peptidases

Talabostat mesylate (PT100) is an orally active, selective inhibitor of dipeptidyl peptidases IV (DPP4, IC50: 0.18 nM), including tumor-associated fibroblast activation protein. This agent may also stimulate the production of colony stimulating factors, such as granulocyte colony-stimulating factor (G-CSF), resulting in the stimulation of hematopoiesis.

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

AA26-9 is an effective and broad-spectrum inhibitor of serine hydrolase.

ICeD-2, an inducer of cell death, effectively induces the killing of HIV-1 infected cells, a process reliant on HIV-1 protease activity. It significantly inhibits the hydrolysis of Gly-Pro-AMC by dipeptidyl peptidases DPP8 and DPP9, and robustly stabilizes DPP9 in peripheral blood mononuclear cells (PBMCs) [1].

Protein conjugates in tissue regeneration 3 (PCTR3) is a specialized pro-resolving mediator (SPM) synthesized from docosahexaenoic acid . DHA is oxidized to 16S,17S-epoxy-protectin, which is converted to PCTR1 by glutathione S-transferase and to PCTR2 and PCTR3 via peptidases. PCTR3 is found in infected mouse spleens and resolving exudate as well as isolated human spleen and septic plasma. It is also found in both M1 and M2 macrophages differentiated from isolated human monocytes.

Iodoacetamide, an alkylating agent, is commonly utilized for cysteine alkylation in proteomics sample preparation.

Leupeptin is a naturally occurring protease inhibitor that can inhibit cysteine, serine and threonine peptidases. Leupeptin is an organic compound produced by actinomycetes. Leupeptin inhibits serine proteinases (trypsin (Ki=3.5 nM), plasmin (Ki= 3.4 nM), porcine kallikrein), and cysteine proteinases (papain, cathepsin B (Ki = 4.1 nM), endoproteinase Lys-C). It does not inhibit α-chymotrypsin or thrombin. Leupeptin is a competitive transition state inhibitor and its inhibition may be relieved by an excess of substrate.

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.