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
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Enterokinase protein (denatured) (Tag Free) (AB202157)
15% SDS-PAGE analysis of ab202157 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
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.
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
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