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TMPRSS15 encodes an enzyme that converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. Zusätzlich bieten wir Ihnen Transmembrane Protease, serine 15 Antikörper (70) und Transmembrane Protease, serine 15 Kits (18) und viele weitere Produktgruppen zu diesem Protein an.
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Pig (Porcine) TMPRSS15 Protein expressed in Yeast - ABIN1574313
Palmai-Pallag, Khodabukus, Kinarsky, Leir, Sherman, Hollingsworth, Harris: The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane-tethered mucins. in The FEBS journal 2005
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Pig (Porcine) TMPRSS15 Protein expressed in Yeast - ABIN2017741
Hariharan, Liang, Chou, Chin: A new model for ligand release. Role of side chain in gating the enediyne antibiotic. in The Journal of biological chemistry 2006
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Cow (Bovine) TMPRSS15 Protein expressed in Yeast - ABIN2001848
Zhu, Dai, Zhang, Li, Fang, Wang, Jiang, Yu, Xia, Niu, Guo, Teng: Structural insights into the neutralization mechanism of monoclonal antibody 6C2 against ricin. in The Journal of biological chemistry 2013
substrate specificities of porcine and bovine enteropeptidases were investigated using the peptide Val-(Asp)(4)-Lys-Ile-Val-Gly and its various analogs with mutations in the (Asp)(4)-Lys 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 is resistant to naturally occurring trypsin inhibitors, confined expression of the isoforms of mesotrypsinogens and enteropeptidase may indicate that mesotrypsin is involved in keratinocyte terminal differentiation
Engineered recombinant enteropeptidase catalytic subunit: effect of N-terminal modification
Produced in enterocytes and goblet cells. Localization on brush border of cells for physiological activation of digestive enzymes. In duodenal polyps and adenocarcinoma at duodenum but not in Brunner's gland adenoma.
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)