Enzymes
Product List
Enterokinase Bovine His
Enteropeptidase/ Enterokinase Bovine Recombinant His Tag
The Enterokinase Bovine is purified by proprietary chromatographic techniques.
Enterokinase Human
Enteropeptidase/ Enterokinase, Light Chain Human Recombinant
Enterokinase Human produced in E.Coli cells is a single, non-glycosylated polypeptide chain containing 237 amino acids (785-1019aa ) and having a molecular mass of 26.4kDa. Enterokinase is purified by proprietary chromatographic techniques
Enterokinase Porcine
Enteropeptidase/ Enterokinase Porcine
If a fusion tag is located in the N-terminus with an enterokinase site, enterokinase will be able to remove the fusion tag and to generate the protein exactly as you need without adding any unwanted residues. THE BioTek’s enterokinase is a highly purified enterokinase from porcine. The enzyme has been extensively purified and tested to ensure that there are no other contaminating proteases.
PROK Tritirachium album
Tritirachium album Proteinase-K Recombinant
Enterokinase Bovine
Enteropeptidase/ Enterokinase Light Chain Bovine Recombinant
Enterokinase (rEK) Bovine Recombinant is the catalytic subunit of bovine enterokinase, which is expressed by E. Coli and purified to yield a high enzyme activity preparation. EK recognizes the sequence Asp-Asp-Asp-Asp-Lys and cleaves the peptide bond after the lysine residue. The enzyme can be used to cleave any fusion protein that carries this sequence. Recombinant Bovine Enterokinase is a single glycosylated polypeptide chain containing 235 amino acids and having an MW of ~28kDa.
Introduction
Enterokinase, also known as enteropeptidase, is a serine protease enzyme produced by the cells of the duodenum. It plays a crucial role in the digestive system by converting trypsinogen, an inactive zymogen, into its active form, trypsin. This activation initiates a cascade of proteolytic reactions essential for the digestion of proteins . Enterokinase is classified under the enzyme commission number EC 3.4.21.9 and belongs to the chymotrypsin-clan of serine proteases .
Key Biological Properties: Enterokinase is a type II transmembrane serine protease localized to the brush border of the duodenal and jejunal mucosa. It consists of a disulfide-linked heavy chain (82-140 kDa) that anchors it to the membrane and a light chain (35-62 kDa) that contains the catalytic subunit .
Expression Patterns and Tissue Distribution: Enterokinase is primarily expressed in the duodenum, the first section of the small intestine. It is produced by the glands of Brunner in the duodenal mucosa and is resistant to destruction by various enzymes in the small intestine .
Primary Biological Functions: The primary function of enterokinase is to activate trypsinogen into trypsin, which then activates other pancreatic digestive enzymes, facilitating the breakdown of proteins into absorbable amino acids .
Role in Immune Responses and Pathogen Recognition: While enterokinase’s primary role is in digestion, its activity indirectly supports immune responses by ensuring proper protein digestion and nutrient absorption, which are vital for maintaining overall health and immune function .
Mechanisms with Other Molecules and Cells: Enterokinase specifically cleaves the acidic propeptide from trypsinogen to yield active trypsin. This cleavage initiates a cascade of proteolytic reactions leading to the activation of many pancreatic zymogens .
Binding Partners and Downstream Signaling Cascades: Enterokinase binds to trypsinogen and catalyzes its conversion to trypsin. The activated trypsin then activates other digestive enzymes, creating a cascade effect essential for efficient protein digestion .
Regulatory Mechanisms Controlling Expression and Activity: Enterokinase is synthesized as a zymogen, proenteropeptidase, which requires activation by duodenase or trypsin. This regulation ensures that enterokinase is activated only in the appropriate location and context .
Transcriptional Regulation and Post-Translational Modifications: The expression of enterokinase is regulated at the transcriptional level, and its activity is controlled through post-translational modifications, including cleavage by other proteases .
Biomedical Research: Enterokinase is used in research to study protein digestion and enzyme activation mechanisms. It is also employed in the production of recombinant proteins by cleaving fusion proteins at specific sites .
Diagnostic Tools and Therapeutic Strategies: Enterokinase’s specificity for certain peptide sequences makes it a valuable tool in diagnostic assays and therapeutic applications, including the production of therapeutic proteins and antibodies .
Role Throughout the Life Cycle: Enterokinase plays a critical role in the digestive process throughout an individual’s life. From infancy, where it aids in the digestion of maternal milk proteins, to adulthood, where it continues to facilitate protein digestion. Its activity is essential for maintaining proper nutrition and overall health .
From Development to Aging and Disease: Proper functioning of enterokinase is crucial for growth and development. Deficiencies or malfunctions in enterokinase activity can lead to digestive disorders and malnutrition, impacting overall health and longevity .
