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Transmembrane protease, serine 15

enterokinase, Enteropeptidase
This gene encodes an enzyme that converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. The precursor protein is cleaved into two chains that form a heterodimer linked by a disulfide bond. This protein is a member of the trypsin family of peptidases. Mutations in this gene cause enterokinase deficiency, a malabsorption disorder characterized by diarrhea and failure to thrive. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Trypsin, ACID, CAN, HAD, Thioredoxin
Papers using enterokinase antibodies
Control of protein functional dynamics by peptide linkers
Xiao Haijuan et al., In International Journal of Medical Sciences, 2004
... High-Affinity Nickel Iminodiacetic Acid (Ni-IDA) Resin and enterokinase were the products of GenScript Corporation (USA) ...
MOLMOL: A program for display and analysis of macromolecular structures
Zhang Yang, In PLoS ONE, 1995
... For GST-Tag™ removal, recombinant enterokinase (rEK; Merck Chemicals Ltd., Nottingham, UK) ...
Papers on enterokinase
Expression of a novel bacteriocin-the plantaricin Pln1-in Escherichia coli and its functional analysis.
Lu et al., Nanjing, China. In Protein Expr Purif, Mar 2016
The fusion protein was purified by Ni-NTA, and thioredoxin was removed by enterokinase.
Expression, purification and characterization of mouse nesfatin-1 in E. coli.
Zhang et al., Nanjing, China. In Biotechnol Appl Biochem, Dec 2015
Six synthetic deoxyoligonucleotides overlapped by PCR encoding nesfatin-1 was cloned into a pET28a vector after the hexa-histidine tagged Multiple Cloning Sites sequence with an enterokinase recognition site incorporated in-between.
Expression and purification of a new recombinant camel hepcidin able to promote the degradation of the iron exporter ferroportin1.
Sari et al., Tunisia. In Protein Expr Purif, Nov 2015
Biologically active recombinant camel hepcidin was obtained thanks to the production of a hepcidin-thioredoxin fusion protein (TRX-HepcD) and a purified camel hepcidin, with an extra methionine at the N-terminus, was obtained after enterokinase cleavage of the fusion protein.
Expression of a glucagon-like peptide-1 analogue, as a therapeutic agent for type II diabetes, with enhanced bioactivity and increased N-terminal homogeneity in Pichia pastoris.
Jin et al., Wuxi, China. In Biotechnol Lett, Nov 2015
We also designed and expressed the novel GLP-1 analogue NGGH, which had a His-tag fused with the N-terminus of GGH and an enterokinase (EK) cleavage site at the fusion junction.
An improved method for high-level soluble expression and purification of recombinant amyloid-beta peptide for in vitro studies.
Tripathi et al., Shillong, India. In Protein Expr Purif, Oct 2015
The Aβ fusion protein was subjected to a Ni-NTA affinity chromatography followed by enterokinase digestion, and the Aβ peptide was purified using glutathione Sepharose affinity chromatography.
Characterization of bioactive recombinant antimicrobial peptide parasin I fused with human lysozyme expressed in the yeast Pichia pastoris system.
Shang et al., Chengdu, China. In Enzyme Microb Technol, Sep 2015
A 4×Gly flexible amino acid linker with an enterokinase cleavage (DDDDK) was designed to link the PI to the C-terminal of hLY.
A High Yield and Cost-efficient Expression System of Human Granzymes in Mammalian Cells.
Walch et al., Fribourg, Switzerland. In J Vis Exp, 2014
The insertion of an enterokinase site at the N-terminus of the protein allowed the generation of active protease that was finally purified by cation exchange chromatography.
Congenital diseases of the gastrointestinal tract.
Lentze, Bonn, Germany. In Georgian Med News, 2014
A variety of congenital diarrheas with disturbances of digestion, hydrolysis, absorption and secretion is described in detail: lactose intolerance, sucrose intolerance, glucose-galactose malabsorption, fructose malabsorption, trehalase and enterokinase deficiency, congenital chloride and sodium diarrhea, congenital hypomagnesaemia, primary bile acid malabsorption, acrodermatitis enteropathica and Menke's syndrome.
