Description: The peptide sequence EQKLISEEDL corresponds to the c-Myc tag , a widely utilized 10-amino-acid epitope derived from the human c-Myc proto-oncogene. This tag is extensively employed in molecular biology for the detection, purification, and analysis of recombinant proteins. Functional Overview Origin : The c-Myc tag is derived from amino acid residues 410–419 of the human c-Myc protein, a nuclear transcription factor involved in cell cycle regulation and apoptosis. Sequence : EQKLISEEDL Molecular Weight : Approximately 1.2 kDa. Applications : Protein Detection : The c-Myc tag is recognized by specific monoclonal antibodies, such as the 9E10 clone, facilitating detection through techniques like Western blotting, immunofluorescence, and immunoprecipitation. Protein Purification : c-Myc-tagged proteins can be purified using affinity chromatography methods that exploit the high-affinity interaction between the tag and anti-c-Myc antibodies. Protein Localization and Interaction Studies : The tag aids in studying protein localization within cells and interactions with other proteins. Versatility : Due to its small size, the c-Myc tag can be fused to either the N-terminus or C-terminus of target proteins without significantly altering their function or localization. Research and Development The c-Myc tag has been instrumental in various research applications: Epitope Tagging : It serves as a model epitope tag in studies aiming to understand protein expression and function. Antibody Production : Synthetic peptides corresponding to the c-Myc tag are used to generate monoclonal and polyclonal antibodies, which are critical tools in protein research. Biotinylation : Biotinylated versions of the c-Myc tag are available, allowing for enhanced detection and purification using streptavidin-based systems. Considerations and Limitations Elution Conditions : While the c-Myc tag can be used for protein purification, elution often requires low pH conditions, which could negatively affect protein functionality. Secretory Pathway Interference : It is not recommended to fuse the c-Myc tag directly behind the signal peptide of a secretory protein, as it can interfere with translocation into the secretory pathway. The EQKLISEEDL sequence, known as the c-Myc tag, is a valuable tool in molecular biology for the detection and purification of recombinant proteins. Its small size and the availability of high-affinity antibodies make it an ideal choice for various protein research applications. | The peptide sequence EQKLISEEDL corresponds to the c-Myc tag, a widely utilized 10-amino-acid epitope derived from the human c-Myc proto-oncogene. This tag is extensively employed in molecular biology for the detection, purification, and analysis of recombinant proteins. Functional Overview -
Origin: The c-Myc tag is derived from amino acid residues 410–419 of the human c-Myc protein, a nuclear transcription factor involved in cell cycle regulation and apoptosis. -
Sequence: EQKLISEEDL -
Molecular Weight: Approximately 1.2 kDa. -
Applications: -
Protein Detection: The c-Myc tag is recognized by specific monoclonal antibodies, such as the 9E10 clone, facilitating detection through techniques like Western blotting, immunofluorescence, and immunoprecipitation. -
Protein Purification: c-Myc-tagged proteins can be purified using affinity chromatography methods that exploit the high-affinity interaction between the tag and anti-c-Myc antibodies. -
Protein Localization and Interaction Studies: The tag aids in studying protein localization within cells and interactions with other proteins. -
Versatility: Due to its small size, the c-Myc tag can be fused to either the N-terminus or C-terminus of target proteins without significantly altering their function or localization. Research and Development The c-Myc tag has been instrumental in various research applications: -
Epitope Tagging: It serves as a model epitope tag in studies aiming to understand protein expression and function. -
Antibody Production: Synthetic peptides corresponding to the c-Myc tag are used to generate monoclonal and polyclonal antibodies, which are critical tools in protein research. -
Biotinylation: Biotinylated versions of the c-Myc tag are available, allowing for enhanced detection and purification using streptavidin-based systems. Considerations and Limitations -
Elution Conditions: While the c-Myc tag can be used for protein purification, elution often requires low pH conditions, which could negatively affect protein functionality. -
Secretory Pathway Interference: It is not recommended to fuse the c-Myc tag directly behind the signal peptide of a secretory protein, as it can interfere with translocation into the secretory pathway. The EQKLISEEDL sequence, known as the c-Myc tag, is a valuable tool in molecular biology for the detection and purification of recombinant proteins. Its small size and the availability of high-affinity antibodies make it an ideal choice for various protein research applications. |
Scientific Background | c-Myc tag EQKLISEEDL is a 10-residue synthetic peptide with the sequence Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu. The sequence contains 1 Asp and 3 Glu residues, contributing anionic character near neutral pH. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
