Skip to Content
Merck
All Photos(1)

Documents

Safety Information

E5144

Sigma-Aldrich

Enterokinase from bovine intestine

powder

Synonym(s):

Enteropeptidase

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

CAS Number:
9014-74-8
Enzyme Commission number:
3.4.21.9 (BRENDA, IUBMB)
EC Number:
232-761-1
MDL number:
MFCD00131020
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.56

biological source

bovine intestine

Quality Level

200

form

powder

mol wt

150 kDa (consisting of 115kDa and 35kDa subunits.)

color

white

shipped in

dry ice

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

Related Categories

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. 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.

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. 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.

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

E5144-50UN-KC:
E5144-BULK-N:
E5144-250UN:
E5144-PH:
E5144-50UN-PW:
E5144-50UN:
E5144PROC:
E5144-VAR:
E5144-BULK:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
Claude Castella et al.
Nitric oxide : biology and chemistry, 68, 125-136 (2017-02-15)
Plant glutathione peroxidases (Gpx) catalyse the reduction of various peroxides, such as hydrogen peroxide (H
Eugene P Ceppa et al.
American journal of physiology. Gastrointestinal and liver physiology, 300(6), G1033-G1042 (2011-03-26)
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
Yunfeng Zhao et al.
FEBS letters, 587(18), 2958-2964 (2013-08-21)
Enteropeptidase can cleave trypsinogen on the sequence of Asp-Asp-Asp-Asp-Lys and plays an important role in food digestion. The RANKL-RANK signalling pathway plays a pivotal role in bone remodelling. In this study, we reported that enteropeptidase can inhibit the RANKL-RANK signalling
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service