Anti-ECS Antibody

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.

Immunoblotting: use at a dilution of 1:1,000- 1:20,000. <br><br>Immunocytochemistry: use at a dilution of 1:100-1:400. <br><br>ELISA: for detection use at a dilution of 1:1,000-1:30,000; for coating use at a dilution of 1:100-1:500. <br><br>Immunoprecipitation: use 1-4ug/mg lysate <br><br>These are recommended dilutions. <br><br>Endusers should determine optimal dilutions for their applications. Detection of ECS-tagged protein in 200, 100, and 50ng of E. coli lysate containing tagged fusion protein with #18830 diluted 1:25,000.

Enterokinase, also known as enteropeptidase, is a serine protease that catalyzes the hydrolysis of peptide bonds in proteins but, unlike other kinases, does not catalyze transfer of phosphate groups. Enterokinase cleaves proteins following a lysine at an enterokinase cleavage site, or ECS (Asp-Asp-Asp-Asp-Lys). In vivo, this cleavage results in trypsin-dependent activation of other pancreatic zymogens, such as chymotrypsinogen, proelastase, procarboxypeptidase and prolipase in the lumen of the gut.