Enterokinase Porcine

Enteropeptidase/ Enterokinase Porcine
Cat. No.
BT17386
Source
Porcine.
Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
Appearance
Sterile Liquid.
Purity
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Porcine enteropeptidase is a specific protease which cleaves after the lysine at its recognition site: Asp-Asp-Asp-Asp-Lys. Enterokinase will not cleave a site followed by proline. Theoretical Mw is 21,880 Dalton, the apparent Mw on SDS-PAGE is about 40 kDa.
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. ProSpec’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.

Product Specs

Introduction
Enteropeptidase, also known as enterokinase, plays a crucial role in human digestion. Produced by cells lining the duodenum, it is secreted into the duodenum from specialized glands called the crypts of Lieberkühn when food enters from the stomach. The enzyme's primary function is to convert trypsinogen (an inactive precursor) into its active form, trypsin. This activation is essential as it triggers a cascade, activating numerous other pancreatic digestive enzymes. Enteropeptidase belongs to the serine protease family (EC 3.4.21.9), specifically the chymotrypsin clan, sharing structural similarities with these enzymes.
Description
Porcine enteropeptidase is a highly specific protease that cleaves peptide bonds after the amino acid lysine within its recognition sequence: Asp-Asp-Asp-Asp-Lys. Importantly, it does not cleave if the recognition site is followed by proline. This enzyme has a theoretical molecular weight of 21,880 Daltons, while its apparent molecular weight on SDS-PAGE is approximately 40 kDa. When a fusion tag is engineered into the N-terminus of a protein with an enterokinase recognition site, enteropeptidase can precisely remove the tag. This results in the generation of the target protein with its intended sequence, without any unwanted residues. THE BioTek's enteropeptidase is a highly purified form derived from porcine. The enzyme undergoes rigorous purification and testing to guarantee the absence of any contaminating proteases.
Physical Appearance
Clear, colorless liquid.
Formulation
Supplied as a solution at a concentration of 2 IU/µl in 50mM Tris-HCl buffer (pH 8.0), containing 0.5M NaCl and 50% glycerol.
Stability
Stable for one year when stored at -20°C. Can be kept at room temperature for up to one week.
Unit Definition
One unit (IU) of enzyme activity is defined as the amount of enteropeptidase required to cleave 50 micrograms of a fusion protein substrate at its specific recognition site, achieving 95% completion in 16 hours at 25°C. This reaction is carried out in a buffer composed of 25mM Tris-HCl (pH 7.6), 50mM NaCl, and 2mM CaCl2.
Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
Source
Porcine.

Product Science Overview

Discovery and Historical Significance

Enteropeptidase was first discovered by Ivan Pavlov, a renowned physiologist who was awarded the Nobel Prize in Physiology or Medicine in 1904 for his studies on gastrointestinal physiology . Pavlov’s student, N. P. Schepowalnikov, demonstrated that duodenal secretions could activate pancreatic proteolytic enzymes, leading to the identification of enteropeptidase as a key activator of these enzymes .

Structure and Function

Enteropeptidase is a type II transmembrane serine protease localized to the brush border of the duodenal and jejunal mucosa . It is synthesized as a zymogen (proenteropeptidase) that requires activation by another protease, such as trypsin or duodenase . The enzyme consists of a disulfide-linked heavy chain (82-140 kDa) that anchors it to the intestinal brush border membrane and a light chain (35-62 kDa) that contains the catalytic subunit .

The primary function of enteropeptidase is to convert trypsinogen, an inactive zymogen, into its active form, trypsin . This activation is crucial because trypsin, in turn, activates other pancreatic digestive enzymes, facilitating the breakdown of proteins in the small intestine .

Physiological Role

Enteropeptidase is essential for proper digestion and nutrient absorption. In the absence of this enzyme, the activation of trypsinogen is impaired, leading to significant digestive issues . The enzyme’s activity ensures that digestive enzymes are activated only in the intestine, preventing premature activation that could damage the pancreas and other tissues .

Research and Clinical Implications

Extensive research has been conducted on enteropeptidase, focusing on its structure, function, and role in various physiological processes . Studies have also explored the enzyme’s involvement in certain disorders and potential inhibitors that could modulate its activity . Understanding enteropeptidase’s mechanisms and interactions can provide insights into developing therapeutic interventions for digestive disorders and other related conditions .

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