Neurokinin A (4-10) TFA is a tachykinin NK2 receptor agonist.
CAT No: R1533
Neurokinin A(4-10) TFA is a synthetic peptide fragment corresponding to residues 4 through 10 of the endogenous neuropeptide Neurokinin A, supplied as its trifluoroacetate salt. As a member of the tachykinin peptide family, this compound is of significant interest in neurobiology and pharmacology due to its involvement in modulating neurotransmission, smooth muscle activity, and inflammatory processes. The truncated sequence retains critical bioactive motifs, making it a valuable research tool for dissecting the functional domains responsible for receptor interaction and downstream signaling. Its defined structure and biological relevance position it as a key reagent for studies exploring the mechanisms of neuropeptide action and receptor specificity.
Receptor binding studies: The peptide fragment is widely employed in investigations of neurokinin receptor subtype selectivity and binding affinity. By isolating the active core region of Neurokinin A, researchers can probe the structural determinants required for interaction with NK2 and other tachykinin receptors. Utilizing this sequence variant enables the elucidation of ligand-receptor recognition mechanisms, which is essential for mapping pharmacophores and guiding the design of selective agonists or antagonists targeting neurokinin-mediated pathways.
Signal transduction research: In cellular and molecular assays, this peptide serves as a tool to activate or modulate signaling cascades downstream of tachykinin receptors. Its application allows for the assessment of intracellular events such as calcium mobilization, second messenger production, and kinase activation following receptor engagement. These studies are instrumental in characterizing the dynamics of neuropeptide-induced responses and in differentiating the contributions of specific peptide fragments to overall biological activity.
Structure-activity relationship (SAR) analysis: The defined sequence of this peptide fragment supports systematic SAR investigations aimed at identifying key residues responsible for bioactivity. By comparing the functional properties of Neurokinin A(4-10) with those of full-length and other truncated analogs, researchers can delineate the minimal structural requirements for receptor activation. Such analyses inform the rational design of novel peptide mimetics with improved selectivity or stability for research and development purposes.
Peptide synthesis and analytical method development: As a well-characterized peptide standard, Neurokinin A(4-10) TFA is frequently utilized in the validation of peptide synthesis protocols and analytical techniques, including HPLC and mass spectrometry. Its defined sequence and physicochemical properties make it suitable as a reference material for method calibration, peptide mapping, and quality control in peptide research laboratories. The use of such standards is critical for ensuring reproducibility and accuracy in peptide-based experimental workflows.
Pharmacological screening: The fragment also finds application in in vitro pharmacological assays designed to evaluate the efficacy and potency of novel compounds targeting tachykinin pathways. By serving as a reference agonist or modulator, it facilitates the benchmarking of experimental compounds and helps establish dose-response relationships in receptor activation studies. This approach is particularly valuable for high-throughput screening platforms seeking to identify new modulators of neuropeptide signaling relevant to neuroscience and inflammation research.
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. TMEM16F and dynamins control expansive plasma membrane reservoirs
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