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LEU-RO Roche

Leupeptin

Ac-Leu-Leu-argininal x 1/2 H2SO4, synthetic

Synonym: Acetyl-Leu-Leu-Arg-al, Leupeptin hemisulfate salt, N-Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate salt

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Properties

Related Categories Biochemicals and Reagents, Enzyme Inhibitors, Enzymes, Inhibitors, and Substrates, Individual Protease Inhibitors, Protease Inhibitors More...
Quality Level   100
biological source   synthetic
assay   ≥96.5%
form   powder
mol wt   Mr 475.6
packaging   pkg of 100 mg (11529048001)
  pkg of 25 mg (11017128001)
  pkg of 5 mg (11017101001)
  pkg of 50 mg (11034626001)
mfr. no.   Roche
solubility   H2O: 50 mg/mL
shipped in   wet ice
storage temp.   2-8°C
SMILES string   OS(O)(=O)=O.CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C=O.CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C=O
InChI   1S/2C20H38N6O4.H2O4S/c2*1-12(2)9-16(24-14(5)28)19(30)26-17(10-13(3)4)18(29)25-15(11-27)7-6-8-23-20(21)22;1-5(2,3)4/h2*11-13,15-17H,6-10H2,1-5H3,(H,24,28)(H,25,29)(H,26,30)(H4,21,22,23);(H2,1,2,3,4)/t2*15-,16-,17-;/m00./s1
InChI key   CIPMKIHUGVGQTG-VFFZMTJFSA-N

Description

Specificity

Leupeptin inhibits serine and thiol proteases such as trypsin, plasmin, proteinase K, kallikrein, papain, thrombin, and cathepsin A and B.
Not affected are α-, β-, γ- and δ- chymotrypsin, pepsin, cathepsin D, elastase, renin, and thermolysin.

Application

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.

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.)

Features and Benefits

Contents
Synthetic, white powder

Quality

Function test: Performance controlled with trypsin.

Preparation Note

Working concentration: 0.5 to 5 μg/ml (1 to 20 μM)

Comparison of working concentrations of pefabloc with leupeptin and PMSF is in files.

Working solution: Solvent is recommended in distilled water.
Highly soluble in water (1 mg/ml), methanol, ethanol, acetic acid, dimethyl formamide and dimethyl sulfoxide.
Poorly soluble in acetone, chloroform, ethyl ether and n-hexane.

Storage conditions (working solution): -15 to -25 °C
In aqueous solution leupeptin is stable for 1 month at 2 to 8 °C or for at least 6 months at - 15 to -25 °C, stored under nitrogen. For best results, freeze the dissolved inhibitor in aliquots and avoid repeated thawing.

Reconstitution

Highly soluble in water (1 mg/ml). Stable for at least one week at 2 to 8 °C and 6 months frozen in aliquots at -15 to -25 °C.

Analysis Note

Leupeptin gives multiple peaks on HPLC due to equilibria among three forms in solution. Purity determined using three main peaks. Majority of contaminating peptide is racemized leupeptin.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport

Documents

Certificate of Analysis (COA)

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