| Identification | Back Directory | [Name]
Leupeptin | [CAS]
103476-89-7 | [Synonyms]
LEUPEPTIN
AC-LLR-CHO
LEUPEPTIN SULFATE
AC-LEU-LEU-ARG-CHO
LEUPEPTIN 1/2 H2SO4
AC-LEU-LEU-ARGININAL
Synonym Acetyl-Leu-L
Leupeptin, Microbial
AC-LLR-CHO, 1/2H2 SO4
acetyl-leu-leu-arg-al
LEUPEPTIN HEMISULFATE
LEUPEPTIN (SYNTHETIC)
LEUPEPTIN HEMISULPHATE
AC-LEU-LEU-L-ARGININAL
Leupeptine hemisulfate
EZNA KIT BACTERIAL RNA
Acetyl-Leu-Leu-Arg-CHO
AC-LEU-LEU-ARG-ALDEHYDE
LEUPEPTIN, 90%, SYNTHETIC
LEUPEPTIN HEMISULFATE SALT
Leupeptin hemisulphate >90%
Leupeptin(Acetyl-Leu-Arginal)
LEUPEPTIN HEMISULFATE SYNTHETIC
ACETYL-L-LEU-LEU-ARG (SULFATED)
AC-LEU-LEU-ARGININAL X 1/2 H2SO4
LEUPEPTIN HEMISULFATE, MICROBIAL
AC-LEU-LEU-ARGININAL HEMISULPHATE
ACETYL-LEU-LEU-ARG-AL HEMISULFATE
LEUPEPTIN HEMISULFATE, ~4000 U/MG
AC-LEU-LEU-ARG-ALDEHYDE HEMISULFATE
M.W. 475.59 C20H38N6O4 · 1/2H2SO4
ACETYL-LEU-LEU-ARG-AL HEMISULFATE SALT
TRIS-GLYCINE BUFFER 10X SOL. PROTEOMICS
leupeptin hemisulfate from microbial*source
ACETYL-L-LEUCYL-L-LEUCYL-L-ARGININAL SULFATE
Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate
N-ACETYL-L-LEUCYL-L-LEUCYL-L-ARGININAL HEMISULFATE
LeupeptinAcetyl-L-leucyl-L-leucyl-L-argininal hemisulfate
Acetyl-Leu-Leu-Arg-al, N-Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate salt
L-Leucinamide, N-acetyl-L-leucyl-N-(1S)-4-(aminoiminomethyl)amino-1-formylbutyl-, sulfate (2:1)
N-acetyl-L-leucyl-N-[(1S)-4-[(aminoiminomethyl)amino]-1-formylbutyl]-L-leucinamide, sulfate (2:1)
Leupeptin hemisulfate salt,Acetyl-Leu-Leu-Arg-al, N-Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate salt | [EINECS(EC#)]
2017-001-1 | [Molecular Formula]
C20H38N6O4 | [MDL Number]
MFCD00081028 | [MOL File]
103476-89-7.mol | [Molecular Weight]
426.55 |
| Chemical Properties | Back Directory | [Appearance]
White to off-white lyophilized powder | [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?#x00b0;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 |
| Hazard Information | Back Directory | [Chemical Properties]
White to off-white lyophilized powder | [Definition]
ChEBI: A peptide sulfate salt obtained by combining leupeptin with 0.5 molar equivalents of sulfuric acid. | [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). | [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. | [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]
Store at -20°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 |
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