E5144
Enterokinase from bovine intestine
powder
Synonym(s):
Enteropeptidase
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50 UNITS
$400.00
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50 UNITS
$400.00
About This Item
$400.00
Check Cart for Availability
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biological source
bovine intestine
Quality Level
form
powder
mol wt
150 kDa (consisting of 115kDa and 35kDa subunits.)
color
white
shipped in
dry ice
storage temp.
−20°C
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General description
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.[1] 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).[2] It has also been used to cleave interleukin-2 (IL-2) protein from the granules[3]
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.
Biochem/physiol Actions
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.[1] 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.[2]
Packaging
Supplied with optimized enterokinase buffer
Unit Definition
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.
Other Notes
Do not used PVDF since free FLAG peptide will bind to the PVDF membrane.
substrate
Product No.
Description
Pricing
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Toni M Antalis et al.
Progress in molecular biology and translational science, 99, 1-50 (2011-01-18)
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Acute pancreatitis is a life-threatening inflammatory disease characterized by abdominal pain of unknown etiology. Trypsin, a key mediator of pancreatitis, causes inflammation and pain by activating protease-activated receptor 2 (PAR(2)), but the isoforms of trypsin that cause pancreatitis and pancreatic
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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
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