MedKoo Cat#: 535265 | Name: Leupeptin Ac-LL

Description:

WARNING: This product is for research use only, not for human or veterinary use.

Leupeptin is a Cysteine Proteinase Inhibitor. Leupeptin, also known as NK381, is a protease inhibitor, will strongly inhibit Trypsin, Papain, Plasmin, Thrombokinase, Kallikrein and Cathepsin B. The half-maximal inhibitory concentration ranges from 0.5 to 75 μg/ml, depending on the enzyme and the substrate. Leupeptin does not inhibit Chymotrypsin, Elastase, Renin, or Pepsin.

Chemical Structure

Leupeptin Ac-LL
CAS#24365-47-7

Theoretical Analysis

MedKoo Cat#: 535265

Name: Leupeptin Ac-LL

CAS#: 24365-47-7

Chemical Formula: C20H38N6O4

Exact Mass: 426.2955

Molecular Weight: 426.56

Elemental Analysis: C, 56.32; H, 8.98; N, 19.70; O, 15.00

Price and Availability

This product is currently not in stock but may be available through custom synthesis. To ensure cost efficiency, the minimum order quantity is 1 gram. The estimated lead time is 2 to 4 months, with pricing dependent on the complexity of the synthesis (typically high for intricate chemistries). Quotes for quantities below 1 gram will not be provided. To request a quote, please click the button below. Note: If this product becomes available in stock in the future, pricing will be listed accordingly.
Bulk Inquiry
Related CAS #
39740-82-4 (HCl) 55123-66-5 (free base) 1082207-96-2 (hemisulfate hydrate) 103476-89-7 (hemisulfate) 24365-47-7 (free base)
Synonym
Leupeptin Ac-LL;
IUPAC/Chemical Name
(2S)-2-acetamido-N-((2S)-1-((5-guanidino-1-oxopentan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)-4-methylpentanamide
InChi Key
GDBQQVLCIARPGH-BSOSBYQFSA-N
InChi Code
InChI=1S/C20H38N6O4/c1-12(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/h11-13,15-17H,6-10H2,1-5H3,(H,24,28)(H,25,29)(H,26,30)(H4,21,22,23)/t15?,16-,17-/m0/s1
SMILES Code
[C@@H](NC([C@H](CC(C)C)NC(C)=O)=O)(C(NC(CCCNC(=N)N)C=O)=O)CC(C)C
Appearance
Solid powder
Purity
>98% (or refer to the Certificate of Analysis)
Shipping Condition
Shipped under ambient temperature as non-hazardous chemical. This product is stable enough for a few weeks during ordinary shipping and time spent in Customs.
Storage Condition
Dry, dark and at 0 - 4 C for short term (days to weeks) or -20 C for long term (months to years).
Solubility
Soluble in DMSO
Shelf Life
>3 years if stored properly
Drug Formulation
This drug may be formulated in DMSO
Stock Solution Storage
0 - 4 C for short term (days to weeks), or -20 C for long term (months).
HS Tariff Code
2934.99.9001
More Info

Preparing Stock Solutions

The following data is based on the product molecular weight 426.56 Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.

