FLAG peptide is an eight amino acids peptide (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys) with an enterokinase-cleavage site; designed for antibody-mediated identification and purification of recombinant proteins.
CAT No: R1355
CAS No:98849-88-8
Synonyms/Alias:FLAG peptide;Dykddddk peptide;98849-88-8;FLAG tag Peptide;DYKDDDDK;Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys;FLAG(TM) peptide;D-Y-K-D-D-D-D-K;(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]hexanoyl]amino]-3-carboxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-carboxypropanoyl]amino]hexanoic acid;CHEBI:189550;H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH;L-Asp-L-Tyr-L-Lys-L-Asp-L-Asp-L-Asp-L-Asp-L-Lys;L-alpha-aspartyl-L-tyrosyl-L-lysyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alpha-aspartyl-L-lysine;FLAG Epitope Peptide;FLAG Peptide TFA salt;SCHEMBL266555;EX-A7479;HY-P0223;Trypsinogen (human pancreas isoenzyme 2 activation peptide), 1-L-aspartic acid-2-L-tyrosine-3-L-lysine-;FLAG(R) Peptide, lyophilized powder;AKOS040763947;CS-6485;FF73381;DA-63459;(2S)-6-AMINO-2-[(2S)-2-[(2S)-2-[(2S)-2-[(2S)-2-[(2S)-6-AMINO-2-[(2S)-2-[(2S)-2-AMINO-3-CARBOXYPROPANAMIDO]-3-(4-HYDROXYPHENYL)PROPANAMIDO]HEXANAMIDO]-3-CARBOXYPROPANAMIDO]-3-CARBOXYPROPANAMIDO]-3-CARBOXYPROPANAMIDO]-3-CARBOXYPROPANAMIDO]HEXANOIC ACID;(2S,5S,8S,11S,14S,17S,20S,23S)-23-amino-2,17-bis(4-aminobutyl)-5,8,11,14-tetrakis(carboxymethyl)-20-(4-hydroxybenzyl)-4,7,10,13,16,19,22-heptaoxo-3,6,9,12,15,18,21-heptaazapentacosane-1,25-dioic acid;
Chemical Name:(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]hexanoyl]amino]-3-carboxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-carboxypropanoyl]amino]hexanoic acid
FLAG peptide is a synthetic peptide epitope widely recognized for its pivotal role in molecular biology and protein research. Comprising a short, hydrophilic amino acid sequence, it is specifically designed to serve as an affinity tag for recombinant protein expression and purification. The sequence's compact structure minimizes interference with protein folding and function, making it a preferred choice for tagging proteins in various expression systems. Its high specificity for anti-FLAG antibodies enables precise detection and isolation, contributing to its popularity in both academic and industrial research settings. The FLAG tag system has become an indispensable tool for facilitating downstream analyses and functional studies, reflecting its robust utility across diverse biochemical applications.
Protein purification: One of the primary applications of the FLAG peptide is in affinity-based purification of recombinant proteins. When fused to target proteins, the peptide tag enables highly selective binding to anti-FLAG affinity resins or columns, allowing researchers to isolate tagged proteins from complex mixtures with high specificity. This approach streamlines the purification process, reducing background contamination and preserving protein integrity, which is essential for subsequent biochemical and structural analyses.
Immunodetection and localization: The FLAG tag is extensively used in immunodetection assays such as Western blotting, immunoprecipitation, and immunofluorescence microscopy. Its unique sequence is recognized with high affinity by monoclonal anti-FLAG antibodies, facilitating sensitive and specific detection of tagged proteins in cellular lysates or tissue samples. This capability is particularly valuable for tracking protein expression, monitoring subcellular localization, and verifying successful transfection or expression in various host systems.
Protein-protein interaction studies: Researchers employ FLAG-tagged constructs to investigate protein-protein interactions through co-immunoprecipitation or pull-down assays. By capturing FLAG-tagged bait proteins and their associated binding partners, scientists can dissect complex interaction networks and elucidate functional protein complexes. The tag's compatibility with gentle elution conditions helps maintain the native state of multiprotein assemblies, supporting accurate characterization of dynamic molecular interactions.
Functional analysis of recombinant proteins: The incorporation of the FLAG sequence into recombinant proteins allows for efficient functional studies, including activity assays and mutagenesis experiments. The tag's minimal size and low immunogenicity reduce the risk of perturbing the protein's native conformation or activity. This feature enables researchers to assess the biological properties of engineered proteins, validate functional domains, and systematically analyze structure-function relationships in vitro and in vivo.
Quality control and assay development: In the context of assay development and quality control, the FLAG peptide serves as a reliable positive control or standard. Its defined sequence and well-characterized immunoreactivity make it suitable for calibrating immunoassays, validating antibody specificity, and optimizing detection protocols. By providing a consistent benchmark, it supports reproducibility and accuracy in quantitative and qualitative analytical workflows, benefiting both research and industrial applications.
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