X-press Tag Peptide is a tag peptide used for protein purification. X-press Tag is also an N-terminal leader peptide; this N-terminal peptide contains a polyhistidine sequence, the Xpress epitope (part of bacteriophage T7 gene 10 protein) and an enterokinase cleavage site. Anti-Xpress antibodies recognize the Xpress epitope sequence found in this leader peptide.
CAT No: R1756
X-press Tag Peptide is a synthetic peptide epitope widely recognized in molecular biology and biochemistry for its role as an affinity tag in recombinant protein expression systems. Structurally, it consists of a short, well-defined amino acid sequence engineered to be minimally immunogenic while providing a unique antigenic determinant. Its compact design allows for straightforward genetic fusion to target proteins, facilitating downstream detection and purification without significantly altering protein conformation or function. The X-press Tag Peptide has become a staple tool in protein engineering, offering researchers a versatile approach for tracking, isolating, and characterizing recombinant proteins in diverse cellular and biochemical contexts.
Affinity purification: In recombinant protein production, the X-press tag serves as a highly specific handle for affinity chromatography. When fused to a protein of interest, it enables efficient capture and elution using tag-specific antibodies or resins, streamlining the purification process. This application is particularly valuable for isolating proteins from complex lysates, reducing background noise, and enhancing yield and purity for subsequent analytical or functional assays. The tag's small size minimizes the risk of interfering with the protein's native structure or activity during purification workflows.
Immunodetection: The unique epitope sequence of the X-press tag allows for precise immunodetection in Western blot, ELISA, and immunofluorescence assays. Researchers can use commercially available anti-X-press tag antibodies to selectively visualize tagged proteins in cell lysates, tissue extracts, or subcellular fractions. This facilitates qualitative and semi-quantitative analysis of protein expression, localization, and processing, supporting studies of gene regulation, protein trafficking, and post-translational modifications in both prokaryotic and eukaryotic systems.
Protein-protein interaction studies: Utilizing the X-press tag as a molecular probe, investigators can examine protein-protein interactions through co-immunoprecipitation or pull-down assays. The tag enables selective isolation of the bait protein along with its interacting partners, allowing for the identification and characterization of protein complexes. Its high specificity and compatibility with various detection platforms make it an effective tool for dissecting signaling pathways, mapping interaction networks, and validating candidate binding partners in functional genomics research.
Functional protein characterization: By facilitating the straightforward isolation and detection of recombinant proteins, the X-press tag supports a range of downstream biochemical analyses. Researchers can efficiently obtain pure, tagged proteins for enzymatic assays, structural studies, or binding experiments, enabling detailed investigation of protein function, stability, and dynamics. The tag's minimal impact on protein behavior ensures that functional assessments reflect the native properties of the target molecule.
Quality control and process monitoring: During recombinant protein production, the X-press tag provides a reliable marker for monitoring expression levels and verifying the integrity of fusion constructs. Analytical methods such as SDS-PAGE, mass spectrometry, or immunoassays can leverage the tag to assess product consistency, detect degradation, and optimize expression conditions. This application is essential for laboratory-scale research as well as process development in biotechnology and biomanufacturing, where reproducibility and product quality are critical concerns.
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