|Related Categories||Bioactive Small Molecules, Biochemicals and Reagents, Cell Biology, Core Bioreagents, Enzyme Inhibitors,|
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One mg will inhibit minimum 1.0 mg of trypsin with activity of approx.10,000 BAEE units per mg protein.
View more information on Trypsin Inhibitor.
Trypsin inhibitor is soluble in water and phosphate buffers at concentrations of 10 mg/ml or higher. Solutions at higher concentrations may be hazy and have a yellow to amber color.
One trypsin unit will produce a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 ml, 1 cm light path.
Soybean trypsin inhibitor inhibits trypsin and to a lesser extent chymotrypsin and plasmin. It forms a 1:1 stoichiometric complex with trypsin. Upon formation of this complex, trypsin may cleave a single arginine-isoleucine bond in the inhibitor. Dissociation of this complex may yield the modified form or the native inhibitor. At the optimal pH for trypsin binding (pH 8.0), the association constant is ≥ 10x108.
Soybean trypsin inhibitor exhibits a high degree of sequence homology with cathepsin D inhibitor from potatoes.1
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Certificate of Analysis
Certificate of Origin
|Precautionary statements||P261-P280-P342 + P311|
|Personal Protective Equipment||Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter|
|Hazard Codes (Europe)||Xn|
|Risk Statements (Europe)||42/43|
|Safety Statements (Europe)||22-36/37-45|
VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF. Nottebaum AF, Cagna G, Winderlich M, et al. J. Exp. Med. 205(12), 2929-45, (2008)
A 1-megadalton translocation complex containing Tic20 and Tic21 mediates chloroplast protein import at the inner envelope membrane. Kikuchi S, Oishi M, Hirabayashi Y, et al. Plant Cell 21(6), 1781-97, (2009)
Isolation and characterization of a trypsin inhibitor from the seeds of kohlrabi (Brassica napus var. rapifera) belonging to the napin family of storage proteins. Svendsen IB, Nicolova D, Goshev I, et al. Carlsberg Res. Commun. 54(6), 231-9, (1989)
Protein minimization: characterization of the synthetic cyclic dodecapeptide corresponding to the reactive site region of the oil rape trypsin inhibitor type-III. Trovato M, Casavola EC, Maras B, et al. Biochem. Biophys. Res. Commun. 302(2), 311-5, (2003)
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