TNF-α (46-65), human is a peptide of TNF-α.
CAT No: R1724
CAS No:144796-72-5
Synonyms/Alias:TNF-alpha (46-65), human;144796-72-5;H-Asn-Gln-Leu-Val-Val-Pro-Ser-Glu-Gly-Leu-Tyr-Leu-Ile-Tyr-Ser-Gln-Val-Leu-Phe-Lys-OH;
TNF-α (46-65), human is a synthetic peptide fragment derived from the central region of human tumor necrosis factor alpha (TNF-α), a key cytokine involved in inflammatory and immune signaling pathways. This peptide encompasses amino acids 46 to 65 of the full TNF-α protein and is widely utilized in investigating the structure-function relationships of cytokines, receptor interactions, and downstream signaling mechanisms. Its defined sequence enables researchers to dissect specific biological activities attributed to this segment of TNF-α, facilitating targeted studies in immunology, cell biology, and peptide-based assay development. The availability of this fragment supports advanced exploration into the molecular determinants of TNF-α-mediated effects, providing a valuable tool for both fundamental and applied research in cytokine biology.
Peptide structure-function analysis: TNF-α (46-65), human serves as a critical reagent for elucidating the structural motifs within TNF-α that are responsible for receptor binding and activation of intracellular signaling cascades. By isolating and studying this specific segment, researchers can identify the minimal sequence elements required for biological activity, contributing to a deeper understanding of cytokine-receptor specificity and the molecular basis of TNF-α function. Such insights are essential for mapping the active sites and for designing peptide analogs or antagonists with modulated activity.
Receptor interaction studies: The defined sequence of this peptide fragment makes it highly suitable for in vitro assays that probe the interaction between TNF-α and its cellular receptors, such as TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Utilizing this fragment allows for the quantitative assessment of binding affinities, competitive inhibition, or receptor activation in cell-based or biochemical systems. These studies are instrumental in delineating the contribution of the central region of TNF-α to receptor engagement and downstream signaling events.
Peptide-based assay development: Due to its well-characterized sequence and biological relevance, TNF-α (46-65), human is frequently employed in the development and optimization of immunoassays, such as enzyme-linked immunosorbent assays (ELISAs) or surface plasmon resonance (SPR) platforms. Incorporation of this fragment as a standard, control, or capture reagent enhances assay specificity and sensitivity when detecting TNF-α or related analytes. Its use streamlines the validation of assay performance in both academic and industrial research settings.
Immunological modeling: The peptide fragment provides a controlled system for modeling immune responses in vitro, particularly in studies exploring cytokine signaling, cross-talk between immune cells, or the development of peptide-based immunomodulators. By applying this defined segment, investigators can dissect the immunological consequences of partial TNF-α signaling, facilitating the evaluation of novel modulators or the mechanistic study of inflammatory pathways under defined experimental conditions.
Peptide synthesis and modification research: As a representative fragment of a biologically significant cytokine, TNF-α (46-65), human is also valuable in synthetic peptide chemistry. It offers a template for studying solid-phase synthesis efficiency, sequence-specific modifications, or the incorporation of non-natural amino acids. Such applications are vital for advancing peptide engineering, enhancing stability, or tailoring bioactivity, supporting the broader field of therapeutic peptide design and functional biomolecule development.
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