DNA ligase 3
CAT No: ta-172
Synonyms/Alias:DNA ligase 3 isoform alpha precursor (790-806)
DNA ligase 3 isoform alpha precursor (790-806) is a synthetic peptide fragment corresponding to a specific region of the DNA ligase 3 alpha isoform, a key enzyme involved in the repair and maintenance of genomic DNA integrity. This peptide represents amino acids 790 to 806 of the precursor protein, a region that may be critical for protein-protein interactions, regulatory modifications, or functional activity within the ligase complex. The study of such defined peptide sequences provides valuable insights into the structural and biochemical properties of DNA ligases, which play central roles in DNA strand joining during base excision repair and other DNA repair pathways. Researchers utilize this peptide fragment to dissect molecular mechanisms underlying DNA repair, to map interaction domains, and to develop targeted assays for investigating protein function in cellular and biochemical contexts.
Protein-Protein Interaction Studies: The synthetic peptide corresponding to the 790-806 region of DNA ligase 3 alpha is frequently employed to investigate specific binding sites and interaction motifs within the ligase complex. By using this fragment in pull-down assays, surface plasmon resonance, or peptide array formats, researchers can systematically identify and characterize partners that interact with this region, including repair factors, scaffold proteins, or regulatory elements. Such studies are essential for elucidating the molecular architecture of DNA repair assemblies and for mapping domains responsible for substrate recognition or regulatory control.
Epitope Mapping and Antibody Production: Due to its defined sequence and structural relevance, the 790-806 peptide serves as a valuable tool for epitope mapping and the generation of sequence-specific antibodies. Immunization with this peptide allows for the production of polyclonal or monoclonal antibodies that recognize the corresponding region in the full-length protein, facilitating applications such as western blotting, immunoprecipitation, and immunofluorescence. These antibodies are crucial for probing the expression, localization, and post-translational modification status of DNA ligase 3 alpha in various biological samples.
Peptide-Based Enzyme Activity Assays: The defined peptide fragment can be incorporated into in vitro enzyme activity assays to study the substrate specificity or catalytic mechanisms of DNA ligase 3 alpha and its interacting partners. By serving as a competitive inhibitor, substrate mimic, or binding probe, the peptide enables quantitative assessment of enzyme kinetics, inhibition profiles, or modification states. Such assays contribute to a deeper understanding of DNA ligase function and regulation, and support the development of new research tools for DNA repair studies.
Structural and Biophysical Analysis: Researchers utilize the 790-806 peptide as a model system for structural and biophysical investigations, including nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), or crystallography. These approaches help reveal secondary structure tendencies, conformational dynamics, and potential post-translational modification sites within this region of DNA ligase 3 alpha. Insights gained from such studies inform the design of mutational analyses, synthetic analogs, or targeted inhibitors for downstream applications in DNA repair research.
Peptide-Protein Interaction Inhibitor Screening: The peptide fragment is also applied in high-throughput screening assays aimed at identifying small molecules or biologics that disrupt critical interactions involving the 790-806 region. By serving as a competitive binding probe, it enables the discovery and characterization of compounds that may modulate DNA ligase 3 alpha function, providing valuable leads for chemical biology studies or the development of novel research tools. These applications support the broader goal of dissecting DNA repair pathways and understanding the molecular basis of genome stability.
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