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E0885

Enterokinase from porcine intestine

lyophilized powder, ≥100 units/mg protein

Synonym(s):

Enteropeptidase

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Pack SizeSKUAvailabilityPrice
40 units
Please contact Customer Service for Availability
$411.00
200 units
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$1,670.00

About This Item

CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-761-1
NACRES:
NA.54
MDL number:
EC Number:
Specific activity:
≥100 units/mg protein

$411.00


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form

lyophilized powder

Quality Segment

specific activity

≥100 units/mg protein

mol wt

150 kDa

purified by

chromatography

composition

Protein, ≥20% Lowry

foreign activity

aminopeptidase ≤1.5%, trypsin ≤1%, free

storage temp.

−20°C

Application

Enterokinase from porcine intestine has been used in a study to investigate complementary DNA cloning and sequencing of rat enteropeptidase. Enterokinase from porcine intestine has also been used to learn more about the insulinotropic region of the gastric inhibitory polypeptide.
The enzyme from Sigma has been used to activate zymogens in order to detect trypsin activity. The study to investigated the structural and evolutionary consequences of unpaired cysteines in trypsinogen.[1] The product has been used to measure trypsin while studying the effect of pesticide induced alterations in gene expression in the lobster, Homarus americanus[2] The enzyme from Sigma has been used to develop a novel assay for measuring levels of lipid-free apoA-I in the presence of lipid-bound apoA-I. Enteropeptidase can specifically cleave human lipid-free apoA-I but not its lipid-bound form resulting in an N-terminal fragment of 22 kDa.[3] It has also been used in a study to examine the effect of calcium and phytic acid on the activation of trypsinogen and the stability of trypsin.

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.

Physical form

Lyophilized powder containing sodium phosphate buffer salts

Other Notes

One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25 °C.

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This Item
E0632E0127C9584
specific activity

≥100 units/mg protein

specific activity

≥0.5 units/mg solid

specific activity

≥4.0 units/mg protein

specific activity

≥125 units/mg protein

form

lyophilized powder

form

salt-free, lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

150 kDa

mol wt

150 kDa

mol wt

25.9 kDa

mol wt

34,000 Da± 600

foreign activity

aminopeptidase ≤1.5%, trypsin ≤1%, free

foreign activity

-

foreign activity

-

foreign activity

carboxypeptidase A ≤1%, chymotrypsin ≤0.1%, trypsin ≤5%

purified by

chromatography

purified by

-

purified by

-

purified by

affinity chromatography


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Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Global Trade Item Number

SKUGTIN
E0885-200UN04061833601273
E0885-40UN04061833601280

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