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.
Calpastatin (184-210), an acetylated synthetic peptide derived from human calpastatin, effectively inhibits the calcium-dependent cysteine proteases, calpain I (µ-calpain) and calpain II (m-calpain), which require micromolar and millimolar calcium concentrations, respectively. Unlike its action on calpains, this 27 amino acid peptide does not inhibit papain (a cysteine protease) or trypsin (a serine protease). Encoded by exon 1B of Ac-calpastatin (184-210), it aligns with a section of inhibitory domain 1, showcasing its specificity and inhibitory function towards calpain enzymes.
Ganolucidic acid A exhibits cytotoxicity, has inhibitory activities against human HeLa cervical cancer cell lines. It shows significant anti-human immunodeficiency virus (anti-HIV)-1 protease activity with IC50 values of 20-90 microM.
Pepstatin Ammonium is a specific inhibitor of aspartic proteaseproduced by actinomycetes(hemoglobin-pepsin, hemoglobin-proctase, casein-pepsin, casein-proctase, casein-acidprotease and hemoglobin-acidprotease with IC50s of 4.5 nM, 6.2 nM, 150 nM, 290 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