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Leptomycin B

Nuclear export inhibitor
ALX-380-100-C100 100 µg 142.00 USD
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Replaces Prod. #: BML-GR338

A potent and specific nuclear export inhibitor. Leptomycin B alkylates and inhibits CRM1/exportin 1, a protein required for nuclear export of proteins containing a nuclear export sequence (NES). In addition to antifungal and antibacterial activities, blocks the cell cycle and is a potent anti-tumor agent. At low nM concentrations, blocks the nuclear export of many proteins including HIV-1 Rev, MAPK/ERK, and NF-κB/IκB and it stabilizes the expression of p53. Other proteins that are influenced by leptomycin B are actin, c-Abl, cyclin B1, MDM2/p53, Iκb, MPF and PKA. Leptomycin B also inhibits the export and translation of many RNAs, including COX-2 and c-Fos mRNAs, by inhibiting export of ribonucleoproteins.

Product Specification

Alternative Name:LMB
Source:Isolated from Streptomyces sp.
Formulation:Solution in 100% ethanol.
Purity:≥96% (HPLC)
Solubility:Soluble in methanol or 100% ethanol; insoluble in water. Unstable in DMSO.
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
Handling:Protect from light. Packaged under inert gas.
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Product Literature References

Ratjadone and leptomycin B block CRM1-dependent nuclear export by identical mechanisms: T. Meissner, et al.; FEBS Lett. 576, 27 (2004), Abstract;
Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism: M. Adachi, et al.; J. Cell. Biol. 148, 849 (2000), Abstract;
Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region: N. Kudo, et al.; PNAS 96, 9112 (1999), Abstract;
CRM1 is responsible for intracellular transport mediated by the nuclear export signal: M. Fukuda, et al.; Nature 390, 308 (1997), Abstract;
Effects of leptomycin B on the cell cycle of fibroblasts and fission yeast cells: M. Yoshida, et al.; Exp. Cell Res. 187, 150 (1990), Abstract;
Leptomycins A and B, new antifungal antibiotics. I. Taxonomy of the producing strain and their fermentation, purification and characterization: T. Hamamoto, et al.; J. Antibiot. (Tokyo) 36, 639 (1983), Abstract;

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