Recombinant Human Enterokinase protein (denatured) is a Human Fragment protein, in the 785 to 1019 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
M A I V G G S N A K E G A W P W V V G L Y Y G G R L L C G A S L V S S D W L V S A A H C V Y G R N L E P S K W T A I L G L H M K S N L T S P Q T V P R L I D E I V I N P H Y N R R R K D N D I A M M H L E F K V N Y T D Y I Q P I C L P E E N Q V F P P G R N C S I A G W G T V V Y Q G T T A N I L Q E A D V P L L S N E R C Q Q Q M P E Y N I T E N M I C A G Y E E G G I D S C Q G D S G G P L M C Q E N N R W F L A G V T S F G Y K C A L P N R P G V Y A R V S R F T E W I Q S F L H
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
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.
Alternative names
ENTK, PRSS7, TMPRSS15, Enteropeptidase, Enterokinase, Serine protease 7, Transmembrane protease serine 15
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Recombinant Human Enterokinase protein (denatured) is a Human Fragment protein, in the 785 to 1019 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- P98073-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl
Sequence info
Amino acid sequence
- M A I V G G S N A K E G A W P W V V G L Y Y G G R L L C G A S L V S S D W L V S A A H C V Y G R N L E P S K W T A I L G L H M K S N L T S P Q T V P R L I D E I V I N P H Y N R R R K D N D I A M M H L E F K V N Y T D Y I Q P I C L P E E N Q V F P P G R N C S I A G W G T V V Y Q G T T A N I L Q E A D V P L L S N E R C Q Q Q M P E Y N I T E N M I C A G Y E E G G I D S C Q G D S G G P L M C Q E N N R W F L A G V T S F G Y K C A L P N R P G V Y A R V S R F T E W I Q S F L H
- Accession
- P98073
- Protein length
- Fragment
- Predicted molecular weight
- 26.4 kDa
- Amino acids
- 785 to 1019
- Nature
- Recombinant
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.
Storage
- 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
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
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.
- Associated diseases and disorders
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.
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1 product image
SDS-PAGE - Recombinant Human Enterokinase protein (denatured) (ab202157)
15% SDS-PAGE analysis of ab202157 (3μg).
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