trypsinogen

Aprotinin (Traskolan) is a broad-spectrum serine protease (BPTI) inhibitor that inhibits the activity of a number of different esterases and proteases. Aprotinin is an antifibrinolytic agent used to minimize hemorrhage during complex surgical procedures.

Chymotrypsinogen is an inactive precursor of Chymotrypsin . Chymotrypsin is a serine protease produced by the pancreas [1] [2] .

L-Cystine (Cystine Acid) is not considered one of the 20 amino acids, L-Cystine (Cystine Acid) is a sulfur-containing derivative obtained from oxidation of cysteine amino acid thiol side chains. It functions as an antioxidant and protects tissues against radiation and pollution, slowing the aging process. It also aids protein synthesis. L-Cystine (Cystine Acid) is abundant in many proteins of skeletal tissues and skin, and found in insulin and digestive enzymes chromotrypsinogen A, papain, and trypsinogen.

MBD is a fluorescent probe for hydrophobic regions in proteins and nucleoproteins, widely used in research and experiments in the field of life sciences.

Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage. Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation/emission spectra of 380/500 nm.

Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage.1,2Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation/emission spectra of 380/500 nm.3