| Cat. No. |
CRP08116 |
| Product Overview |
Recombinant Bovine
Enterokinase produced in Pichia. Pastoris is a single glycosylated
polypeptide chain containing 235 amino acids and having a molecular
mass of approximately 43.0 kDa. |
| Description |
Enterokinase is a
serine proteinase in the duodenum that plays a critical role in
mammalian digestion. It is the physiological activator of pancreatic
trypsinogen. It converts trypsinogen into its active form trypsin,
by cleaving its aminoterminal hexapeptide Val(Asp)4-Lys. More
recently, the enterokinase has been shown to have a broad utility in
cleaving fusion proteins produced in Escherichia coli. The enzyme is
particularly suitable for this role because of its high degree of
specificity, its tolerance to a wide range of reaction conditions,
and the fact that its recognition sequence lies entirely on the
aminoterminal side of the scissile bond. This enzymatic activity
allows release of carboxyl-terminal fusion partners from fusion
proteins without leaving unwanted amino acid residues on their amino
termini. |
| Unit Definition |
One unit is defined
as the amount of enzyme needed to cleave 50 ug of fusion protein in
16 hours to 95% completion at 25°C in a buffer containing 25 mM
Tris-HCl, pH 7.6, 50 mM NaCl, and 2 mM CaCl2. |
| Formulation |
50 mM Tris-HCl, pH
8.0, 0.5M NaCl and 50% glycerol. |
| Physical Appearance |
Sterile liquid |
| Endotoxin |
Less than 1EU/mg of
rbEK as determined by LAL method. |
| Storage |
One year when stored
at -20°C. Avoid repeated freeze/thaw cycles. |
| Gene Information
|
Gene Name |
protease, serine, 7 (enterokinase)
|
|
Synonyms |
PRSS7; EC 3.4.21.9;
ENTK; Enterokinase; MGC133046; enterokinase; enteropeptidase;
proenterokinase; Enteropeptidase precursor; Serine protease 7; human
enterokinase;EC 3.4.21.9; protease, serine, 7; serine protease
(enterokinase). |
|
GeneID |
282009 |
|
mRNA Refseq |
NM_174439 |
|
Protein Refseq |
NP_776864 |
|
Enzyme Commission Number |
EC
3.4.21.9 |
|
UniProt ID |
P98072 |
|
Chromosome Location |
1 |
|
Reaction |
The reaction
catalysed by Enteropeptidase:
trypsinogen → trypsin + octapeptide
Enteropeptidase cleaves after Lysine if the Lys is preceded by four
Asp and not followed by a Pro. |
|
Function |
peptidase activity;scavenger receptor activity |
|
-humo.png) |
Download Datasheet
 |
|
Crystal
structure of Enteropeptidase with an inhibitor
protease, serine, 7
(human) |
|