Leupeptin, a reversible competitive inhibitor of serine and thiol-proteinases, effectively inhibits plasmin, trypsin, proteinase K, kallikrein, papain, calpain, and cathepsins B, H, and L. It does not inhibit pepsin, cathepsin D, thrombin, or α-chymotrypsin. Leupeptin is commonly used in biochemical experiments to protect target proteins during protein isolation from tissues or other samples, and it can be removed by dialysis. The effective working concentration ranges from 10 to 100 μM. Leupeptin is effective in various salt forms. The hemisulfate form is the most widely commercialized, while the hydrochloride form is less commonly used in molecular biology. This product is the hemisulfate form of leupeptin. A 10 mM stock solution can be prepared and stored stably for 1 week at 4°C, or aliquoted and stored at -20°C for at least 6 months. Working solutions (10–100 μM) are stable for only several hours; during use, keep the working solution on ice for temporary storage (a few hours). Components Name 20112ES08 20112ES50 Leupeptin (Ultra Pure) 5 mg 5 mg×10 Specifications Chinese Synonym N-Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate English Synonym N-Acetyl-L-leucyl-L-argininal hemisulfate salt; Acetyl-Leu-Leu-Arg-al CAS Number 103476-89-7 Molecular Formula C₂₀H₃₈N₆O₄ · 1/2 H₂SO₄ Molecular Weight 475.59 Appearance White amorphous powder Solubility Soluble in water (50 mg/mL), ethanol, acetic acid, and DMF Peptide Sequence Ac-Leu-Leu-Arg-al, hemisulfate salt Structure Storage This product should be stored at -25~-15℃ for 2 years. Notes 1. For your safety and health, wear a lab coat and disposable gloves while handling this product. 2. This product is intended for research use only. Documents: Safety Data Sheet 20112_MSDS_HB251017_EN.PDF Manuals 20112_Manual_Ver.EN20251017.pdf
