cathepsin-d

Cathepsin D and E FRET Substrate acetate is a fluorogenic substrate for cathepsins D and E but not for B, H, or L. Cathepsin D and E FRET Substrate acetate can be used in mechanistic studies on cathepsins D and E studies.

Cathepsin D and E FRET Substrate acetate is a fluorogenic substrate selectively cleaved by cathepsins D and E at the Phe-Phe amide bond, demonstrating no activity towards cathepsins B, H, or L. This specificity renders it essential for routine assays and mechanistic studies focusing on cathepsins E and D[1].

Mca-GKPILFFRL-Dpa-r-amide, FRET substrate for cathepsin D and E. Also cleaved by napsin A.

H-Pro-Thr-Glu-Phe-p-nitro-Phe-Arg-Leu-OH is a water-soluble polypeptide that serves as a substrate for the enzymes cathepsin D, pepsin, and pepsinogen, with potential applications in biochemical analysis [1] [2].

Parasin I, a peptide fragment derived from the N-terminal region of histone H2A in catfish (P. asotus), plays a critical role in host defense. This antimicrobial peptide is produced through the action of cathepsin D on histone H2A within the skin mucosa of injured P. asotus. Demonstrating efficacy against a spectrum of Gram-positive and Gram-negative bacteria, as well as fungi, Parasin I exhibits minimum inhibitory concentrations (MICs) of 1-2 µg/ml, 1-4 µg/ml, and 1-2 µg/ml, respectively.