3X HA Tag

3X HA Tag contains three tandem HA epitopes used for affinity capture and immunodetection. Repeated aromatic and charged residues enhance antibody recognition. Researchers employ it in protein-labeling, pull-downs, and imaging assays. Applications include tagged-protein purification, detection optimization, and epitope mapping.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R2841

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M.F/Formula
C205H272N38O67S
M.W/Mr.
4372.9
Sequence
One Letter Code:MEYPYDVPDYAAEYPYDVPDYAAEYPYDVPDYAAKLE
Three Letter Code:H-Met-Glu-Tyr-Pro-Tyr-Asp-Val-Pro-Asp-Tyr-Ala-Ala-Glu-Tyr-Pro-Tyr-Asp-Val-Pro-Asp-Tyr-Ala-Ala-Glu-Tyr-Pro-Tyr-Asp-Val-Pro-Asp-Tyr-Ala-Ala-Lys-Leu-Glu-OH

3X HA Tag is a synthetic peptide epitope composed of three tandem repeats of the influenza hemagglutinin (HA) tag sequence, widely utilized in molecular biology and protein research. As a peptide reagent, it serves as a highly effective fusion tag for the detection, purification, and characterization of recombinant proteins. The trimeric configuration of the HA epitope enhances antibody binding affinity and detection sensitivity, making it especially valuable in applications where robust and specific recognition is required. Its compact size, minimal interference with protein function, and compatibility with a broad range of host systems have established it as a standard tool for protein engineering, cell biology, and biochemical analysis.

Epitope Tagging: In recombinant protein research, the 3X HA Tag is extensively used as an epitope tag to facilitate the identification and localization of fusion proteins. By genetically fusing the tag to a protein of interest, researchers can leverage commercially available monoclonal antibodies for highly specific detection in techniques such as Western blotting, immunofluorescence, and immunoprecipitation. The triple-repeat structure significantly increases signal intensity, allowing for enhanced visualization of low-abundance proteins or proteins expressed in challenging systems.

Affinity Purification: The 3X HA Tag enables efficient affinity purification of tagged proteins from complex biological samples. Utilizing anti-HA affinity matrices, researchers can selectively isolate fusion proteins under mild, non-denaturing conditions, preserving native structure and activity. This approach streamlines downstream applications such as enzymatic assays, interaction studies, and structural analysis, providing a robust and reproducible method for obtaining high-quality protein preparations for further characterization.

Protein-Protein Interaction Studies: The tag's strong and specific antibody recognition makes it an ideal tool for co-immunoprecipitation and pull-down assays aimed at mapping protein-protein interactions. By tagging one interaction partner with the 3X HA epitope, complexes can be selectively captured and analyzed, enabling the elucidation of molecular networks and signaling pathways. The increased avidity provided by the triple tag enhances recovery and detection of transient or weakly interacting partners, supporting detailed mechanistic studies.

Cellular Localization Analysis: The 3X HA Tag is frequently employed in cell biology to monitor the subcellular distribution of fusion proteins. Through immunocytochemistry or live-cell imaging using fluorescently labeled antibodies, researchers can track the dynamic localization, trafficking, and compartmentalization of proteins within cells. The tag's small size minimizes perturbation of native protein function, ensuring accurate representation of physiological behavior while providing a reliable handle for visualization.

Protein Quantification: Quantitative analysis of protein expression levels is another important application of the 3X HA Tag. The enhanced signal generated by the triple epitope allows for sensitive and reproducible quantitation in assays such as ELISA, Western blot, or flow cytometry. This capability is particularly advantageous in high-throughput screening, comparative expression studies, and experimental validation of gene constructs, where precise and consistent measurement of protein abundance is critical for data interpretation and experimental success.

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