103476-89-7

Basic information

• Product Name: Leupeptin
• Synonyms: AC-LEU-LEU-ARGININAL HEMISULPHATE;AC-LEU-LEU-ARGININAL X 1/2 H2SO4;AC-LEU-LEU-L-ARGININAL;AC-LLR-CHO;AC-LLR-CHO, 1/2H2 SO4;N-ACETYL-L-LEUCYL-L-LEUCYL-L-ARGININAL HEMISULFATE;Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate;leupeptin hemisulfate from microbial*source
• CAS NO: 103476-89-7
• Molecular Formula: C20H38N6O4
• Molecular Weight: 426.55
• EINECS: 2017-001-1
• Product Categories: Protease;Pepetides;ProteaseInhibitors;peptides;inhibitor;Inhibitors
• Mol File: 103476-89-7.mol
• Article Data: 0

Chemical Properties

• Appearance: White to Off-white/Powder
• Density: 1.21g/cm³
• Refractive Index: 1.557
• Storage Temp.: −20°C
• Solubility: H2O: 10 mM Solutions are stable for a week at 4 °C.
• Water Solubility: soluble
• Stability: Stable for 1 year from date of purchase as supplied Solutions in distilled water, ethanol or methanol may be stored at -20°C for up to 3 months.
• CAS DataBase Reference: Leupeptin(CAS DataBase Reference)
• NIST Chemistry Reference: Leupeptin(103476-89-7)
• EPA Substance Registry System: Leupeptin(103476-89-7)

Safety Data

• Hazard Codes: Xn
• Statements: 20/21/22-63-36/37/38
• Safety Statements: 22-24/25-36/37-36-36/37/39-26-7/8
• RIDADR: 3077
• WGK Germany: 3
• F: 10-23
• Hazardous Substances Data: 103476-89-7(Hazardous Substances Data)

Usage

Description

Leupeptin hemisulfate (103476-89-7) is a reversible inhibitor of trypsin-like proteases and cysteine proteases. Inhibits trypsin, plasmin, papain and cathepsin B, H and L.1-3?Blocks various apoptotic pathways in T cells.4?Commonly used in cell lysis buffers to protect proteins from degradation. Typical working concentration is 1μM (0.5 μg/ml).

Chemical Properties

White to off-white lyophilized powder

Uses

Different sources of media describe the Uses of 103476-89-7 differently. You can refer to the following data:
1. Reversible protease inhibitor, which inhibits cathepsin B, calpain and trypsinPharmaceutical composition containing leupeptin hemisulfate is used as an anti-malarial agent. It is employed in the treatment of noise-induced hearing loss. It also protects the heart from myocardial stunning. Further, it is used to inhibit serine, cysteine proteases, plasmin, trypsin, papain, kallikrein and cathepsin B.
2. Leupeptin as well as other protease inhibitors like antipain, chymostatin, pepstatin, and phosphoramidon are useful for the protection of proteins during their isolation from tissues or membranes. Leupeptin can be removed from the reaction by dialysis.Note: To check other protease inhibitors, try our Protease Inhibitor Set including Antipain Dihydrochloride, Aprotinin, Bestatin, Chymostatin, E-64, EDTA-Na2, Leupeptin, Pefabloc SC, Pepstatin, and Phosphoramidon.
3. Leupeptin has been used as a protease inhibitor: in ice-cold lysis buffer to harvest cells for western immunoblotting and immunoprecipitation,in chromatin immunoprecipitation (ChIP) lysis buffer for the isolation of fragmented chromatin samples in lysis buffer I to lyse the cells for tandem affinity purification (TAP)

Definition

ChEBI: A peptide sulfate salt obtained by combining leupeptin with 0.5 molar equivalents of sulfuric acid.

General Description

Leupeptin, or N-acetyl-L-leucyl-L-leucyl-L-argininal, is a naturally occurring tripeptide that acts particularly as a serine protease inhibitor and as a cysteine protease inhibitor. Its mechanism of action involves structurally similar covalent binding reactions:In the active site of serine proteases, leupeptin forms a covalent hemiacetal adduct between the aldehyde group of leupeptin and the hydroxyl group of a serine residue in the enzyme active site.In the active site of cysteine proteases, the electrophilic (aldehyde) carbon of leupeptin forms a comparable bond with the sulfur atom of a cysteine residue in the enzyme active site.

Biochem/physiol Actions

Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain, calpain, and cathepsin B. Does not inhibit pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM. There have been numerous studies using leupeptin to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin. (Loss of cochlear hair cells is believed to be mediated by calpain.)

References

1) Aoyagi?et al.?(1969),?Leupeptins, new protease inhibitors from Actinomycetes; J. Antibiot.,?22?283 2) Barrett?et al.?(1981),?Cathepsin B, Cathepsin H and Cathepsin L; Methods Enzymol., Pt C,?80?535 3) Knight?et al. (1980),?Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin; Biochem. J.,?189?447 4) Sarin?et al. (1995),?A protease-dependent TCR-induced death pathway in mature lymphocytes; J. Immunol.,?154?5806

InChI:InChI=1/C20H38N6O4/c1-12(2)9-16(24-14(5)28)18(29)26-19(30)17(10-13(3)4)25-15(11-27)7-6-8-23-20(21)22/h11-13,15-17,25H,6-10H2,1-5H3,(H,24,28)(H4,21,22,23)(H,26,29,30)/t15?,16-,17-/m0/s1