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AB202157

Recombinant Human Enterokinase protein (denatured) (Tag Free)

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Recombinant Human Enterokinase protein (denatured) (Tag Free) is a Human Fragment protein, in the 785 to 1019 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

ENTK, PRSS7, TMPRSS15, Enteropeptidase, Enterokinase, Serine protease 7, Transmembrane protease serine 15

1 Images
SDS-PAGE - Recombinant Human Enterokinase protein (denatured) (Tag Free) (AB202157)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Enterokinase protein (denatured) (Tag Free) (AB202157)

15% SDS-PAGE analysis of ab202157 (3μg).

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P98073

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MAIVGGSNAKEGAWPWVVGLYYGGRLLCGASLVSSDWLVSAAHCVYGRNLEPSKWTAILGLHMKSNLTSPQTVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQQMPEYNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQSFLH","proteinLength":"Fragment","predictedMolecularWeight":"26.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":1019,"aminoAcidStart":785,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P98073","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Enterokinase also known as enteropeptidase is a serine protease enzyme with a significant role in the digestive process. It exhibits a mass of approximately 150 kDa and predominantly localizes in the brush border of the small intestine particularly in the duodenum. Enterokinase activates trypsinogen to trypsin by cleaving a specific lysine-isoleucine peptide bond which is a critical step in protein digestion. This enzyme exists as a membrane-bound protein facilitating its interaction with substrates within the intestinal lumen.
Biological function summary

Enterokinase triggers the activation cascade of pancreatic serine proteases necessary for protein breakdown. It acts as a gateway enzyme for the activation of several inactive enzymes into their active forms. Enterokinase functions independently and is not part of a large protein complex. Its role ensures efficient conversion of digestive enzymes like trypsinogen highlighting its importance in nutrient assimilation.

Pathways

Enterokinase plays a role in the digestive enzyme activation pathway specifically initiating the conversion of key proenzymes into active forms. The enzyme is integral to the protein digestion pathway along with other proteases like trypsin and chymotrypsin which further break down proteins into peptides and amino acids. Enterokinase's activity is essential for the downstream function of these proteases emphasizing its place at the pathway's front line.

Enterokinase deficiency can lead to severe protein malnutrition as seen in enterokinase deficiency disorder which results in an inability to fully digest dietary proteins. Additionally alterations in enterokinase function may relate to digestive disturbances and pancreatic disorders. This relationship underlines the enzyme's connection with trypsin heightened in cases where trypsinogen conversion is impaired further affecting digestive efficiency.

Specifications

Form

Liquid

Additional notes

ab202157 was purified by conventional chromatography techniques.

General info

Function

Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.

Sequence similarities

Belongs to the peptidase S1 family.

Post-translational modifications

The chains are derived from a single precursor that is cleaved by a trypsin-like protease.

Product protocols

Target data

Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
See full target information TMPRSS15

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