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ChemicalBook--->CAS DataBase List--->9014-74-8

9014-74-8

9014-74-8 Structure

9014-74-8 Structure
IdentificationBack Directory
[Name]

ENTEROKINASE
[CAS]

9014-74-8
[Synonyms]

REK
ENTK
PRSS7
TMPRSS15
EC 3.4.21.9
ENTEROKINASE
ENTEROPEPTIDASE
Serine protease 7
Peptidase, entero-
ENTEROKINASE, BOVINE
RECOMBINANT ENTEROKINASE
Native Calf Enterokinase
ENTEROKINASE, LIGHT CHAIN
Enteropeptidasefromporcine
Native Bovine Enterokinase
Native Porcine Enterokinase
ENTEROPEPTIDASE, LIGHT CHAIN
Bovine TMPRSS15 Protein, His Tag
enterokinase from porcine intestine
Recombinant Bovine Enterokinase(rEK)
Enterokinase from Human, Recombinant
Enteropeptidase catalytic light chain
Enteropeptidase non-catalytic heavy chain
Enterokinase solution from calf intestine
Enterokinase from bovine intestine, Recombinant
Enterokinase from porcine intestine,Enteropeptidase
ENTEROPEPTIDASE FROM PORCINE INTESTINE LYOPHILIZED POWDER
[EINECS(EC#)]

232-761-1
[Molecular Formula]

NULL
[MDL Number]

MFCD00131020
Chemical PropertiesBack Directory
[Definition]

An enzyme found in the small intestine, which converts trypsinogen into trypsin.
[storage temp. ]

−20°C
[form ]

salt-free, lyophilized powder
[color ]

white
[CAS DataBase Reference]

9014-74-8
[EPA Substance Registry System]

Peptidase, entero- (9014-74-8)
Safety DataBack Directory
[Symbol(GHS) ]


GHS07,GHS08
[Signal word ]

Danger
[Hazard statements ]

H315-H319-H334-H335
[Precautionary statements ]

P261-P284-P304+P340-P305+P351+P338-P342+P311
[WGK Germany ]

3
Hazard InformationBack Directory
[Uses]

Typical conditions for fusion protein cleavage:
Adjust the concentration of the fusion protein to 1.5 mg/ml and a pH between 7.0-8.0 with 500 mM Tris-HCl, pH 8.0, 2.0 mM CaCl2, and 1% Tween? 20
Add enterokinase to fusion protein solution at a ratio of ~ 0.02 units per 1 mg fusion protein and mix
Incubate reaction mixture at ~25 °C for 16 hours
[General Description]

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.
[Biochem/physiol Actions]

Enterokinase is a membrane bound serine protease that specifically and rapidly converts trypsinogen to trypsin, thereby, triggering the conversion of other zymogens to active enzymes. It has a molecular mass of approximately 150 kDa. The enzyme is a heterodimer consisting of 35-47 kDa subunits. The light and the heavy chains are linked by two disulfide bridges. It is a glycoprotein containing 35% carbohydrate. The polypeptide chain of trypsinogen is hydrolyzed only after an -(Asp)4-Lys- sequence. The enzyme is inhibited by soybean trypsin inhibitor. Enterokinase is typically used in protein modification and amino acid sequence determination.
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