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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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Pricing

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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