Molecular structure of Leupeptin hemisulfate, CAS Number: 55123-66-5
Leupeptin hemisulfate (CAS 103476-89-7)
See product citations (19)
Alternate Names:
Leupeptin hemisulfate also known as N-Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate salt; Acetyl-leucyl-leucyl-arginal
Application:
Leupeptin hemisulfate is a reversible, competitive protease inhibitor of proteases cathepsin, calpain, and trypsin
CAS Number:
103476-89-7
Molecular Weight:
475.59
Molecular Formula:
C20H38N6O4•1/2H2SO4
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.
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SDS & Certificate of Analysis
Leupeptin hemisulfate is a reversible, competitive protease inhibitor that may act to inhibit cathepsins B, H, L, and S, calpain, and trypsin. It is also a reversible inhibitor of cysteine, serine and threonine proteases that are produced naturally by Streptomyces. Leupeptin hemisulfate has no effect against chymotrypsin, elastase, renin or pepsin. In biochemical research, it is used frequently as a reducing agent in experiments designed to study proteins, enzymes, amino acids and neuropeptides. Leupeptin hemisulfate can also be used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest. Overall, researchers use it to study the effects of protease inhibition on cell metabolism, enzyme activity, gene expression, protein synthesis, protein degradation, and protein folding.
Leupeptin hemisulfate (CAS 103476-89-7) References
- Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1. | Fassati, A. and Goff, SP. 2001. J Virol. 75: 3626-35. PMID: 11264352
- Sequence analysis, tissue distribution, and expression of rat cathepsin S. | Petanceska, S. and Devi, L. 1992. J Biol Chem. 267: 26038-43. PMID: 1281481
- Phosphorylation of p70s6 kinase is implicated in androgen-induced levator ani muscle anabolism in castrated rats. | Xu, T., et al. 2004. J Steroid Biochem Mol Biol. 92: 447-54. PMID: 15698549
- Microtubules in mesophyll cells of nonacclimated and cold-acclimated spinach: visualization and responses to freezing, low temperature, and dehydration. | Bartolo, ME. and Carter, JV. 1991. Plant Physiol. 97: 175-81. PMID: 16668366
- Inhibitors of cathepsin B. | Frlan, R. and Gobec, S. 2006. Curr Med Chem. 13: 2309-27. PMID: 16918357
- Characterization of vascular-specific RSs1 and rolC promoters for their utilization in engineering plants to develop resistance against hemipteran insect pests. | Saha, P., et al. 2007. Planta. 226: 429-42. PMID: 17323077
- Analysis of the limitations of hepatitis B surface antigen expression in soybean cell suspension cultures. | Ganapathi, TR., et al. 2007. Plant Cell Rep. 26: 1575-84. PMID: 17534624
- Isolation of Cytokinetic Actomyosin Rings from Saccharomyces cerevisiae and Schizosaccharomyces pombe. | Huang, J., et al. 2016. Methods Mol Biol. 1369: 125-136. PMID: 26519310
- Inhibition of plant cell proteolytic activities that degrade tubulin. | Morejohn, LC., et al. 1985. Cell Biol Int Rep. 9: 849-57. PMID: 2864138
- Preparation of Clathrin-Coated Vesicles From Arabidopsis thaliana Seedlings. | Mosesso, N., et al. 2018. Front Plant Sci. 9: 1972. PMID: 30687367
- Leupeptins, new protease inhibitors from Actinomycetes. | Aoyagi, T., et al. 1969. J Antibiot (Tokyo). 22: 283-6. PMID: 5810993
- Taxol-induced rose microtubule polymerization in vitro and its inhibition by colchicine. | Morejohn, LC. and Fosket, DE. 1984. J Cell Biol. 99: 141-7. PMID: 6145718
- Cathepsin B, Cathepsin H, and cathepsin L. | Barrett, AJ. and Kirschke, H. 1981. Methods Enzymol. 80 Pt C: 535-61. PMID: 7043200
- Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin. | Knight, CG. 1980. Biochem J. 189: 447-53. PMID: 7213339
Inhibitor of:
