Enterokinase, Bovine Active Protein | TMPRSS15 active protein

Enterokinase, Recombinant, Bovine (Enteropeptidase)

Cat. Num. AAA636836

• Gene Names: TMPRSS15; ENTK; PRSS7
• Purity: Highly Purified; 90%, as determined by SDS-PAGE and visualized by silver stain.
• Synonyms: Enterokinase; Bovine; Recombinant; Bovine (Enteropeptidase); TMPRSS15 active protein

• Purity/Purification: Highly Purified; 90%, as determined by SDS-PAGE and visualized by silver stain.
• Form/Format: Supplied as a liquid in 20mM HEPES, 50mM NaCl, 50% glycerol, pH 6.8.

• Activity: Measured by its ability to cleave the chromogenic substrate, thiobenzyl benzyloxycarbonyl-L- lysinate (Z-Lys-SBzl) in the presence of 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB). Cleavage of the substrate was measured by monitoring the rate of 3-carboxy-4-nitrothiophenoxide production from the absorbance changes at 405 nm, using the extinction coefficient 13260 M-1 cm-1. The specific activity, measured with 100 M substrate and 2 ng enzyme in 50 mM Tris/HCl, pH 7.4 at room temperature, is > 35 nmoles/min/ g. rbEnterokinase can cleave fusion proteins having an accessible Enterokinase cleavage site (DDDDK). At an average ratio for fusion protein:rbEnterokinase of 1000:1 (w/w), cleavage up to 90% completion is achieved within one hour at room temperature. Non-specific cleavage at basic residues has also been observed for some proteins. It is recommended that cleavage reaction be optimized for each fusion protein. The reaction may be terminated by passing the sample through a soybean trypsin inhibitor (SBTI)-agarose affinity column to remove the rbEnterokinase from the reaction mixture. SBTI inhibits rbEnterokinase with a K i of 1.6 nM (Lu, D., et al., 1997, J. Biol. Chem. 272:31293).
• Endotoxin Level: < 1.0 EU per 1 g of the protein as determined by the LAL method.
• Preparation and Storage: Samples are stable for up to six months at -20 degree C in a manual defrost freezer from the date of receipt. The protein can be aliquoted and stored at -20 degree C in a manual defrost freezer for three months without a significant loss of activity. Avoid repeated freeze-thaw cycles.

Related Product Information for TMPRSS15 active protein

EK initiates activation of pancreatic proteases by converting trypsinogen to trypsin, which in turn activates chymotrypsin, carboxypeptidases and elastases. Located in intestinal brush border, it is a disulfide bond linked dimer of the heavy and light chains, which are derived from the same single-chain precursor. The multidomain-containing heavy chain consists of a short cytoplamic tail, a transmembrane, a SEA, a SRCR, a MAM, two CUB and two LDL-receptor class A domains. The light chain contains the catalytic domain of trypsin-like serine proteases. The purified recombinant bovine EK (residues 788-1035) corresponds to a disulfide bond-linked dimer that consists of the C-terminal fragment of the heavy chain (residues 788-800) and the light chain (residues 801-1035).

Product Categories/Family for TMPRSS15 active protein

Molecular Biology; MB-Enzymes

NCBI and Uniprot Product Information

• NCBI GI #: 223942069
• NCBI GeneID: 5651
• NCBI Accession #: NP_002763.2
• NCBI GenBank Nucleotide #: NM_002772.2
• UniProt Accession #: P98073; Q2NKL7
• Molecular Weight: Based on N-terminal amino acid sequencing, the recombinant bovine Enterokinase has two chains, with N-termini starting at Ala-Cys 788 and Ile 801, corresponding to the C-terminal fragment of the heavy chain (Ala-Cys 788-Lys 800) and light chain (Ile 801-H
• NCBI Official Full Name: enteropeptidase
• NCBI Official Synonym Full Names: transmembrane protease, serine 15
• NCBI Official Symbol: TMPRSS15
• NCBI Official Synonym Symbols: ENTK; PRSS7
• NCBI Protein Information: enteropeptidase; enterokinase; serine protease 7; protease, serine, 7 (enterokinase)
• UniProt Protein Name: Enteropeptidase
• Protein Family: Enteropeptidase
• UniProt Gene Name: TMPRSS15
• UniProt Synonym Gene Names: ENTK; PRSS7
• UniProt Entry Name: ENTK_HUMAN

NCBI Description

This gene encodes an enzyme that converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. The precursor protein is cleaved into two chains that form a heterodimer linked by a disulfide bond. This protein is a member of the trypsin family of peptidases. Mutations in this gene cause enterokinase deficiency, a malabsorption disorder characterized by diarrhea and failure to thrive. [provided by RefSeq, Jul 2008]

Uniprot Description

PRSS7: 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. Defects in TMPRSS15 are a cause of enterokinase deficiency (ENTKD); a life-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive. Belongs to the peptidase S1 family.

Protein type: Protease; EC 3.4.21.9; Membrane protein, integral

Chromosomal Location of Human Ortholog: 21q21.1

Cellular Component: integral to membrane; brush border

Molecular Function: serine-type endopeptidase activity; scavenger receptor activity

Biological Process: receptor-mediated endocytosis; proteolysis

Disease: Enterokinase Deficiency