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

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

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.