cathepsin b

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].

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.

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.

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

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).

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].

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].

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].