Bovine Anhydrotrypsin Purified Immobilized

<strong>Bovine Anhydrotrypsin Purified Immobilized</strong>_x000D_ <strong>Catalog number:</strong> B2017110_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 1 mL_x000D_ <strong>Molecular Weight or Concentration:</strong> N/A_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> a molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -80C_x000D_ <strong>Keywords:</strong> Bovine Anhydrotrypsin Purified Immobilized_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: Ishii S, Yokosawa H, Kumazaki T, Nakamura I. Immobilized anhydrotrypsin as a specific affinity adsorbent for tryptic peptides Methods Enzymol. 1983;91:378-83._x000D_ 2: Ishii S, Yokosawa H, Shiba S, Kasai K. Specific isolation of biologically-active peptides by means of immobilized anhydrotrypsin and anhydrochymotrypsin Adv Exp Med Biol. 1979;120A:15-27._x000D_ 3: Yokosawa H, Ishii S. Immobilized anhydrotrypsin as a biospecific affinity adsorbent for the peptides produced by trypsin-like proteases Anal Biochem. 1979 Sep 15;98(1):198-203._x000D_ 4: Wilimowska-Pelc A, Stachowiak D, Gładysz M, Olichwier Z, Polanowski A. Antiproteolytic activity of goose pancreas: purification, inhibitory properties and amino-acid sequence of a Kazal type trypsin inhibitor Acta Biochim Pol. 1996;43(3):489-96._x000D_ 5: Odani S, Tominaga K, Kondou S, Hori H, Koide T, Hara S, Isemura M, Tsunasawa S. The inhibitory properties and primary structure of a novel serine proteinase inhibitor from the fruiting body of the basidiomycete, Lentinus edodes Eur J Biochem. 1999 Jun;262(3):915-23._x000D_ 6: Stachowiak D, Polanowski A, Bieniarz G, Wilusz T. Isolation and amino-acid sequence of two inhibitors of serine proteinases, members of the squash inhibitor family, from Echinocystis lobata seeds Acta Biochim Pol. 1996;43(3):507-13._x000D_ 7: Huber R, Bode W, Kukla D, Kohl U, Ryan CA. The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor III. Structure of the anhydro-trypsin-inhibitor complex Biophys Struct Mech. 1975 May 30;1(3):189-201._x000D_ 8: Weder JK, Haussner K. Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigonella foenum-graecum L.) seeds. Demonstration and purification Z Lebensm Unters Forsch. 1991 May;192(5):455-9._x000D_ 9: Markland W, Roberts BL, Saxena MJ, Guterman SK, Ladner RC. Design, construction and function of a multicopy display vector using fusions to the major coat protein of bacteriophage M13 Gene. 1991 Dec 20;109(1):13-9._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/8922034">10: Stachowiak D, Polanowski A, Bieniarz G, Wilusz T. Isolation and amino-acid sequence of two inhibitors of serine proteinases, members of the squash inhibitor family, from Echinocystis lobata seeds Acta Biochim Pol. 1996;43(3):507-13.</a>_x000D_ _x000D_ <strong>Products Related to Bovine Anhydrotrypsin Purified Immobilized can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>