3X FLAG® Peptide

lyophilized powder

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
Empirical Formula (Hill Notation):
Molecular Weight:
MDL number:


lyophilized powder

Quality Level


(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.


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).


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. For the gentle elution of 3X FLAG fusion proteins from the ANTI-FLAG® M2 affinity gels. 1X FLAG Peptide (F3290) will not elute 3X FLAG fusion proteins from ANTI-FLAG® affinity gels.

Browse additional application references in our FLAG® Literature portal.

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.

Legal Information

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

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Raghu R Edupuganti et al.
Nature structural & molecular biology, 24(10), 870-878 (2017-09-05)
RNA modifications are integral to the regulation of RNA metabolism. One abundant mRNA modification is N
Andrew T Schiffmacher et al.
The Journal of cell biology, 215(5), 735-747 (2016-11-20)
During epithelial-to-mesenchymal transitions (EMTs), cells disassemble cadherin-based junctions to segregate from the epithelia. Chick premigratory cranial neural crest cells reduce Cadherin-6B (Cad6B) levels through several mechanisms, including proteolysis, to permit their EMT and migration. Serial processing of Cad6B by a...
Oriane Mauger et al.
Nucleic acids research, 43(3), 1869-1882 (2015-01-22)
Alternative splicing is the main source of proteome diversity. Here, we have investigated how alternative splicing affects the function of two human histone methyltransferases (HMTase): G9A and SUV39H2. We show that exon 10 in G9A and exon 3 in SUV39H2...
Ninghai Gan et al.
Nature, 572(7769), 387-391 (2019-07-23)
The bacterial pathogen Legionella pneumophila creates an intracellular niche permissive for its replication by extensively modulating host-cell functions using hundreds of effector proteins delivered by its Dot/Icm secretion system1. Among these, members of the SidE family (SidEs) regulate several cellular...
Min Hwa Shin et al.
PLoS genetics, 12(2), e1005884-e1005884 (2016-03-02)
The inactivation of p53 creates a major challenge for inducing apoptosis in cancer cells. An attractive strategy is to identify and subsequently target the survival signals in p53 defective cancer cells. Here we uncover a RUNX2-mediated survival signal in p53...
Comparison of elution techniques for small-scale protein purification of FLAG® tag proteins using anti-FLAG® M2 magnetic beads.
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Protocol for immunoprecipitation (IP) of FLAG fusion proteins using M2 monoclonal antibody 4% agarose affinity gels
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