Native Bovine Aprotinin/Pancreatic Trypsin Inhibitor

Product Description

Native Bovine Aprotinin/Pancreatic Trypsin Inhibitor
Catalog number: B2016556
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 5 mg, 10 mg, 25 mg, 50 mg, 100 mg
Molecular Weight or Concentration: N/A
Supplied as: Powder
Applications: a molecular tool for various biochemical applications
Storage: −20°C
Keywords: BPI, BPTI, MGC148815, aprotinin, basic protease inhibitor
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:
1: Li R, Battiste JL, Woodward C. Native-like interactions favored in the unfolded bovine pancreatic trypsin inhibitor have different roles in folding Biochemistry. 2002 Feb 19;41(7):2246-53.
2: Ang MJ, Lim HA, Poulsen A, Wee JL, Ng FM, Joy J, Hill J, Chia CS. Miniature bovine pancreatic trypsin inhibitors (m-BPTIs) of the West Nile virus NS2B-NS3 protease J Enzyme Inhib Med Chem. 2016;31(sup2):194-200.
3: Kuroda Y, Kim PS. Folding of bovine pancreatic trypsin inhibitor (BPTI) variants in which almost half the residues are alanine J Mol Biol. 2000 May 5;298(3):493-501.
4: Tulla-Puche J, Getun IV, Woodward C, Barany G. Native-like conformations are sampled by partially folded and disordered variants of bovine pancreatic trypsin inhibitor Biochemistry. 2004 Feb 17;43(6):1591-8.
5: Weissman JS, Kim PS. Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9900-4.
6: Hao MH, Pincus MR, Rackovsky S, Scheraga HA. Unfolding and refolding of the native structure of bovine pancreatic trypsin inhibitor studied by computer simulations Biochemistry. 1993 Sep 21;32(37):9614-31.
7: Marks CB, Vasser M, Ng P, Henzel W, Anderson S. Production of native, correctly folded bovine pancreatic trypsin inhibitor by Escherichia coli J Biol Chem. 1986 Jun 5;261(16):7115-8.
8: Chang JY. Distinct folding pathways of two homologous disulfide proteins: bovine pancreatic trypsin inhibitor and tick anticoagulant peptide Antioxid Redox Signal. 2011 Jan 1;14(1):127-35.
9: Oddone R, Barra D, Amiconi G, Ascenzi P, Tarricone C, Bolognesi M, Bortolotti F, Menegatti E. Binding of native and [homoserine lactone-52]-52,53-seco-bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor) to porcine pancreatic beta-kallikrein-B and bovine alpha-chymotrypsin: thermodynamic study J Mol Recognit. 1994 Mar;7(1):39-46.
10: Creighton TE, Goldenberg DP. Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor J Mol Biol. 1984 Nov 5;179(3):497-526.

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