E5144
Enterokinase from bovine intestine
powder
Synonyme(s) :
Enteropeptidase
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About This Item
Produits recommandés
Source biologique
bovine intestine
Niveau de qualité
Forme
powder
Poids mol.
150 kDa (consisting of 115kDa and 35kDa subunits.)
Couleur
white
Conditions d'expédition
dry ice
Température de stockage
−20°C
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Description générale
Enterokinase also referred to as enteropeptidase, is a transmembrane protein. This intestinal protease contains a heavy chain and a light chain linked by a disulfide bond. The amino-terminal sequence of the bovine enteropeptidase is homologous to trypsin-like serine proteases. Enterokinase is a highly specific serine protease that is used for the removal of the FLAG peptide from N-terminal and Met-N-terminal fusion proteins. It does not remove the C-terminal FLAG.
Application
Enterokinase from bovine intestine has been used to remove S-Tag and N-terminal His-tag from recombinant glutathione peroxidase 1 (Gpx1). It has also been used to cleave interleukin-2 (IL-2) protein from the granules
Enterokinase is a member of the S1 peptidase family. In vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. Enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags.
Actions biochimiques/physiologiques
Enterokinase catalyzes the proteolytic activation of pancreatic proteases. This action prevents the harmful tissue damage produced by the autoactivation of pancreatic proteases in the pancreas. Enterokinase recognizes Lys or Arg residues in the peptide. Lack of enterokinase can harm food digestion and absorption mechanism. Enterokinase is a highly specific serine protease that is used for the removal of the FLAG peptide from N-terminal and Met-N-terminal fusion proteins. It does not remove the C-terminal FLAG.
Conditionnement
Supplied with optimized enterokinase buffer
Définition de l'unité
One unit is that amount of enterokinase which results in >95% cleavage of 1 µg of purified FLAG-BAP fusion protein in 18 hours at 37 °C. One FLAG-BAP unit is equal to 10x the activity of a standard trypsinogen unit.
Autres remarques
Do not used PVDF since free FLAG peptide will bind to the PVDF membrane.
Substrat
Réf. du produit
Description
Tarif
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
B Thomas Bäckström et al.
BMC biotechnology, 7, 3-3 (2007-01-06)
Fluorescence activated cell sorting (FACS) is a powerful technique for the qualitative and quantitative detection of biomolecules used widely in both basic research and clinical diagnostic applications. Beads displaying a specific antigen are used to bind antibodies which are then
Toni M Antalis et al.
Progress in molecular biology and translational science, 99, 1-50 (2011-01-18)
Serine proteases of the trypsin-like family have long been recognized to be critical effectors of biological processes as diverse as digestion, blood coagulation, fibrinolysis, and immunity. In recent years, a subgroup of these enzymes has been identified that are anchored
A Light et al.
Trends in biochemical sciences, 14(3), 110-112 (1989-03-01)
The serine protease enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The enzyme consists of two subunits linked by a disulfide bond. The heavy chain achors enterokinase in the intestinal brush border membrane
Thomas Zauner et al.
Analytical chemistry, 83(19), 7356-7363 (2011-09-07)
Proteases are widely used in analytical sciences and play a central role in several widespread diseases. Thus, there is an immense need for highly adaptable and sensitive assays for the detection and monitoring of various proteolytic enzymes. We established a
Marine E Gasparian et al.
Protein expression and purification, 79(2), 191-196 (2011-04-26)
Enteropeptidase (synonym: enterokinase, EC 3.4.21.9) is a heterodimeric serine protease of the intestinal brush border that activates trypsinogen by highly specific cleavage of the trypsinogen activation peptide following the sequence (Asp)(4)-Lys. It has also great biotechnological interest because of the
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
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