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Antifungal antibiotic that is an inhibitor of the nuclear export of proteins; acts by binding directly to and inhibiting CRM1/exportin-1. Inhibits the nuclear export of the HIV regulatory protein Rev and stabilizes p53. Antitumor in vitro and in vivo.
|Storage||Desiccate at -20°C|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
|Solubility||Soluble in ethanol (supplied pre-dissolved in anhydrous ethanol, 27µg/ml)|
References are publications that support the biological activity of the product.
Roberts et al (1986) In vivo and in vitro anticancer activity of the structurally novel and highly potent antibiotic CI 940 and its hydroxy analog (PD 114,721). Cancer Chemother.Pharmacol. 16 95 PMID: 3081269
Wolff et al (1997) Leptomycin B is an inhibitor of nuclear export: inhibition of nucleocytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem.Biol. 4 139 PMID: 9190288
Freedman and Levine (1998) Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol.Cell.Biol. 18 7288 PMID: 9819415
Kudo et al (1998) Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1. Exp.Cell Res. 242 540 PMID: 9683540
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Keywords: Leptomycin B, Leptomycin B supplier, inhibitors, inhibits, nuclear, export, proteins, antitumor, Protein, Translocation, LeptomycinB, CI940, antibiotics, CI, 940, LMB, Translocation,, Exocytosis, &, Endocytosis, Antibiotics, 1987, Tocris Bioscience
3 Citations for Leptomycin B
Citations are publications that use Tocris products. Selected citations for Leptomycin B include:
Cao et al (2014) Characterization of the nucleocytoplasmic shuttle of the matrix protein of influenza B virus. J Virol 88 7464 PMID: 24741102
Cao et al (2012) A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication. J Virol 86 4883 PMID: 22345442
Horan et al (2013) Proteasomal degradation of herpes simplex virus capsids in macrophages releases DNA to the cytosol for recognition by DNA sensors. J Immunol 190 2311 PMID: 23345332
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