F4799 Sigma

3X FLAG® Peptide

lyophilized powder

Synonym: Met-Asp-Tyr-Lys-Asp-His-Asp-Gly-Asp-Tyr-Lys-Asp-His-Asp-Ile-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys, ddddk peptide, dykddddk peptide



Related Categories FLAG Affinity Purification, FLAG Peptides, FLAG System, Molecular Biology, Plant Biotechnology,
form   lyophilized powder
concentration   (Recommended working concentration is 100 μg/ml for elute 3X FLAG fusion proteins from the ANTI-FLAG® M2 affinity gel.)
shipped in   wet ice
storage temp.   2-8°C


Preparation Note

To prepare a stock solution, dissolve in TBS (50 mMTris-HCl, pH 7.4, with 150 mM NaCl) at a concentration of 5 mg/ml.


For use in competitive elution of 3X FLAG® fusion proteins from the ANTI-FLAG® M2 monoclonal antibody (F1804) in solution or bound to agarose on the ANTI-FLAG® M2 agarose affinity gel (A2220). This is achieved by Affinity Chromatography.

Browse additional application references in our FLAG® Literature portal.

General description

The 3X FLAG Peptide is a synthetic peptide of 23 amino acid residue. The Asp-Tyr-Lys-Xaa-Xaa-Asp motif is repeated three times in the peptide. Eight amino acids at the C-terminus make up the classic FLAG sequence (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys).

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ANTI-FLAG is a registered trademark of Sigma-Aldrich Co. LLC

FLAG is a registered trademark of Sigma-Aldrich Co. LLC

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Safety Information

WGK Germany 
Protocols & Articles
Peer-Reviewed Papers


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Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans Doyon,Y et al. Mol. Cell. Biol. 24(25), 1884-1896, (2004)


TopBP1 Activates the ATR-ATRIP Complex Kumagai,A et al. Cell 124(5), 943-955, (2006)


Development of a Protein Chip: A MS-Based Method for Quantitation of Protein Expression and Modification Levels Using an Immunoaffinity Approach Warren,E et al. Anal. Chem. 76(14), 4082-4092, (2004)


Evidence for an alternative glycolytic pathway in rapidly proliferating cells. Vander Heiden, M.G., et al. Science 1492, 1492-9, (2010)


Alternative splicing regulates the expression of G9A and SUV39H2 methyltransferases, and dramatically changes SUV39H2 functions. Mauger O, Klinck R, Chabot B, et al. Nucleic Acids Res. 43(3), 1869-82, (2015)


Genome-wide analysis of phosphorylated PhoP binding to chromosomal DNA reveals several novel features of the PhoPR-mediated phosphate limitation response in Bacillus subtilis. Salzberg LI, Botella E, Hokamp K, et al. J. Bacteriol. 197(8), 1492-506, (2015)


EphrinB1: novel microtubule associated protein whose expression affects taxane sensitivity. Colbert PL, Vermeer DW, Wieking BG, et al. Oncotarget 6(2), 953-68, (2015)


Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling. Vallabhapurapu S Nat. Immunol. 9(12), 1364-70, (2008)


The SET domain proteins SUVH2 and SUVH9 are required for Pol V occupancy at RNA-directed DNA methylation loci. Liu ZW, Shao CR, Zhang CJ, et al. PLoS Genet. 10(1), e1003948, (2014)


Characterization of mouse IFT complex B. Follit JA Cell Motil. Cytoskeleton 66(8), 457-68, (2009)


RFXB and its splice variant RFXBSV mediate the antagonism between IFNgamma and TGFbeta on COL1A2 transcription in vascular smooth muscle cells. Fang M Nucleic Acids Res. 37(13), 4393-406, (2009)


Mutations in the human naked cuticle homolog NKD1 found in colorectal cancer alter Wnt/Dvl/beta-catenin signaling. Guo J, Cagatay T, Zhou G, et al. PLoS ONE 4(11), e7982, (2009)


Enzymatically inactive U(S)3 protein kinase of Marek's disease virus (MDV) is capable of depolymerizing F-actin but results in accumulation of virions in perinuclear invaginations and reduced virus growth. Schumacher D Virology 375(1), 37-47, (2008)


The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment. Colombo M Virol. J. 6, 59, (2009)


NEDD4 ubiquitinates TRAF3 to promote CD40-mediated AKT activation. Fang DF, He K, Wang N, et al. Nat. Commun. 5, 4513, (2014)


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