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F4799

Sigma-Aldrich

3xFLAG™ Peptide

≥90% (HPLC/MS), lyophilized powder

Synonym(s):

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

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About This Item

Empirical Formula (Hill Notation):
C120H169N31O49S
Molecular Weight:
2861.87
MDL number:
MFCD01863911
UNSPSC Code:
12352202
NACRES:
NA.32

product name

3X FLAG® Peptide, lyophilized powder

assay

≥90% (HPLC/MS)

Quality Level

200

form

lyophilized powder

shipped in

wet ice

storage temp.

2-8°C

General description

Recommended working concentration is 100 μg/ml for elute 3X FLAG fusion proteins from the ANTI-FLAG® M2 affinity gel.
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).

Application

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.


Learn more product details in our FLAG® application 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 Merck KGaA, Darmstadt, Germany
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

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Certificates of Analysis (COA)

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Yannick Doyon et al.
Molecular and cellular biology, 24(5), 1884-1896 (2004-02-18)
The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. Its catalytic component, Esa1, is essential for cell cycle progression, gene-specific regulation and has been implicated in DNA repair. Almost
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
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
Monika Raab et al.
Nature communications, 8, 16001-16001 (2017-07-13)
Lymphocyte function-associated antigen 1 (LFA-1) affinity and avidity changes have been assumed to mediate adhesion to intercellular adhesion molecule-1 for T-cell conjugation to dendritic cells (DC). Although the T-cell receptor (TCR) and LFA-1 can generate intracellular signals, the immune cell
Radu Tusco et al.
Nature communications, 8(1), 1264-1264 (2017-11-04)
Selective autophagy is a catabolic process with which cellular material is specifically targeted for degradation by lysosomes. The function of selective autophagic degradation of self-components in the regulation of innate immunity is still unclear. Here we show that Drosophila Kenny
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