Trypsin inhibitor CAS 9035-81-8 Biological Catalysts Enzymes
|trypsin inhibitor from phaseolus limensis (lima bean);trypsin inhibitor,defined (1x)solution;trypsin inhibitor, kohlrabi seed;contrykal;iniprol;TRYPSIN INHIBITOR FROM SOYBEAN >10000 BEAA;Trypsin inhibitor from soyabean;TRYPSIN Inhibitor extrapure
|Trypsin inhibitor Chemical Properties
|H2O: >10 mg/mL
|Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml).
|Trypsin inhibitor Usage And Synthesis
|Trypsin Inhibitor, Corn is a specific reversible inhibitor of trypsin and potent inhibitor of human factor XIIa.
|Trypsin inhibitor from chicken egg white has been used:
- to produce denatured, oxidized and deglycosylated ovomucoid and used to stimulate patient derived cell cultures for mapping T cell epitopes
- to treat nuclei for flow cytometric analysis
- in Holtfreter′s solution, used for the dissociation of planarians into cells
|This product has been tested for cell culture applications. Trypsin has been used in a study to assess the potential application in animal cell culture of an alkaline protease from a ton-toxigenic mangrove isolate of Vibri sp. V26. Trypsin has also been used in a study to improve the detection of fungi in eosinophilic mucin.
|Ovomucoid or trypsin inhibitor is an abundant protein in most avian egg whites. The hen′s egg protein is composed of about 186 amino acid residues, and is highly glycosylated. Three tandem domains are each homologous with pancreatic trypsin inhibitor. It is highly immunogenic, and probably accounts for most cases of egg allergy.
|This inhibitor acts against trypsin, and chymotrypsin and plasmin to a lesser extent. It will also inhibit proteases with mechanisms similar to trypsin, plasma kallikrein and coagulation Factor X. The trypsin inhibitor will not act against metalloproteases, tissue-baseed kallikrein, acid proteases, or thio proteases. This inhibitor acts by forming a 1:1 stoichiometric complex with the protease active site, and then cleaving a single arginine-isoleucine bond on the inhibitor. The inhibition is both reversible and pH dependent.