Recalculate based on batch purity %
Concentration / Solvent Volume / Mass 1 mg 5 mg 10 mg
1 mM 1.15 mL 5.76 mL 11.51 mL
5 mM 0.23 mL 1.15 mL 2.3 mL
10 mM 0.12 mL 0.58 mL 1.15 mL
50 mM 0.02 mL 0.12 mL 0.23 mL
1: Hashimoto Y. Gelatin Zymography Using Leupeptin for the Detection of Various Cathepsin L Forms. Methods Mol Biol. 2017;1594:243-254. doi: 10.1007/978-1-4939-6934-0_16. PMID: 28456988. 2: Suzukake K, Takada M, Hori M, Umezawa H. Biosynthesis of leupeptin. IV. Is protein turnover in leupeptin producer cells affected by leupeptin? J Antibiot (Tokyo). 1980 Oct;33(10):1172-6. doi: 10.7164/antibiotics.33.1172. PMID: 7451369. 3: Hori M, Hemmi H, Suzukake K, Hayashi H, Uehara Y, Takeuchi T, Umezawa H. Biosynthesis of leupeptin. J Antibiot (Tokyo). 1978 Jan;31(1):95-8. doi: 10.7164/antibiotics.31.95. PMID: 627527. 4: Kim IS, Lee KJ. Physiological roles of leupeptin and extracellular proteases in mycelium development of Streptomyces exfoliatus SMF13. Microbiology. 1995 Apr;141 ( Pt 4):1017-25. doi: 10.1099/13500872-141-4-1017. PMID: 7773379. 5: Suzukake K, Hori M, Tamemasa O, Umezawa H. Purification and properties of an enzyme reducing leupeptin acid to leupeptin. Biochim Biophys Acta. 1981 Oct 13;661(2):175-81. doi: 10.1016/0005-2744(81)90001-2. PMID: 7295735. 6: Yamashita K, Watanabe K, Takayama H, Mizuguchi S, Ishibashi M, Miyazaki H, Tanaka W, Umezawa H. Assay of plasma leupeptin using the reversible binding of leupeptin to bovine pancreatic trypsin. Anal Biochem. 1986 Aug 1;156(2):503-7. doi: 10.1016/0003-2697(86)90285-x. PMID: 3766949. 7: Kieran D, Greensmith L. Inhibition of calpains, by treatment with leupeptin, improves motoneuron survival and muscle function in models of motoneuron degeneration. Neuroscience. 2004;125(2):427-39. doi: 10.1016/j.neuroscience.2004.01.046. PMID: 15062985. 8: Haspel J, Shaik RS, Ifedigbo E, Nakahira K, Dolinay T, Englert JA, Choi AM. Characterization of macroautophagic flux in vivo using a leupeptin-based assay. Autophagy. 2011 Jun;7(6):629-42. doi: 10.4161/auto.7.6.15100. Epub 2011 Jun 1. PMID: 21460622; PMCID: PMC3127049. 9: Kim IS, Lee KJ. Kinetic study on the production and degradation of leupeptin in Streptomyces exfoliatus SMF13. J Biotechnol. 1995 Aug 15;42(1):35-44. doi: 10.1016/0168-1656(95)00061-t. PMID: 7662340. 10: Salminen A. Effects of the protease inhibitor leupeptin on proteolytic activities and regeneration of mouse skeletal muscles after exercise injuries. Am J Pathol. 1984 Oct;117(1):64-70. PMID: 6385726; PMCID: PMC1900567. 11: Kim IS, Kim YB, Lee KJ. Characterization of the leupeptin-inactivating enzyme from Streptomyces exfoliatus SMF13 which produces leupeptin. Biochem J. 1998 Apr 15;331 ( Pt 2)(Pt 2):539-45. doi: 10.1042/bj3310539. PMID: 9531495; PMCID: PMC1219386. 12: Savory PJ, Rivett AJ. Leupeptin-binding site(s) in the mammalian multicatalytic proteinase complex. Biochem J. 1993 Jan 1;289 ( Pt 1)(Pt 1):45-8. doi: 10.1042/bj2890045. PMID: 8424770; PMCID: PMC1132128. 13: Veeraragavan K, Gagnon C. Leupeptin and chymostatin inhibit mammalian protein methylesterase activity. Biochem Biophys Res Commun. 1987 Jan 30;142(2):603-8. doi: 10.1016/0006-291x(87)90316-0. PMID: 3814152. 14: Ivy GO, Kanai S, Ohta M, Sato Y, Otsubo K, Kitani K. Leupeptin causes an accumulation of lipofuscin-like substances in liver cells of young rats. Mech Ageing Dev. 1991 Mar;57(3):213-31. doi: 10.1016/0047-6374(91)90048-5. PMID: 2056777. 15: Furuno K, Ishikawa T, Kato K. Appearance of autolysosomes in rat liver after leupeptin treatment. J Biochem. 1982 May;91(5):1485-94. doi: 10.1093/oxfordjournals.jbchem.a133840. PMID: 6178729. 16: Abaamrane L, Raffin F, Schmerber S, Sendowski I. Intracochlear perfusion of leupeptin and z-VAD-FMK: influence of antiapoptotic agents on gunshot-induced hearing loss. Eur Arch Otorhinolaryngol. 2011 Jul;268(7):987-93. doi: 10.1007/s00405-011-1487-0. Epub 2011 Jan 19. PMID: 21246210. 17: Ivy GO, Roopsingh R, Kanai S, Ohta M, Sato Y, Kitani K. Leupeptin causes an accumulation of lipofuscin-like substances and other signs of aging in kidneys of young rats: further evidence for the protease inhibitor model of aging. Ann N Y Acad Sci. 1996 Jun 15;786:12-23. doi: 10.1111/j.1749-6632.1996.tb39048.x. PMID: 8687013. 18: Freeman SJ, Lloyd JB. Inhibition of proteolysis in rat yolk sac as a cause of teratogenesis. Effects of leupeptin in vitro and in vivo. J Embryol Exp Morphol. 1983 Dec;78:183-93. PMID: 6663224. 19: Yao J, Qiu Y, Jia L, Zacks DN. Autophagosome immunoisolation from GFP-LC3B mouse tissue. Autophagy. 2019 Feb;15(2):341-346. doi: 10.1080/15548627.2018.1539591. Epub 2018 Oct 30. PMID: 30354910; PMCID: PMC6333448. 20: Kitano S, Irimura K, Sasaki T, Abe N, Baba A, Miyake Y, Katunuma N, Yamamoto K. Suppression of gingival inflammation induced by Porphyromonas gingivalis in rats by leupeptin. Jpn J Pharmacol. 2001 Jan;85(1):84-91. doi: 10.1254/jjp.85.84. PMID: 11243579.