ARTC1 is a peptide modeled on ADP-ribosyltransferase activity domains, highlighting residues influencing substrate recognition. The motif supports work on post-translational modification and enzymatic regulation. Researchers use it to probe catalytic determinants and binding interfaces. Its structural elements enable mechanistic characterization.
CAT No: ta-185
ARTC1, or ADP-ribosyltransferase C1, is an enzyme that catalyzes the transfer of ADP-ribose moieties from NAD+ to specific target proteins, thereby modulating their function and activity. As a member of the ecto-ADP-ribosyltransferase family, ARTC1 plays a significant role in post-translational modification processes that regulate cellular signaling, protein-protein interactions, and immune responses. Its unique enzymatic activity and substrate specificity have positioned it as an important molecular tool for studying ADP-ribosylation mechanisms, cell surface protein regulation, and related biochemical pathways in mammalian systems. The availability of recombinant ARTC1 has enabled researchers to investigate its biological functions, substrate preferences, and potential roles in various physiological and pathophysiological contexts.
Enzymatic mechanism studies: ARTC1 serves as a valuable reagent for dissecting the biochemical mechanisms underlying ADP-ribosylation. Researchers utilize purified enzyme preparations to characterize the kinetics, substrate specificity, and catalytic properties of ecto-ADP-ribosyltransferases in vitro. These studies contribute to a deeper understanding of how ADP-ribose modification influences protein structure and function, as well as the broader regulatory networks governing cell signaling and communication.
Cell surface protein modification: The enzyme is frequently employed to investigate the ADP-ribosylation of cell surface proteins, which can alter receptor activity, modulate signal transduction, and impact intercellular communication. By applying ARTC1 to cultured cells or isolated membrane preparations, scientists can delineate which surface proteins are susceptible to modification, assess the functional consequences of these modifications, and explore the dynamic interplay between extracellular enzymes and membrane-associated targets.
Immunological research: Given its expression on immune cells, ARTC1 is instrumental in studies focused on immune regulation and signaling. Experimental systems employing this enzyme facilitate the analysis of ADP-ribosylation-dependent modulation of immune cell receptors, such as those involved in T cell activation or macrophage function. These investigations shed light on the molecular mechanisms by which ADP-ribosyltransferases influence immune responses and may reveal new regulatory checkpoints within the immune system.
Protein-protein interaction mapping: The ability of ARTC1 to selectively modify specific protein substrates allows researchers to probe protein-protein interactions and complex formation. By labeling target proteins with ADP-ribose moieties, it becomes possible to track interaction partners, map binding domains, and elucidate the structural basis of protein assemblies. This application is particularly valuable in the context of identifying novel components of cell surface signaling complexes or characterizing the assembly of multiprotein networks.
Analytical assay development: ARTC1 is also utilized in the development of biochemical assays designed to monitor ADP-ribosyltransferase activity, screen for modulators or inhibitors, and quantify ADP-ribosylation events. These assays provide sensitive and specific platforms for high-throughput screening, mechanistic studies, and the evaluation of small molecules that impact enzyme function. The use of recombinant enzyme in such analytical systems enhances reproducibility and enables the detailed characterization of enzymatic activity under controlled experimental conditions.
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