Molecular structure of Leptomycin B, CAS Number: 87081-35-4
Leptomycin B (CAS 87081-35-4)
See product citations (35)
Alternate Names:
LMB; Elactocin
Application:
Leptomycin B is a potent and specific nuclear export inhibitor that acts as an antifungal agent
CAS Number:
87081-35-4
Purity:
≥95%
Molecular Weight:
540.74
Molecular Formula:
C33H48O6
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
Leptomycin B is a potent and specific nuclear export inhibitor, and class II histone deacetylase inhibitor. It alkylates and inhibits CRM1 (exportin), a protein required for nuclear export of proteins containing a nuclear export sequence (NES). In addition to antifungal and antibacterial activities, Leptomycin B blocks the cell cycle and is a potent anti-tumor agent. At low nM concentrations, it blocks the nuclear export of many proteins including HIV-1 Rev, MAPK/ERK, and NF-kappaB/IkappaB, and it stabilizes the expression of p53. Leptomycin B also inhibits the export and translation of many RNAs, including COX-2 and c-Fos mRNAs, by inhibiting export of ribonucleoproteins.
Leptomycin B (CAS 87081-35-4) References
- Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. | Kudo, N., et al. 1999. Proc Natl Acad Sci U S A. 96: 9112-7. PMID: 10430904
- HDAC4 deacetylase associates with and represses the MEF2 transcription factor. | Miska, EA., et al. 1999. EMBO J. 18: 5099-107. PMID: 10487761
- A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes. | Huang, TT., et al. 2000. Proc Natl Acad Sci U S A. 97: 1014-9. PMID: 10655476
- Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism. | Adachi, M., et al. 2000. J Cell Biol. 148: 849-56. PMID: 10704436
- Protein ligands to HuR modulate its interaction with target mRNAs in vivo. | Brennan, CM., et al. 2000. J Cell Biol. 151: 1-14. PMID: 11018049
- Leptomycin B, an inhibitor of the nuclear export receptor CRM1, inhibits COX-2 expression. | Jang, BC., et al. 2003. J Biol Chem. 278: 2773-6. PMID: 12468543
- Co-treatment with deoxycholic acid and azoxymethane accelerates secretion of HMGB1 in IEC6 intestinal epithelial cells. | Fujii, K., et al. 2009. Cell Prolif. 42: 701-9. PMID: 19614672
- Effects of leptomycin B on the cell cycle of fibroblasts and fission yeast cells. | Yoshida, M., et al. 1990. Exp Cell Res. 187: 150-6. PMID: 2298254
- Leptomycin B inhibits the proliferation, migration, and invasion of cultured gastric carcinoma cells. | Zhu, H., et al. 2020. Biosci Biotechnol Biochem. 84: 290-296. PMID: 31619134
- Involvement of PML-I in reformation of PML nuclear bodies in acute promyelocytic leukemia cells by leptomycin B. | Wang, C., et al. 2019. Toxicol Appl Pharmacol. 384: 114775. PMID: 31669778
- CRM1 Promotes Capsid Disassembly and Nuclear Envelope Translocation of Adenovirus Independently of Its Export Function. | Lagadec, F., et al. 2022. J Virol. 96: e0127321. PMID: 34757845
- Leptomycins A and B, new antifungal antibiotics. I. Taxonomy of the producing strain and their fermentation, purification and characterization. | Hamamoto, T., et al. 1983. J Antibiot (Tokyo). 36: 639-45. PMID: 6874585
- Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. | Wolff, B., et al. 1997. Chem Biol. 4: 139-47. PMID: 9190288
- CRM1 is responsible for intracellular transport mediated by the nuclear export signal. | Fukuda, M., et al. 1997. Nature. 390: 308-11. PMID: 9384386
- Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1. | Kudo, N., et al. 1998. Exp Cell Res. 242: 540-7. PMID: 9683540
- Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. | Freedman, DA. and Levine, AJ. 1998. Mol Cell Biol. 18: 7288-93. PMID: 9819415
Inhibitor of:
