CAS 9014-74-8
:Enteropeptidase
Description:
Enteropeptidase, also known as enterokinase, is a serine protease enzyme primarily produced in the duodenum, where it plays a crucial role in the digestive process. It catalyzes the conversion of trypsinogen to trypsin, an essential step in protein digestion. Enteropeptidase is a glycoprotein, which means it has carbohydrate groups attached to its polypeptide chain, influencing its stability and activity. The enzyme is highly specific, recognizing a particular amino acid sequence in its substrates. Its activity is optimal at a slightly alkaline pH, reflecting the conditions in the small intestine. Enteropeptidase is also significant in clinical settings, as it can be used in various biotechnological applications, including protein purification and the study of proteolytic processes. The CAS number 9014-74-8 uniquely identifies this enzyme in chemical databases, facilitating research and regulatory compliance. Overall, enteropeptidase is vital for proper digestion and nutrient absorption, highlighting its importance in both physiology and biochemistry.
Formula:Unspecified
Synonyms:- E.C. 3.4.21.9
- E.C. 3.4.4.8
- Ec 3.4.21.9
- Ec 3.4.4.8
- Enterokinase
- Enterokinase From Calf Intestine
- Enterokinases
- Enteropeptidase
- Enteropeptidases
- Peptidase, entero-
- Recombinant enterokinase,from E.coli
- See more synonyms
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Found 3 products.
Recombinant enterokinase
CAS:<p>Entorokinase (also known as enteropeptidase; EC 3.4.21.9) is a proteolytic enzyme (proteinase) that activates trypsinogen into its active form, trypsin. One unit of Entorokinase will produce 1.0 nmole of trypsin from trypsinogen per min at pH 5.6 and 25 °C.</p>Enteropeptidase
CAS:<p>Enteropeptidase (historic name entorokinase; EC 3.4.21.9) is a proteolytic enzyme (proteinase) that activates trypsinogen into its active form, trypsin. One unit of enteropeptidase will produce 1.0 nmole of trypsin from trypsinogen per min at pH 5.6 and 25 °C.</p>Purity:Min. 95%