Rare genetic diseases with human lean and/or starvation phenotype open new avenues for obesity and type II diabetes treatment.
Harosh, Fontaine, France. In Curr Pharm Biotechnol, 2013
This approach has led to the identification of the congenital enteropeptidase deficiency gene and the Anderson's Disease gene as a potential targets for obesity and type II diabetes treatment.
Several affinity tags commonly used in chromatographic purification.
Liang et al., Chengdu, China. In J Anal Methods Chem, 2012
The most commonly used endopeptidases are enterokinase, factor Xa, thrombin, tobacco etch virus, and human rhinovirus 3C protease.
Dissecting structural basis of the unique substrate selectivity of human enteropeptidase catalytic subunit.
Kirpichnikov et al., Moscow, Russia. In J Biomol Struct Dyn, 2011
Characterization of the different catalytic activity of human and bovine enteropeptidase light chains toward hydrolysis of peptides and proteins lacking tetraaspartate sequence.
Keratinocytes synthesize enteropeptidase and multiple forms of trypsinogen during terminal differentiation.
Hibino et al., Yokohama, Japan. In J Invest Dermatol, 2010
Because mesotrypsin is resistant to naturally occurring trypsin inhibitors, confined expression of the isoforms of mesotrypsinogens and enteropeptidase may indicate that mesotrypsin is involved in keratinocyte terminal differentiation
New advances in cell physiology and pathophysiology of the exocrine pancreas.
Mössner, Leipzig, Germany. In Dig Dis, 2009
Trypsinogen is activated by the gut mucosal enzyme enterokinase.
The trail of my studies on glycoproteins from enterokinase to tumor markers.
Yamashina, Kyoto, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2009
This review describes the results of the author's studies on glycoproteins which have been carried out for more than 50 years.
Substrate specificities of porcine and bovine enteropeptidases toward the peptide Val-(Asp)4-Lys-Ile-Val-Gly and its analogs.
Takahashi et al., Yokohama, Japan. In Biosci Biotechnol Biochem, 2008
substrate specificities of porcine and bovine enteropeptidases were investigated using the peptide Val-(Asp)(4)-Lys-Ile-Val-Gly and its various analogs with mutations in the (Asp)(4)-Lys sequence as substrates
Intracellular co-localization of trypsin-2 and matrix metalloprotease-9: possible proteolytic cascade of trypsin-2, MMP-9 and enterokinase in carcinoma.
Salo et al., Helsinki, Finland. In Exp Cell Res, 2008
Enterokinase directly cleaved proMMP-9 at the Lys65-Ser66 site.
A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitis.
Férec et al., Berlin, Germany. In Nat Genet, 2006
Upon activation by enterokinase or trypsin, purified recombinant G191R protein showed a complete loss of trypsin activity owing to the introduction of a new tryptic cleavage site that renders the enzyme hypersensitive to autocatalytic proteolysis.
Expression of enteropeptidase in differentiated enterocytes, goblet cells, and the tumor cells in human duodenum.
Kitamoto et al., Kumamoto, Japan. In Am J Physiol Gastrointest Liver Physiol, 2003
Produced in enterocytes and goblet cells. Localization on brush border of cells for physiological activation of digestive enzymes. In duodenal polyps and adenocarcinoma at duodenum but not in Brunner's gland adenoma.
Production of biologically active salmon calcitonin in the milk of transgenic rabbits.
Cottingham et al., Edinburgh, United Kingdom. In Nat Biotechnol, 1998
Expression of a fusion protein comprising human alpha lactalbumin joined by an enterokinase cleavable linker to sCT was directed to the mammary gland under the control of the ovine beta lactoglobulin promoter.
Domains specifying thrombin-receptor interaction.
Coughlin et al., San Francisco, United States. In Nature, 1991
By replacing this cleavage site with the cleavage site for enterokinase, we have created a functional enterokinase receptor.
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