TNF-α (10-36), human is a peptide of human TNF-α.
TNF-α (10-36), human is a synthetic peptide fragment derived from the human tumor necrosis factor alpha (TNF-α) protein, encompassing amino acids 10 through 36 of the native sequence. As a bioactive segment of TNF-α, this peptide represents a functionally relevant region involved in modulating cellular signaling pathways associated with inflammation, apoptosis, and immune regulation. Its defined sequence and structural fidelity make it a valuable tool for dissecting the mechanistic roles of TNF-α in various biological processes. Researchers utilize this peptide to investigate structure-function relationships, receptor interactions, and downstream signaling events, contributing to a deeper understanding of cytokine biology in both normal and pathological states.
Signal transduction studies: TNF-α (10-36), human is frequently employed in research focused on elucidating the molecular mechanisms underlying TNF-α-mediated signal transduction. By providing a specific, well-characterized portion of the full-length cytokine, the peptide allows investigators to analyze how discrete regions of TNF-α interact with cellular receptors such as TNFR1 and TNFR2. This targeted approach supports the identification of domain-specific effects on signaling cascades, including the activation of NF-κB, MAPK, and apoptotic pathways, thereby advancing knowledge of cytokine-driven cellular responses.
Receptor binding analysis: The peptide serves as a critical reagent in studies aimed at mapping the binding domains of TNF-α to its cell surface receptors. Researchers use the 10-36 fragment to probe the structural determinants of ligand-receptor affinity and specificity, employing techniques such as surface plasmon resonance, competitive binding assays, and molecular docking. Insights gained from these experiments inform the design of receptor antagonists or mimetics and contribute to the rational development of molecules that modulate TNF-α signaling for research purposes.
Peptide-based inhibitor screening: As a representative functional motif within the TNF-α molecule, this peptide is utilized in high-throughput screening protocols to identify small molecules, peptides, or antibodies capable of disrupting critical protein-protein interactions. By serving as a target or competitor in binding assays, the fragment enables the discovery and characterization of inhibitors that selectively interfere with TNF-α activity. These findings are instrumental in advancing chemical biology studies and the exploration of cytokine modulation strategies in vitro.
Epitope mapping and antibody validation: Investigators often rely on the TNF-α (10-36) fragment for detailed epitope mapping and validation of antibodies directed against TNF-α. The defined sequence facilitates the assessment of antibody specificity and affinity, supporting the development and quality control of immunological reagents. Such applications are essential for generating reliable tools for immunoassays, Western blotting, and immunoprecipitation, ensuring robust detection and quantification of TNF-α in diverse experimental systems.
Peptide structural analysis: The fragment is also used as a model system for biophysical and structural studies, including nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), and crystallography. These approaches enable researchers to characterize the secondary structure, conformational dynamics, and folding properties of the TNF-α 10-36 region in isolation or in complex with binding partners. Insights from structural analyses inform the broader understanding of TNF-α's bioactivity, stability, and interaction interfaces, supporting rational design in peptide engineering and cytokine research.
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