell culture supernatant, Serum, Other biological fluids,
Assay type:Enzyme activity,
Sensitivity:= 10 µU,
Assay time:2h,
Assay Platform:Microplate reader
Product details:
How the assay works
In the trypsin activity assay protocol, trypsin cleaves a substrate to generate p-nitroaniline (p-NA) which is detected at OD = 405 nm. Since the color intensity is proportional to p-NA content, trypsin activity can be accurately measured.
Trypsin Activity Assay Kit (Colorimetric) protocol summary :
- Add samples, positive control and standards to wells
- Add chymotrypsin inhibitor to sample and positive control wells and incubate for 10 min at room temp
- Add reaction mix and incubate 25°C protected from light
- Measure optical density (OD 405nm) in a kinetic mode at 25°C for 1 – 2 hours protected from light
How other researchers are using
Trypsin Activity Assay Kit (Colorimetric) has been used in a variety of sample type including:
Mouse intestinal tissues
Mouse Cecal tissue
Mouse Pancreatic Acinar Cells
References:
1-Bianchimano P et al. 2023
2-Bolsega S et al. 2023
3-Yang L et al. 2023
Related and recommended products
For fluorometric detection, we recommend Trypsin Activity Assay Kit (Fluorometric)
ab282916
This product is manufactured by BioVision, an Abcam company and was previously called K771 Trypsin Activity Colorimetric Assay Kit. K771-100 is the same size as the 100 test size of ab102531.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Trypsin is a serine protease enzyme with a molecular mass around 24 kDa. Known also as "bovine trypsin" or "pancreatic trypsin" it functions primarily in the digestive system. Trypsin hydrolyzes peptide bonds specifically at the carboxyl side of the amino acids lysine and arginine. The enzyme is produced in the pancreas as an inactive precursor trypsinogen which converts to active trypsin in the small intestine.
Biological function summary
Trypsin breaks down proteins into smaller peptides facilitating digestion. It is not part of a complex but interacts with other pancreatic enzymes like chymotrypsin and elastase. Trypsin also plays a regulatory role in activating other zymogens like procarboxypeptidase and chymotrypsinogen essential in the complete protein digestion process.
Pathways
The catalytic actions of trypsin are integral to the digestive pathway in the gastrointestinal tract. It ensures the efficient breakdown and absorption of nutrients. In the trypsin activation pathway it activates other proteases which are significant for protein catabolism. This enzyme collaborates closely with anti-trypsin inhibitors that regulate its activity preventing autodigestion and maintaining homeostasis.
Trypsin relates closely to pancreatitis and cystic fibrosis. Unregulated activation of trypsinogen within the pancreas causes pancreatitis a condition characterized by inflammation and damage to pancreatic cells. Alpha-1 anti-trypsin an important inhibitor of trypsin connects to conditions like emphysema and liver disease due to its dysfunctional regulation indicating a broader implication of trypsin in maintaining cellular health.
