Hemokinin 1 (mouse) is a selective agonist of neurokinin-1 receptor, with Ki of 0.175 nM and 560 nM for human NK1 receptor and human NK2 receptor, respectively.
Hemokinin 1 mouse is a biologically active peptide belonging to the tachykinin family, characterized by its conserved C-terminal sequence and its origin in murine species. As a neuropeptide, it has garnered significant interest for its role in modulating cellular signaling pathways, particularly those involving G protein-coupled receptors. The distinctive sequence and expression profile of this peptide make it a valuable tool in neurobiology, immunology, and peptide signaling research. Its capacity to interact with neurokinin receptors and influence various physiological processes underscores its importance as a research reagent for dissecting peptide-mediated communication in mammalian systems.
Receptor binding studies: Hemokinin 1 serves as a robust ligand in the study of tachykinin receptor pharmacology, especially regarding neurokinin-1 (NK1) and related receptor subtypes. Researchers frequently employ the peptide to characterize receptor affinity, selectivity, and downstream signaling mechanisms in both native and recombinant systems. By using it as a reference compound or experimental probe, scientists can delineate the structure-activity relationships that govern receptor-ligand interactions, facilitating the discovery and validation of novel receptor modulators or antagonists.
Neuroimmune interaction research: The peptide's ability to modulate immune cell function has positioned it as a key tool in exploring neuroimmune crosstalk. Investigations into its effects on cytokine release, immune cell migration, and inflammatory signaling have provided valuable insights into how neuropeptides influence immune responses in murine models. Its application in such studies enables the dissection of signaling cascades and cellular behaviors relevant to inflammation, host defense, and tissue homeostasis.
Peptide signaling pathway analysis: Hemokinin 1 is frequently utilized to probe intracellular signaling events triggered by tachykinin engagement. Researchers use it to stimulate cells in vitro, monitoring downstream events such as calcium mobilization, MAP kinase activation, or gene expression changes. These experiments help elucidate the mechanisms by which tachykinins regulate cellular activity, supporting efforts to map complex peptide signaling networks in the nervous and immune systems.
In vivo functional studies: Experimental use of this peptide in murine models allows for the assessment of its physiological roles within an intact organism. Investigators employ it to examine behavioral, nociceptive, or cardiovascular responses, providing a means to link molecular interactions with systemic outcomes. Such studies are instrumental in clarifying the functional significance of tachykinins in mammalian biology and in validating hypotheses generated from in vitro experiments.
Peptide structure-function investigations: The defined sequence and murine specificity of Hemokinin 1 make it a useful substrate for structure-activity relationship studies. By introducing targeted modifications or analogs, researchers can assess the contribution of specific residues to receptor binding, biological activity, or proteolytic stability. These efforts support the rational design of peptide-based probes and contribute to a deeper understanding of tachykinin biochemistry, informing both basic research and the development of specialized reagents for advanced studies.
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