tatM2NX fuses a TAT-derived transduction sequence with an M2NX functional domain to enable intracellular targeting. The cationic TAT region enhances uptake, while the appended motif engages protein partners. Researchers investigate its delivery efficiency and structural conformation. Applications include CPP engineering, intracellular signaling studies, and targeted-peptide transport.
CAT No: R2398
CAS No:2126166-03-6
Synonyms/Alias:tatM2NX;tat-M2NX;GTPL11080;DA-78210;2126166-03-6;
tatM2NX is a synthetic peptide composed of the HIV-1 TAT protein transduction domain fused to a sequence derived from the influenza A virus M2 protein. This chimeric peptide is engineered to facilitate cellular uptake and intracellular delivery of the M2-derived domain, leveraging the membrane-translocating properties of the TAT motif. Owing to its unique structure, tatM2NX has become a valuable tool in molecular and cellular biology research, particularly in studies aimed at dissecting membrane protein functions, protein-protein interactions, and intracellular signaling pathways. Its bifunctional design enables researchers to explore the biological activity of the M2 segment within living cells, while ensuring efficient transport across cellular membranes.
Cellular delivery studies: The TAT domain in tatM2NX enables efficient translocation of the peptide across cellular membranes, making it a robust model for investigating mechanisms of peptide-mediated delivery. Researchers utilize this peptide to study the kinetics and pathways of cell penetration, endosomal escape, and cytoplasmic localization, providing insights that inform the design of more effective delivery vectors for macromolecules or bioactive agents.
Membrane protein research: By incorporating the M2-derived sequence, tatM2NX serves as a functional mimic for segments of the influenza A M2 ion channel. It is employed in studies examining the structural and functional aspects of viral membrane proteins, including investigations into proton transport, oligomerization, and membrane association. Such research supports a deeper understanding of viral entry, replication, and host-cell interactions at the molecular level.
Protein-protein interaction assays: The chimeric nature of tatM2NX allows it to be used as a probe for mapping interactions between viral protein domains and host cellular factors. In vitro and cell-based assays leverage this peptide to identify binding partners, characterize interaction affinities, and elucidate the role of the M2 domain in modulating host-pathogen dynamics. This application is particularly relevant for virology and antiviral drug discovery efforts.
Intracellular signaling investigations: The ability of tatM2NX to access the cytosolic compartment makes it a useful tool for modulating and monitoring intracellular signaling cascades. Researchers employ the peptide to perturb specific pathways associated with viral infection, stress responses, or membrane dynamics, enabling functional studies that would be challenging with non-permeant peptides or proteins.
Peptide engineering and functional studies: The modular architecture of tatM2NX provides a versatile scaffold for the development and evaluation of novel cell-penetrating peptides and chimeric constructs. Its application extends to comparative studies assessing the efficiency of different transduction domains, the stability of peptide conjugates, and the intracellular fate of engineered biomolecules. These investigations contribute to advancing peptide-based research tools and delivery technologies in the broader field of chemical biology.
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