2310057J18Rik, 2610027L16Rik, 4930430F08Rik, 4931406C07Rik, 82-FIP, 9130206N08Rik, ANP32D, BAT1, BC005561, BRF2, C17orf39_4933439F18Rik, C18orf18, C2orf12, C7orf26, CARKD, CAT56, CELF5, CGI-96, CGI-99_2700060E02Rik, CIP29, CNBD1, CNOT1, CNOT2, CNOT3, CNOT6L, CPEB, CPSF2, CPSF4, CPSF4L, CPSF6, CRM, CRM1, CRMP-2, CRSP150_CRSP2, CstF-64, Cxx1c, D630037F22Rik, DDX27, DDX54, Deltex (DTX; E3 ubiquitin ligase), EBFP, EG240921, EG665149, ELL3, ELYS, ESF1, EXOSC1, Exportin 5, Fibrillarin, FMIP, FOXP1, GAR1, Gle1, Gm906, Gm98, GPATCH2, GTF2IRD2, Gvin1, HCFC1R1, hCG_1781062, hDcp1b, HEATR3, HEN2, HES1, HIV-1 Rev, HOTTL, hunchback, Importin-12, Importin-7, Importin-8, INTS5, ISOC2, Iws1, karyopherin α, karyopherin α5, karyopherin α6, karyopherin α7, karyopherin β1, karyopherin β2, karyopherin β3, KIAA0391, KIAA1688, KLHL38, KRR1, Lamin B2, LARP5, LOC100039560, LOC100040682, LOC100041115, LOC151174, LOC284395, LOC440900, LOC644838, LOC645553, LOC646576, LOC728392, LPPR3, LRRC59, LSm12, LSm14B, MAN1, MEL-28, Mex3a, Mex3c, Mex67, Mex67p, Midasin, MNAB, MOD5, MPP10, mrnp41, MUP16, Myosin IXb, N10, NIPA, NLP, NMD3, NNP-1, Nocturnin, NOL11, NOL8, Nop10, Nop17, NOP9, Nopp140, NPA1, nRNP, NTF2, Nup210L, NupL2, NXF7, NXT-1, p54/nrb, PABPN (poly(A) binding protein nuclear), Pan3, PAP-α, PAP-γ, PAPD4, PAPD5, PBF, Peroxin 7, Pex7p, PHYHD1, Pol I/II/III RPB8, Pol III RPC62, POLR3E, POLR3K, POM121L2, Positive cofactor 4, PSE1, PUS3, R3HCC1, Ran, Ran BP-1, Ran BP-2, Ran BP-3, Ran BP-3L, Ran BP-6, Rasl2-9, Raver1, RBM13, RBM16, RBM19, RBM23, RBM29, RBM34, RBM7, RBMS1, RBMY1, RBP, REF2, REXO2, RGPD, RNA pol β, RNase K, RNase Z1, RNPS1, RPA135, RPAIN, RPL26, Rpp20, Rpp29, Rpp38, RPS4X, RQCD1, RRP22, Rrp6, Seh1, SERHL2, SFRS17A, She, Six6os1, SLBP, Sm, Sm B, Sm B′, SMG7, SNAPC 190, Snrp116, Snurportin-1, STAU1, STOP, SUHW3, SUN1, symplekin, TAF II p100, TAF II p150, TBL3, TCEANC, TFIIE-α, TFIIF RAP 74, TFIIH 2C, TFIIIB, TFIIIC102, THOC1, THOC2, THOC3, THOC6, THUMPD1, THUMPD2, TIS11B, TOE1, Trim12c, TRUB2, TUTase, U1 snRNP 70, U2 snRNP B′′, u4/u6 snRNP, UTP11L, UTP14A, UTP14C, UTP15, UTP23, VEST1, WBSCR16, WBSCR27, WDR43, WDR61, WDR70, WDR85, XAF1, XRN2, ZBTB8OS, ZCCHC14, ZCCHC7, ZFP36L3, ZGPAT, ZNF213, and ZNF593.Activator of:
14-3-3 γ, 4933422H20Rik, ADAM19, AIP2, APC10, ASB-2, BZW1, C20orf112, Caprin1, CBP80, CD74, Cdc123, CIRH1A, CNOT10, CNOT7, Codanin-1, coilin, CPSF7, CRSP34_Med27, CSN7b, CstF-50, CstF-64, DDX1, DDX19B, DDX21, DDX50, DDX57, DIS3L, DOM3Z, DRIM, EAP1, ENOPH1, EXOSC1, EXOSC2, EXOSC5, Exportin 4, Exportin T, FBL16, FBL2, FBL6, FBP2, gp210, group VI iPLA2, hDcp1a, hDcp1b, hnRNP J, hnRNP Q, IMP-1, INTS10, INTS8, INTS9, karyopherin α3, karyopherin α6, karyopherin α7, karyopherin β2, KIAA1618, LARP7, LOC345630, LOC729978, LSm2, LSm4, LSm7, LTV1, MAGOH, MBNL3, Mex67p, MOV10, MRP-L38, MRP-S16, MRP-S18A, MRT4, NIP7, NLF1, Nop14, Nop56, Nop58, NPM3, Nup155, Nup160, Nup214, Nup37, Nup54, Nup93, NXF2, NXF7, OTUD4, p100, PABP, PABPC2, PABPC3, PABPC6, PAI-RBP1, Paip1, PATL1, PATL2, PC5/6, PHYHIP, Pol III RPC39, POLR1E, POLR2G, POLR3D, POM121L, PRA1, Rab 8B, RALYL, Ran BP-10, Ran BP-4, Ran GAP1, Rasl2-9, RBM12, RBM15, RBM32A, RBM47, RBMXL2, RBMXL3, RIA1_Eftud1, Ribosomal Protein L10L, Ribosomal Protein L12P8, Ribosomal Protein L29, Ribosomal Protein L6, Ribosomal Protein S24, Ribosomal Protein S28, RIP/Rab, RNA pol β′, RNase 2, RNase Z1, RNF184, RNF186, RPA40, RPL15, RPS4Y2, RPUSD1, RSL24D1, RUNX2, SART-3, SFRS17A, SFRS2IP, SKIV2L, Sm G, SNX5, SUGT1, SURF-6, TAPT1, TFIIIC90, TREX-2, TRIM40, TSEN2, TSR1, UBF, UNR, UTP11L, UTP14C, VPS4A, WDR3, WDR4, ZCCHC11, and ZCCHC8.Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Leptomycin B, 50 µg | sc-358688 | 50 µg | $105.00 | |||
Leptomycin B, 500 µg | sc-358688A | 500 µg | $408.00 | |||
Leptomycin B, 2.5 mg | sc-358688B | 2.5 mg | $1224.00 |