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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
GHS08,GHS05

Signal Word

Danger

Hazard Statements

H318,H334

Hazard Classifications

Eye Dam. 1 - Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

PDSCL

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PRTR

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FSL

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ISHL Indicated Name

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ISHL Notified Names

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Cartagena Act

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JAN Code

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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
Sergio A Urzúa et al.
The journal of physical chemistry. B, 126(28), 5231-5240 (2022-07-13)
Under the most common experimental conditions, the adsorption of proteins to solid surfaces is a spontaneous process that leads to a rather compact layer of randomly oriented molecules. However, controlling such orientation is critically important for the development of catalytic
Montserrat Alcázar-Valle et al.
Molecules (Basel, Switzerland), 25(15) (2020-08-06)
Beans (Phaseolus spp.) are one of the most important legumes for their nutritional value and health benefits in many world regions. In addition to Phaseolus vulgaris, there are four additional species that are cultivated in many regions of the world
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.
View All Related Papers

Protocols

Trypsin Assay Procedure (EC 3.4.21.4)

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

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