Replaces Prod. #: ALX-350-019
Inhibitor of intracellular protein transport and protein secretion, interfering with trafficking in the trans-Golgi network, leading to the accumulation of cycling proteins in ERGIC clusters. Blocks ADP-ribosylation factor (Arf) in an inactive GDP-bound conformation and thereby prevents binding of COPI coats to ERGIC and Golgi membranes. Upon brefeldin A treatment the Golgi rapidly tubulates and fuses with the ER by an energy-, temperature-, and microtubule-dependent process. In contrast, the drug has little effect on the ERGIC, which keeps its identity, although the ERGIC clusters become larger and more uniformly distributed in the cytoplasm of the cells. Inhibits intracellular collagen degradation. Also inhibits apical Na+ channels in epithelia. Induces apoptosis.
Product Details
| Alternative Name: | BFA, Ascotoxin, Decumbin |
| |
| Formula: | C16H24O4 |
| |
| MW: | 280.4 |
| |
| Source: | Isolated from Eupenicillium brefeldianum. |
| |
| CAS: | 20350-15-6 |
| |
| MI: | 14: 1369 |
| |
| Purity: | ≥98% (HPLC) |
| |
| Appearance: | White to off-white solid. |
| |
| Solubility: | Soluble in DMSO (20mg/ml), 100% ethanol (5mg/ml), methanol, acetone or ethyl acetate (1mg/ml). |
| |
| Shipping: | Ambient |
| |
| Long Term Storage: | -20°C |
| |
| Regulatory Status: | RUO - Research Use Only |
| |
Please mouse over
Product Literature References
Proteomic Profiling and Functional Analysis of B Cell-Derived Exosomes upon Pneumocystis Infection: D. Ma, et al.; J. Immunol. Res.
2022, 5187166 (2022),
Abstract;
Proteostasis regulators restore function of epilepsy-associated GABAA receptors: X. Di, et al.; Cell Chem. Biol.
28, 46 (2021),
Abstract;
Full Text
TLR agonists enhance responsiveness of inflammatory innate immune cells in HLA-B*57-positive HIV patients: L. Dold, et al.; J. Mol. Med. (Berl.)
99, 147 (2021),
Application(s): TLR activation of monocytes and NK cells,
Abstract;
Full Text
Shp-2 is critical for ERK and metabolic engagement: C. Niogret, et al.; Nat. Commun.
10, 1444 (2019),
Abstract;
Full Text
Shp-2 is critical for ERK and metabolic engagement downstream of IL-15 receptor in NK cells: C. Niogret, et al.; Nat. Commun.
10, 1444 (2019),
Abstract;
Full Text
Mesenchymal stem cells alleviate experimental autoimmune cholangitis through immunosuppression and cytoprotective function mediated by galectin-9: J. Fan, et al.; Stem Cell Res. Ther.
9, 237 (2018),
Abstract;
Mesenchymal stem cells induced CD4+ T cell apoptosis in treatment of lupus mice: S. Huang, et al.; Biochem. Biophys. Res. Commun.
507, 30 (2018),
Abstract;
Puerarin attenuates smoke inhalation injury by regulation of Th1/Th2 expression and inhibition of Th17 cells in rats: F. Zhang, et al.; Int. Immunopharmacol.
28, 546 (2015),
Application(s): Cell culture ,
Abstract;
Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70: K.F. Xu, et al.; PNAS
102, 2784 (2005),
Abstract;
NKT cells provide help for dendritic cell-dependent priming of MHC class I-restricted CD8+ T cells in vivo: D. Stober, et al.; J. Immunol.
170, 2540 (2003),
Abstract;
Full Text
Brefeldin A: deciphering an enigmatic inhibitor of secretion: A. Nebenfuhr, et al.; Plant Physiol.
130, 1102 (2002), Review,
Abstract;
Brefeldin A: the advantage of being uncompetitive: P. Chardin & F. McCormick; Cell
97, 153 (1999),
Abstract;
Brefeldin A inhibition of apical Na+ channels in epithelia: R.S. Fisher, et al.; Am. J. Physiol.
270, C138 (1996),
Abstract;
Brefeldin A is a potent inducer of apoptosis in human cancer cells independently of p53: R.G. Shao, et al.; Exp. Cell Res.
227, 190 (1996),
Abstract;
Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes: P.A. Randazzo, et al.; J. Biol. Chem.
268, 9555 (1993),
Abstract;
Brefeldin A inhibits degradation as well as production and secretion of collagen in human lung fibroblasts: C.R. Ripley, et al.; J. Biol. Chem.
268, 3677 (1993),
Abstract;
Brefeldin A and the endocytic pathway. Possible implications for membrane traffic and sorting: W. Hunziker, et al.; FEBS Lett.
307, 93 (1992), (Review),
Abstract;
Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein: J.G. Donaldson, et al.; Nature
360, 350 (1992),
Abstract;
Brefeldin A, thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis: B.D. Price, et al.; J. Cell. Physiol.
152, 545 (1992),
Abstract;
Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF: J.B. Helms & J.E. Rothman; Nature
360, 352 (1992),
Abstract;
Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein: J.G. Donaldson, et al.; Science
254, 1197 (1991),
Abstract;
Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae: L. Orci, et al.; Cell
64, 1183 (1991),
Abstract;
Guanine nucleotides modulate the effects of brefeldin A in semipermeable cells: regulation of the association of a 110-kD peripheral membrane protein with the Golgi apparatus: J.G. Donaldson, et al.; J. Cell Biol.
112, 579 (1991),
Abstract;
Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway: J. Lippincott-Schwartz, et al.; Cell
60, 821 (1990),
Abstract;
Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum: T. Fujiwara, et al.; J. Biol. Chem.
263, 18545 (1988),
Abstract;
Full Text
Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes: Y. Misumi, et al.; J. Biol. Chem.
261, 11398 (1986),
Abstract;
Full Text
Über die Isolierung neuer Stoffwechselprodukte aus Penicillium brefeldianum Dodge.: E. Harri, et al.; Helv. Chim. Acta 46, 1235 (1963),
Decumbin, a new compound from a species of Penicillium: V.L. Singleton, et al.; Nature
181, 1072 (1958),
Abstract;
