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Key Documents

MAK290

Sigma-Aldrich

Trypsin Activity Colorimetric Assay Kit

sufficient for 100 colorimetric tests

Synonym(s):

Trypsin Enzyme Activity Kit

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About This Item

UNSPSC Code:
12161503
NACRES:
NA.84

detection method

colorimetric

relevant disease(s)

gastrointestinal diseases

storage temp.

−20°C

General description

Trypsin (EC 3.4.21.4) is a pancreatic serine protease, which hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and cleavage may not occur if a proline residue is on the carboxyl side. Tryptic digestion of the protein of interest results in a highly specific cleavage and a limited number of peptide fragments.

Suitability

Suitable for the detection of Trypsin activity in various samples.

Principle

In this assay, trypsin cleaves a substrate to generate p-nitroaniline (p-NA) which is detected at λ= 405 nm. Since the color intensity is proportional to p-NA content, trypsin activity can be accurately measured. The kit detects 10–100 mU (p-NA unit) trypsin in various samples.

Pictograms

Health hazardCorrosion

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Dam. 1 - Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A Aderibigbe et al.
Poultry science, 99(10), 5007-5017 (2020-09-30)
Trypsin inhibitors (TI) resident in soybeans affects protein utilization. While heat treatment influences residual TI, it simultaneously affects the structure and solubility of the soybean proteins and confounds any response to exogenous proteases. Using purified TI, the effect of exogenous
Ahmad Farooq et al.
Gastroenterology, 161(3), 982-995 (2021-05-30)
Heavy alcohol consumption is a common cause of acute pancreatitis; however, alcohol abuse does not always result in clinical pancreatitis. As a consequence, the factors responsible for alcohol-induced pancreatitis are not well understood. In experimental animals, it has been difficult
Ali Hanafiah Hakim et al.
Animals : an open access journal from MDPI, 12(7) (2022-04-13)
The study aimed at determining the ileal nutrient digestibility, digestive enzyme activity, intestinal morphology, and nutrient transporters mRNA expressions in broiler chickens fed with fermented PKC (LPKC) based diets with different levels of fat supplementation under hot and humid conditions.

Protocols

This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).

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