cathepsin

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.

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

Cathepsin B, a cysteine protease, plays a role in various forms of programmed cell death, such as apoptosis, pyroptosis, ferroptosis, necroptosis, and autophagic cell death [1].

Cathepsin G(1-5), an antimicrobial peptide identified within the clostripain-digested cathepsin G mixture [1], exhibits bactericidal properties.

Cathepsin D and E FRET Substrate acetate is a fluorogenic substrate selectively cleaved by cathepsins D and E at the Phe-Phe amide bond, without activity towards cathepsins B, H, or L. This specificity makes it an essential tool for routine assays and mechanistic studies focusing on cathepsins E and D[1].

(Rac)-Z-Phe-Phe-FMK (Cathepsin L-IN-2) is a cathepsin L inhibitor that inhibits the tendency of β-amyloid to induce apoptotic changes .

Leupeptin hemisulfate is a protease inhibitor with cell membrane-permeable, reversible, competitive, and oral activities. Leupeptin hemisulfate inhibits the activity of Cathepsin B, Cathepsin H, and Cathepsin L, and blocks fusion of amphipathic lysosomes. Leupeptin hemisulfate also has anti-inflammatory activity.

Acetyl-Calpastatin (184-210)(human) acetate is a potent, selective and reversible calpain inhibitor with Ki values of 0.2 nM and 6 μM for µ-calpain and cathepsin L, respectively.

Gly-Phe β-naphthylamide acetate is the substrate of Cathepsin C and can be used for research on the function of cathepsin C, intralysosomal hydrolysis and lysosomal membrane permeability.

Leupeptin is a competitive protease inhibitor produced by actinomycetes. Leupeptin can inhibit cysteine, serine and threonine peptidases. Leupeptin inhibits serine proteinases (trypsin (Ki=3.5 nM), plasmin (Ki= 3.4 nM), porcine kallikrein), and cysteine p

Pepstatin (Pepsin Inhibitor S 735A) is a specific aspartic proteases inhibitor produced by actinomycetes, and inhibits the aspartic proteases cathepsin D, pepsin and renin.

NFAT Inhibitor (VIVIT peptide) is a cell-permeable compound that selectively inhibits calcineurin-mediated dephosphorylation of NFAT.

Z-WEHD-FMK is a cell-permeable and irreversible inhibitor of caspase-1/5. It also shows a robust inhibitory effect on cathepsin B activity (IC50: 6 μM).

Z-FG-NHO-Bz is a selective inhibitor of cathepsin [1].

RKLLW-NH2 is an inhibitor of the protease Cathepsin L [1].

Z-Phe-Phe-Diazomethylketone is a selective inhibitor of cathepsin L [1].

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

H-Arg-4MβNA (H-Arg-4MbNA) is a peptide that serves as a substrate for cathepsin H. The enzyme activity is often detected in gel electrophoresis.

Hepcidin-1 (mouse) TFA, an endogenous peptide hormone, regulates iron homeostasis by upregulating mRNA levels of TRAP, cathepsin K, and MMP-9, enhancing TRAP-5b protein secretion, and downregulating FPN1 protein levels, thereby increasing intracellular iron. It also promotes osteoclast differentiation [1].

Ac-VLPE-FMK, a tetrapeptidyl mono-fluoromethyl ketone (m-FMK), functions as an inhibitor of both Cathepsin B (Cat-B) and Cathepsin L (Cat-L), and is utilized in research pertaining to the aggressiveness of cancer [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.

Ac-Leu-Val-Lys-Aldehyde is a potent inhibitor of cathepsin B, exhibiting inhibitory concentration (IC50) values of 4 nM. It notably diminishes cell death in the striatum induced by quinolinic acid and leads to the accumulation of LC3-II [1].

Hepcidin-1 (mouse) is a peptide hormone that regulates iron balance, elevates mRNA for TRAP, cathepsin K, and MMP-9, and promotes TRAP-5b protein secretion. This compound also reduces FPN1 protein levels and boosts intracellular iron, ultimately aiding in osteoclast differentiation [1].

Acetyl-Calpastatin(184-210)(human) TFA, a potent, selective, and reversible inhibitor of calpain, demonstrates Ki values of 0.2 nM for µ-calpain and 6 μM for cathepsin L, indicating high specificity and efficacy in inhibiting these enzymes [1] [2].

Selective calpain inhibitor. Strongly inhibits calpain I (Ki = 0.2 nM) and II but does not inhibit papain, trypsin and cathepsin L (Ki = 6 μM). Increases secretion of amyoid β-protein (Aβ) 42, Aβ40 and Aβ42 ratio.

LL-37 scrambled peptide acetate is a scrambled peptide of cathepsin antimicrobial peptide LL-37, which is often used as a negative control for LL-37 peptide in experiments.

Ac-PLVE-FMK (Ac-Pro-Leu-Val-Glu(OMe)-CH2F), a tetrapeptidyl fluoromethylketone (FMKs), serves as a cathepsin inhibitor. It is utilized in cancer research [1].

N-CBZ-Phe-Arg-AMC (Z-FR-AMC) TFA serves as a substrate for cathepsin, facilitating the evaluation of lysosomal cathepsin enzyme activity [1] [2].