α2-Macroglobulin, α2ML1, 2310051M13Rik, 5430419D17Rik, 8030411F24Rik, 9330182L06Rik, A430107O13Rik, ACP2, Acrosin, Antipain dihydrochloride, apoL10a, apoL10b, apoL7a, apoL7c, apoL7e, ARRDC5, ASB-1, ASB-12, ASB-3, ASB-7, ASTL, Atg4a, Atg4D, ATP-BL, BC048546, BLM hydrolase, BLOS3, Calpain, Calpain 15_Solh, Cathepsin, cathepsin 8, cathepsin A, cathepsin B, cathepsin H, cathepsin J, cathepsin L, cathepsin M, cathepsin Q, cathepsin S, CFBP, CHIC2, Chondroitinase, Chymostatin, Chymotrypsin, CLAP, CLN5, CLPSL1, Corin, CPA1, CPA2, CPA5, CPAMD8, CPB, CPD, CPVL, CST, Cst9, CSTL1, CTLA-2α, cystatin 10, cystatin 12, cystatin 13, cystatin 8, cystatin 9, cystatin B, cystatin C, Cystatin D, cystatin E/M, cystatin F, cystatin SN, Desc4, EG433016, EG622976, EG667977, EMID1, ENSMUSG00000071517, EPDR1, ERAP1, ERp27, FAM162B, FIBCD1, Gm46, GNPTG, GNS, granzyme A, granzyme C, granzyme E, granzyme G, granzyme H, granzyme M, granzyme N, H2-Aa, H2-Q1, H2-Q10, H2-T10, H2-T22, H2-T9, HECTD1, HECTD2, HKIB9, HLA-B, HLA-B7, HLA-DM, HLA-DR, HLA-DX, HPS-6, HtrA4, Intra-acrosomal protein, ITM2B, Jade-1, Kex2, Kininogen II, KLHDC7A, Klk1b4, Klk26, KLKb2, Klkb21, Klkb22, KLKBL4, LAMP-2, Legumain, LMBRD1, LOC100042018, LOC150935, LOC728379, LOC728400, LRRC42, LRRC43, LYZL1, Marapsin 2, Mast Cell Protease, Mast Cell Protease 8, Matriptase-2, MC-CPA, mCST E2, megsin, Mesotrypsinogen, MHC class IIβ, MHC Ts H-2s,f, Mill1, MRCL3, MUP2, MUP3, MUP4, murinoglobulin 2, NAGPA, neuroserpin, Neurotrypsin, ORAOV1, OTTMUSG00000013284, OTTMUSG00000014862, OTTMUSG00000015173, OTTMUSG00000015220, OTTMUSG00000015279, OTTMUSG00000015337, OTTMUSG00000015417, OTTMUSG00000015643, OTTMUSG00000015752, OTTMUSG00000016293, OVCA2, P-Rex2, PAI-2, Papain, PC5/6, PCIA1, PCSK1N, PERP (p53 apoptosis effector related to PMP22), PGPEP1L, PNAd, Polyserase-1, POP2, PQLC1, PRB2, PRB3, prochymosin, Pronase, Prostasin, Protease, PRSS16, Prss32, PRSS33, Prss34, PRSS35, PRSS37, Prss39, Prss47, PRSS50, PRSS51, PRSSL1, Rab L5, RHBDD2, RHBDL2, Rhomboid, RNF115, RNF181, RT1-Bβ, SCGB1D4, Sel-1L3, Semenogelin-2, SerpinA11, SerpinA1b, SerpinA1d, SerpinA1e, SerpinA2, SerpinA3g, SerpinA3j, SerpinA3n, SerpinB1b, Serpinb3c, Serpinb3d, SerpinB6B, SerpinB6C, Serpinb6d, SerpinB6e, SerpinB8, SerpinB9g, SERPINE3, SPCS3, spectrin β II, Spi10, Spi11, SPINK14, SPINK2, SPINK6, SPINK7, SPUVE, stefin A1L1, stefin A2, stefin A2l1, stefin A3L1, Svs7, TAPBPL, TATI, Testisin, TFEB, TIP120, TLCK, TMEM169, TMPRSS11A, TMPRSS11B, TMPRSS11E, TMPRSS11F, TMPRSS12, TMPRSS13, TMPRSS3, TMPRSS4, TMPRSS5, TPCK, TPPII, TRAP, TRIM30B, TRIM38, TRIM43, TRIM43B, TRIM44, TRIM49B, TRIM50, TRIM6, TRIM6-TRIM34, TRIM64B, TRIM64C, Trypsin, Trypsin X3, Trypsin-1, Trypsin-10, Trypsin-3, Tryptase γ, uPA, USP26, V3R 2, Vmn2r62, Vmn2r70, Vrho, WFDC17, ZFP30, ZP4, and ZUFSP.Activator of:
1700074P13Rik, 2010005H15Rik, 2310051M13Rik, 9330182L06Rik, Aminopeptidase B, APEH, Arylsulfatase I, BC100530, bectenecin, Calpain 15_Solh, Calpain II, cathepsin Q, CD63, Chromozym TRY, CLN1, CRISP-8, CT45-1, CTBS, cystatin 11, EG433016, ERAP2, FBXO29, FucT-X, GILT, group IIF sPLA2, H2-Db, H2-T22, HAI-1, HAI-2, HSBP1L1, KIAA0776, KLHL15, KLK15, Klk1b4, Klk26, KLK9, KLKb2, KLKb8, LIMP I, LOC646960, LONRF1, Lyst, MARCH4, MFSD8, murinoglobulin 2, Ocathepsin, PACE4, PN-1, PRSS16, Prss28, PRSS35, Prss39, Prss47, PRSS55, SERHL, SerpinA1c, SerpinA3i, SerpinB1b, Serpinb3b, SerpinB6C, SerpinB9g, stefin A1, stefin A1L1, stefin A2, stefin A3, Tesp2, TESSP-1, TMPRSS11B, TMPRSS11C, TMPRSS11E2, TMPRSS11F, TMPRSS13, TMPRSS3, TMPRSS5, TMPRSS7, TMPRSSs8, TPSB1, TRC8, Trypsin-4, tsg 101, UBE1L2, UBE2B, UBL5, Ubr1, UFD2, and UNQ9391.Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Leupeptin hemisulfate, 5 mg | sc-295358 | 5 mg | $72.00 | |||
Leupeptin hemisulfate, 10 mg | sc-295358C | 10 mg | $99.00 | |||
Leupeptin hemisulfate, 25 mg | sc-295358A | 25 mg | $145.00 | |||
Leupeptin hemisulfate, 50 mg | sc-295358D | 50 mg | $265.00 | |||
Leupeptin hemisulfate, 100 mg | sc-295358E | 100 mg | $489.00 | |||
Leupeptin hemisulfate, 500 mg | sc-295358B | 500 mg | $1399.00 |