enterokinase from porcine intestine
Enteropeptidase
CAS: 9014-74-8
Molecular Formula:
enterokinase from porcine intestine - Names and Identifiers
enterokinase from porcine intestine - Physico-chemical Properties
| Appearance | Liquid |
| Color | white |
| Storage Condition | -20°C |
| MDL | MFCD00131020 |
| Use | This product is for scientific research only and shall not be used for other purposes. |
enterokinase from porcine intestine - Risk and Safety
| WGK Germany | 3 |
enterokinase from porcine intestine - Introduction
As a tool, protease is used for specific breakage of recombinant fusion proteins, especially for bioengineering pharmaceutical industry, genetic engineering, biochemistry, molecular biology and other research. & & Enzyme Activity Definition: The amount of enzyme required to degrade 0.05 mg of Thioredoxin-NP-27 95% to NP-27 at 37 ℃ within 16 hours is defined as 1 active unit. & & 1 × recombinant bovine enterokinase reaction buffer: 50mM Tris-HCl,pH 8.0(22 ℃),1mM CaCl,0.1% Tween-20. & & influencing factors of enterokinase activity:>2M Urea,>250mM NaCl,>20mM β-ME,>0.1% SDS,>50mM imidazole. If the sample solution contains one or more of the above components, in order to obtain the ideal enzyme digestion result, please dialyze the sample into 1 × reaction buffer first, and then perform the enzyme digestion experiment. & & scope of application: temperature 4~45 ℃,pH4.5~9.5.
Last Update：2022-10-16 17:41:03
enterokinase from porcine intestine - Reference Information
| EPA chemical information | Information provided by: ofmpub.epa.gov (external link) |
| product description | it is reported that the light chain of recombinant enterokinase has the specificity of holoenzyme in vitro, and the enzyme digestion activity of genetically engineered fusion protein substrate is significantly higher than that of purified bovine enterokinase. The source of natural enterokinase is limited, and enterokinase extracted from animal tissues is easy to contaminate other proteins, which brings difficulties to practical application. This requires the production of high purity enterokinase by genetic engineering. Recombinant enterokinase can cleave lysine carboxy-terminal peptide bonds containing four aspartic acids: aspartic acid-aspartic acid-aspartic acid-aspartic acid-lysine (DDDDK). The fusion protein can be effectively cut in a wide pH range (4.5-9.5) and a wide temperature range. Recombinant enterokinase removes the fusion protein located at the N-terminus of the protein to remove unwanted fusion tags. |
| use | character: sterilized liquid. Use of recombinant: biochemical research. It is a serine protease, which can efficiently and specifically hydrolyze the fusion protein expressed by engineering bacteria (the recognition order is-(Asp)4Lys↓-) to release the target protein. Because enterokinase has the characteristics of high specificity and high hydrolysis efficiency, it is widely used in the development of genetic engineering products; it can be used as a protease to specifically identify and cut the substrate containing enterokinase cleavage sites. One of its applications is as a tool for the specific fragmentation of recombinant fusion proteins, especially for bioengineering pharmaceutical industry and genetic engineering, biochemistry, molecular biology and other research. However, the source of natural enterokinase is limited, and enterokinase extracted from animal tissues is contaminated with other proteases, which brings difficulties to practical application. This requires the production of high purity enterokinase by genetic engineering. The high-purity enterokinase activity produced by genetic engineering methods is similar to that of natural enzymes, but the enterokinase cleavage rate is faster |
Last Update：2024-04-09 20:52:54
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CAS: 9014-74-8
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