Brefeldin A

[BFA, Ascotoxin, Decumbin]



BML-G405-0005	5 mg	80.00 USD

BML-G405-0025	25 mg	270.00 USD

BML-G405-0100	100 mg	795.00 USD

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.

Formula:	C₁₆H₂₄O₄

MW:	280.4

Purity:	≥98% (TLC)

Appearance:	White to off-white solid.

CAS:	20350-15-6

MI:	14: 1369

Source/Host:	Isolated from Eupenicillium brefeldianum.

Solubility:	Soluble in DMSO (20mg/ml), 100% ethanol (5mg/ml), methanol, acetone or ethyl acetate (1mg/ml).

Shipping:	AMBIENT

Long Term Storage:	-20°C

Hazard:	HARMFUL.

Background / Technical Information:	Please click here for the comprehensive product data sheet.

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Product Literature References

Decumbin, a new compound from a species of Penicillium: V.L. Singleton, et al.; Nature 181, 1072 (1958),

Über die Isolierung neuer Stoffwechselprodukte aus Penicillium brefeldianum Dodge.: E. Harri, et al.; Helv. Chim. Acta 46, 1235 (1963),

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

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

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;

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;

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;

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 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;

Brefeldin A: the advantage of being uncompetitive: P. Chardin & F. McCormick; Cell 97, 153 (1999), Abstract;

Brefeldin A: deciphering an enigmatic inhibitor of secretion: A. Nebenfuhr, et al.; Plant Physiol. 130, 1102 (2002), Review, 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

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;