Product Description
Brefeldin A is a specific inhibitor of protein trafficking which blocks the protein transport from the endoplasmic reticulum to the Golgi complex.
IC50 & Target: Autophagy[4], CRISPR/Cas9[5]
In Vitro: Brefeldin A treatment for 15 h or 40 h, causes dramatic swelling of the Endoplasmic Reticulum (ER) and shifts its localization to the periphery of normal rat kidney (NRK) cells. Prolonged Brefeldin A treatment results in marked disruption of the MT and actin cytoskeleton[1]. ADP-ribosylation of BARS is mediated by formation of a conjugate between Brefeldin A and ADPR. BARS shows BAC binding when incubated with the medium from the BFA-treated CD38+ HeLa cells[2]. Brefeldin A induces anchorage-independent cell death in MDA-MB-231 breast cancer cells, inhibits the formation of MDA-MB-231 colonies in 3D and 2D cultures and inhibits the migration and MMP 9 (Matrix Metallopeptidase 9) activity of MDA-MB-231[3].
Information
CAS No20350-15-6
FormulaC16H24O4
Clinical Informationclinicalinformation
PathwayAnti-infection
Autophagy
Cell Cycle/DNA Damage
TargetAntibiotic
Autophagy
Bacterial
CRISPR/Cas9
HSV
Mitophagy
Specifications
FormWhite to off-white (Solid)
Purity / Grade99.10%
SolubilityDMSO : 100 mg/mL (356.68 mM; Need ultrasonic);
Ethanol :11.11 mg/mL (39.63 mM; Need ultrasonic)
SmilesO[C@@H]1C[C@]2([H])[C@@](/C=C/CCC[C@H](C)OC(/C=C/[C@H]2O)=O)([H])C1
Misc Information
Alternative NamesBFA;Cyanein;Decumbin; 4H-Cyclopent[f]oxacyclotridecin-4-one, 1, 6, 7, 8, 9, 11a, 12, 13, 14, 14a-decahydro-1, 13-dihydroxy-6-methyl-, (1R, 2E, 6S, 10E, 11aS, 13S, 14aR)-
Observed Molecular Weight280.36
References[1]. Alvarez C, et al. Brefeldin A (BFA) disrupts the organization of the microtubule and the actin cytoskeletons. Eur J Cell Biol. 1999 Jan;78(1):1-14.
[2]. Colanzi A, et al. Molecular mechanism and functional role of brefeldin A-mediated ADP-ribosylation of CtBP1/BARS. Proc Natl Acad Sci U S A. 2013
Jun 11;110(24):9794-9.
[3]. Tseng CN, et al. Brefeldin A reduces anchorage-independent survival, cancer stem cell potential and migration of MDA-MB-231 human breast cancer
cells. Molecules. 2014 Oct 29;19(11):17464-77.
[4]. Wang J, et al. Erythroleukemia cells acquire an alternative mitophagy capability. Sci Rep. 2016 Apr 19;6:24641.
[5]. Yu C, et al. Small molecules enhance CRISPR genome editing in pluripotent stem cells. Cell Stem Cell. 2015 Feb 5;16(2):142-7.
[6]. Nozawa N, et al. Subcellular localization of herpes simplex virus type 1 UL51 protein and role of palmitoylation in Golgi apparatus targeting. J Virol.
2003 Mar;77(5):3204-16.
[7]. Jensen HL, Rygaard J, Norrild B. A time-related study of Brefeldin A effects in HSV-1 infected cultured human fibroblasts. APMIS. 1995;103(7-8):530-
539. doi:10.1111/j.1699-0463.1995.tb01402.x