MAK290
Trypsin Activity Colorimetric Assay Kit
sufficient for 100 colorimetric tests
Synonym(s):
Trypsin Enzyme Activity Kit
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About This Item
NACRES:
NA.84
UNSPSC Code:
12161503
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.
Application
Suitable for the detection of Trypsin activity in various samples.
Biochem/physiol Actions
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Dam. 1 - Resp. Sens. 1
Storage Class
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
监管及禁止进口产品
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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
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
Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.
本方案适用于使用Nα-苯甲酰基-L-精氨酸乙酯（BAEE）作为底物测定胰蛋白酶活性。本方案是基于连续分光光度速率测定（A253，光程= 1cm）方案：
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Instructions
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