T7 Tag Peptide

T7 Tag Peptide is a 11 amino acid peptide derived from the T7 major capsid protein, and serves as a tag in many expression vectors that is based on the very efficient T7 RNA polymerase expression system.

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

CAT No: R1702

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M.F/Formula
C₄₁H₇₁N₁₃O₁₆S₃
M.W/Mr.
1098.27
Sequence
One Letter Code: MASMTGGQQMG
three Letter Code: Met-Ala-Ser-Met-Thr-Gly-Gly-Gln-Gln-Met-Gly

T7 Tag Peptide is a synthetic peptide epitope derived from the leader sequence of the T7 bacteriophage gene 10 protein. Characterized by its short, well-defined amino acid sequence, it is widely recognized in molecular biology and protein engineering for its utility as an affinity tag. Its compact structure, immunogenic properties, and compatibility with various detection and purification systems make it a valuable tool for researchers working with recombinant proteins. The T7 Tag Peptide's utility lies in its ability to facilitate the study, isolation, and characterization of fusion proteins across a range of experimental platforms.

Protein Expression Analysis: As a fusion tag, the T7 peptide is frequently employed to monitor recombinant protein expression in prokaryotic and eukaryotic systems. When genetically fused to a target protein, the tag enables sensitive detection using anti-T7 antibodies in techniques such as Western blotting, ELISA, and immunofluorescence. This approach allows researchers to verify expression, assess protein stability, and optimize production conditions without the need for target-specific antibodies, thereby streamlining the analysis of novel or poorly characterized proteins.

Affinity Purification: The T7 tag serves as a highly effective affinity handle for the purification of recombinant proteins. Immobilized anti-T7 antibody resins or other specific capture reagents can selectively bind tagged proteins from complex lysates, facilitating rapid and efficient isolation under native or denaturing conditions. This affinity-based strategy significantly enhances the purity and yield of target proteins, proving indispensable for downstream biochemical or structural studies.

Protein-Protein Interaction Studies: The defined epitope of the T7 tag allows it to be used as a molecular probe in co-immunoprecipitation and pull-down assays. By enabling the selective capture of tagged proteins and their interacting partners, the tag supports the elucidation of protein complexes and interaction networks. This capability is particularly valuable in mapping signaling pathways, validating candidate interactors, and dissecting molecular mechanisms within cellular systems.

Immunodetection and Localization: The strong immunogenicity and specificity of the T7 epitope facilitate its use in immunodetection applications. Researchers can employ fluorescently labeled anti-T7 antibodies to visualize the subcellular localization of fusion proteins in fixed or live cells. This approach is instrumental in tracking protein trafficking, monitoring compartmentalization, and investigating dynamic cellular processes, especially when endogenous antibodies are unavailable or unsuitable.

Peptide-Based Assay Development: The synthetic nature and well-characterized sequence of the T7 tag make it an ideal standard or control in assay development. It can be used to calibrate immunoassays, validate antibody specificity, or benchmark detection sensitivity. In addition, the peptide itself serves as a model substrate in enzymatic or binding studies, offering a reliable platform for optimizing assay conditions and ensuring experimental reproducibility.

Collectively, these application directions underscore the T7 Tag Peptide's versatility and technical value in modern protein science. Its widespread adoption in molecular cloning, protein purification, and analytical workflows reflects its robust performance and adaptability to diverse research needs. By integrating the T7 tag into experimental designs, laboratories can achieve greater efficiency, reproducibility, and clarity in the study of recombinant proteins and their functional roles.

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