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TMPRSS15 encodes an enzyme that converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. Additionally we are shipping Transmembrane Protease, serine 15 Proteins (28) and Transmembrane Protease, serine 15 Kits (16) and many more products for this protein.
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substrate specificities of porcine and bovine enteropeptidases were investigated using the peptide Val-(Asp)(4)-Lys (show LYZ Antibodies)-Ile-Val-Gly and its various analogs with mutations in the (Asp)(4)-Lys (show LYZ Antibodies) sequence as substrates
The Y174R variant showed improved specificities for substrates containing the sequences DDDDK (kcat/KM = 6.83 x 106 M-1 sec-1) and DDDDR (kcat/KM = 1.89 x 107 M-1 sec-1) relative to all other enteropeptidase variants reported to date.
Enteropeptidase is a gene associated with a starvation human phenotype and a novel target for obesity treatment
Human enteropeptidase shows 10x faster kinetics compared to other animal sources but low solubility under low salt conditions. A supercharged variant of enteropeptidase light chain with increased solubility was used for crystallization.
Characterization of the different catalytic activity of human and bovine enteropeptidase light chains toward hydrolysis of peptides and proteins lacking tetraaspartate sequence.
Because mesotrypsin (show PRSS3 Antibodies) is resistant to naturally occurring trypsin inhibitors, confined expression of the isoforms of mesotrypsinogens and enteropeptidase may indicate that mesotrypsin (show PRSS3 Antibodies) is involved in keratinocyte terminal differentiation
Engineered recombinant enteropeptidase catalytic subunit: effect of N-terminal modification
Enterokinase directly cleaved proMMP-9 at the Lys65-Ser66 site.
Enteropeptidase could inhibit osteoclastogenesis in vitro through the cleavage of RANK.
peptide sequencing of amino terminus of light chain of cow enterokinase, identifying the cleavage site
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.
, melanization protease 2
, prophenoloxidase-activating enzyme
, serine protease 7
, transmembrane protease, serine 7
, transmembrane protease serine 7
, protease, serine, 7 (enterokinase)
, transmembrane protease serine 15
, enteropeptidase, light chain (L chain)