Trypsin Agarose Catalog number: B2013953 Lot number: Batch Dependent Expiration Date: Batch dependent Amount: 25 units Molecular Weight or Concentration: ≥15 units/mL Supplied as: Suspension Applications: molecular tool for various biochemical applications Storage: 2-8°C Keywords: Trypsin Agarose Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um. References Walter B. Characterization of agarose-bound trypsin Biochim Biophys Acta. 1976 May 13;429(3):950-3. Sinha NK, Light A. Refolding of reduced, denatured trypsinogen and trypsin immobilized on Agarose beads J Biol Chem. 1975 Nov 25;250(22):8624-9. Lei MG, Reeck GR. Combined use of trypsin-agarose affinity chromatography and reversed-phase high-performance liquid chromatography for the purification of single-chain protease inhibitor from corn seeds J Chromatogr. 1986 Aug 29;363(2):315-21. Quan TH, Benjakul S. Trypsin_inhibitor from duck albumen: Purification and characterization J Food Biochem. 2019 May;43(5):e12841. Poonsin T, Simpson BK, Visessanguan W, Yoshida A, Klomklao S. Optimal immobilization of trypsin from the spleen of albacore tuna (Thunnus alalunga) and its characterization Int J Biol Macromol. 2020 Jan 15;143:462-471. Vogt W, Schmidt G, Dieminger L, Lynen R. Formation and composition of the C3 activating enzyme complex of the properdin system. Sequential assembly of its components on solid-phase trypsin-agarose Z Immunitatsforsch Exp Klin Immunol. 1975 Jul;149(5):440-55. Poonsin T, Simpson BK, Benjakul S, Visessanguan W, Yoshida A, Osatomi K, Klomklao S. Anionic trypsin from the spleen of albacore tuna (Thunnus alalunga): Purification, biochemical properties and its application for proteolytic degradation of fish muscle Int J Biol Macromol. 2019 Jul 15;133:971-979. Chan YS, Zhang Y, Sze SC, Ng TB. A thermostable trypsin_inhibitor with antiproliferative activity from small pinto beans J Enzyme Inhib Med Chem. 2014 Aug;29(4):485-90. Ito M, Ikegami Y, Omori A, Yamagata T. Conversion of endoglycoceramidase-activator II by trypsin to the 27.9 kDa polypeptide possessing full activity: purification of activator for endoglycoceramidase by trypsin treatment followed by trypsin-inhibitor_agarose column application J Biochem. 1991 Sep;110(3):328-32.
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