Trypsinogen from Bovine Pancreas

<strong>Trypsinogen from Bovine Pancreas</strong>_x000D_ <strong>Catalog number:</strong> B2013987_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 50 mg_x000D_ <strong>Molecular Weight or Concentration:</strong> 23.981 kDa_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> −20°C_x000D_ <strong>Keywords:</strong> Trypsinogen from bovine pancreas_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Sendler M, Weiss FU, Golchert J, Homuth G, van den Brandt C, Mahajan UM, Partecke LI, Dring P, Gukovsky I, Gukovskaya AS, Wagh PR, Lerch MM, Mayerle J. Cathepsin B-Mediated Activation of Trypsinogen in Endocytosing Macrophages Increases Severity of Pancreatitis in Mice Gastroenterology. 2018 Feb;154(3):704-718.e10._x000D_ 2: Wilimowska-Pelc A, Mejbaum-Katzenellenbogen W. A simple method for isolating trypsin from trichloroacetic acid extracts of bovine pancreas Anal Biochem. 1978 Oct 15;90(2):816-20._x000D_ 3: Gorrill AD, Thomas JW. Trypsin, chymotrypsin, and total proteolytic activity of pancreas, pancreatic juice, and intestinal contents from the bovine Anal Biochem. 1967 May;19(2):211-25._x000D_ 4: Rovery M. Limited proteolyses in pancreatic chymotrypsinogens and trypsinogens Biochimie. 1988 Sep;70(9):1131-5._x000D_ 5: Puigserver A, Desnuelle P. Identification of an anionic trypsinogen in bovine pancreas Biochim Biophys Acta. 1971 May 25;236(2):499-502._x000D_ 6: Le Huerou I, Wicker C, Guilloteau P, Toullec R, Puigserver A. Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity within the trypsin family Eur J Biochem. 1990 Nov 13;193(3):767-73._x000D_ 7: Ogawa H, Kusumi I, Ogata A, Wada A, Sakagami H, Mitsuhashi K, Date K. Autoactivation of pancreatic trypsinogen is controlled by carbohydrate-specific interaction FEBS Lett. 2015 Feb 27;589(5):569-75._x000D_ 8: Brodrick JW, Largman C, Johnson JH, Geokas MC. Human cationic trypsinogen. Purification, characterization, and characteristics of autoactivation J Biol Chem. 1978 Apr 25;253(8):2732-6._x000D_ 9: Bodley MD, Naud RJ, Oelofsen W, Ptthy A. Ostrich trypsinogen: purification, kinetic properties and characterization of the pancreatic enzyme Int J Biochem Cell Biol. 1995 Jul;27(7):719-28._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/588260">10: Mahony PC, Offord RE. The production of the second activation peptide from trypsinogen isolated from individual pancreases Biochem J. 1977 Oct 1;167(1):287. </a>_x000D_ _x000D_ <strong>Products Related to Trypsinogen from Bovine Pancreas can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>