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Enteropeptidase

Enteropeptidase structure

Enteropeptidase 

structure
  • CAS No:

    9014-74-8

  • Chemical Name:

    Enteropeptidase

  • Synonyms:

    Enteropeptidase;Peptidase,entero-;Enterokinase;E.C. 3.4.21.9;E.C. 3.4.4.8;EC 3.4.21.9;EC 3.4.4.8;Enteropeptidases;Enterokinases

  • Categories:

    Analytical Chemistry  >  Standard

Description

An enzyme found in the small intestine, which converts trypsinogen into trypsin.

Enteropeptidase Basic Attributes

232-761-1

Characteristics

white salt-free, lyophilized powder

−20°C

Safety Information

NONH for all modes of transport

3

P261-P284-P304 + P340-P305 + P351 + P338-P342 + P311

H315-H319-H334-H335

Enteropeptidase Use and Manufacturing

Properties: Sterilized liquid. Recombinant use: biochemical research. It is a serine protease, which can efficiently and specifically hydrolyze the fusion protein expressed by the engineering bacteria (the recognition sequence is -(Asp)4Lys↓--) to release the target protein. Enterokinase is widely used in the development of genetic engineering products because of its high specificity and high hydrolysis efficiency; it can be used as a substrate for protease to specifically recognize and cleave enterokinase cleavage sites, and its application First, it is used as a protease for the specific fragmentation of recombinant fusion proteins, and is particularly suitable for research in the bioengineering pharmaceutical industry, genetic engineering, biochemistry, and molecular biology. However, the source of natural enterokinase is limited, and the enterokinase extracted from animal tissues is contaminated with other proteases, which brings difficulties to practical application. This requires the use of genetic engineering methods to produce high-purity enterokinase. The activity of high-purity enterokinase produced by genetic engineering methods is similar to that of natural enzymes, but enterokinase cleaves faster.

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