Leupeptin Property

alpha 

-76 º (c=1, water)

storage temp. 

-20°C

solubility 

H₂O: 10 mM Solutions are stable for a week at 4 °C. Stock solutions are stable up to 6 months at −20°C.

form 

Powder

color 

White to Off-white

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.

InChIKey

CIPMKIHUGVGQTG-VFFZMTJFSA-N

Safety

Hazard Codes 

Xn

Risk 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

HS Code 

29252900

Hazard and Precautionary Statements (GHS)

Symbol(GHS)

Signal word

Warning

Precautionary statements

P261Avoid breathing dust/fume/gas/mist/vapours/spray.

P264Wash hands thoroughly after handling.

P264Wash skin thouroughly after handling.

P280Wear protective gloves/protective clothing/eye protection/face protection.

P501Dispose of contents/container to..…

Leupeptin Chemical Properties,Usage,Production

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

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.

Uses

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.

Uses

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.)

storage

+4°C

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