Synonym: Trasylol, Trypsin inhibitor (basic)
|Related Categories||AN-AZ, Bioactive Small Molecules, Biochemicals and Reagents, Cell Biology, Enzyme Inhibitors,|
|mol wt||mol wt ~6,500|
|solubility||H2O: >10 mg/mL|
|Gene Information||cow ... PTI(404172)|
Another commonly used unit of activity is the KIU (Kallikrein Inhibitor Unit).
1 TIU ∼ 1,300 KIU.
Affinity purified to remove trace impurities from A 1153.
One trypsin inhibitor unit (TIU) will decrease the activity of 2 trypsin units by 50% where one trypsin unit will hydrolyze 1.0 μmole of N-α-benzoyl-
Aprotinin is a competitive serine protease inhibitor which is used to block the active sites of various enzymes, such as trypsin, chymotrypsin, kallikrein and plasmin.
Binding is reversible with most aprotinin-protease complexes dissociating at pH > 10 or < 3. Effective concentration equimolar with protease. Aprotinin is a monomeric globular polypeptide that is derived from bovine lung. It has a molecular weight of 6512 and consists of 16 different amino acid types arranged in a chain 58 residues long 1.
Aprotinin is a protein consisting of 58 amino acids, arranged in a single polypeptide chain that is crosslinked by three disulfide bridges.
Customers Also Viewed
recombinant, expressed in Nicotiana, ≥5 TIU/mg protein, ≥98% (SDS-PAGE)
saline solution, 3-7 TIU/mg protein
lyophilized powder, 3-8 TIU/mg solid
lyophilized powder, 3-8 TIU/mg solid, BioReagent, suitable for cell culture
Certificate of Analysis
Certificate of Origin
2. SCOPE The scope of this procedure is all products that have a specification for Aprotinin activity.
Keywords: Enzymology, Extinction coefficient
Neutron and X-ray crystallographic analysis of Achromobacter protease I at pD 8.0: protonation states and hydration structure in the free-form. Ohnishi Y, Yamada T, Kurihara K, et al. Biochim. Biophys. Acta 1834(8), 1642-7, (2013)
Aprotinin may increase mortality in low and intermediate risk but not in high risk cardiac surgical patients compared to tranexamic acid and ε-aminocaproic acid -- a meta-analysis of randomised and observational trials of over 30.000 patients. Meybohm P, Herrmann E, Nierhoff J, et al. PLoS ONE 8(3), e58009, (2013)
Influence of different storage conditions and anticoagulants on the measurement of total and acylated ghrelin in dogs: a preliminary study. Tvarijonaviciute A, Martínez-Subiela S, and Ceron JJ Vet. Rec. 172(11), 289, (2013)
Oxidative folding of peptides with cystine-knot architectures: kinetic studies and optimization of folding conditions. Reinwarth M, Glotzbach B, Tomaszowski M, et al. ChemBioChem. 14(1), 137-46, (2013)
Replacement of aprotinin by ε-aminocaproic acid in infants undergoing cardiac surgery: consequences for blood loss and outcome. Martin K, Gertler R, MacGuill M, et al. Br. J. Anaesth. 110(4), 615-21, (2013)
Retrospective cohort analysis of a single dose of aprotinin use in children undergoing cardiac surgery: a single-center experience. Fan Y, Lin R, Yang L, et al. Paediatr. Anaesth. 23(3), 242-9, (2013)
Entropy-enthalpy transduction caused by conformational shifts can obscure the forces driving protein-ligand binding. Fenley AT, Muddana HS, and Gilson MK Proc. Natl. Acad. Sci. U. S. A. 109(49), 20006-11, (2012)
Trautschold, I., et al. Biochem. Pharmacol. 16, 59, (1967)
Review: Biochemistry of aprotinin and aprotinin-like inhibitors. Gebhard, W. Res. Monogr. Cell Tissue Physiol. 12, 375, (1986)
Beynon, R.J. and Bond, J.S., ed. Proteolytic Enzymes: A Practical Approach, (1989), 247
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Need larger quantities for your development, manufacturing or research applications?