Orexin B, human (TFA) is an endogenous agonist at Orexin receptor with Kis of 420 and 36 nM for OX1 and OX2, respectively.
Orexin B, human TFA is a synthetic peptide corresponding to the human sequence of Orexin B, also known as hypocretin-2, supplied as the trifluoroacetate (TFA) salt. As a neuropeptide, it plays a central role in the regulation of arousal, wakefulness, and appetite by binding to orexin receptors in the central nervous system. The peptide's well-defined sequence and high degree of specificity make it a valuable reagent for investigating the physiological and molecular mechanisms underlying orexinergic signaling. Its utility extends across neurobiology, pharmacology, and peptide-receptor interaction studies, supporting both foundational research and the development of new experimental models.
Receptor binding studies: Researchers commonly employ Orexin B peptides to elucidate the binding properties and pharmacodynamics of orexin receptors, particularly OX2R (orexin receptor type 2). By using this peptide in in vitro binding assays or cell-based receptor activation experiments, scientists can characterize ligand-receptor interactions, assess receptor selectivity, and quantify downstream signaling events. Such studies are fundamental for mapping the structural determinants of receptor activation and for screening the effects of novel small molecules or peptide analogs on orexinergic pathways.
Neuropharmacology research: The human Orexin B sequence serves as a critical tool in neuropharmacological investigations aimed at understanding the modulation of sleep-wake cycles, feeding behavior, and reward processing. Application of the peptide to cultured neurons, brain slices, or animal models enables researchers to probe the functional consequences of orexinergic activation, dissect neuronal circuitry, and explore the peptide's influence on neurotransmitter release. Its use facilitates the study of neuropeptide-driven physiological processes and supports the identification of novel pharmacological targets within the central nervous system.
Peptide structure-activity relationship (SAR) analysis: Orexin B, human TFA is frequently utilized in SAR studies to determine how specific amino acid residues contribute to receptor binding affinity and agonist potency. By systematically modifying the peptide sequence and comparing the bioactivity of resulting analogs, researchers can identify key structural features responsible for biological function. These insights are instrumental in guiding the rational design of next-generation orexin receptor modulators and optimizing peptide-based probes for mechanistic studies.
Signal transduction pathway elucidation: Employing Orexin B in cellular assays allows for detailed examination of intracellular signaling cascades triggered by orexin receptor activation. Researchers can monitor events such as G-protein coupling, calcium mobilization, and downstream phosphorylation processes to build comprehensive models of orexin-mediated signal transduction. Such mechanistic insights are essential for understanding how orexinergic signaling integrates with other neurochemical systems and regulates complex physiological states.
Peptide-based assay development: The well-characterized nature of this synthetic peptide makes it an ideal standard or positive control in the development and validation of biochemical assays targeting the orexin system. Its use in receptor binding assays, enzyme-linked immunosorbent assays (ELISAs), or high-throughput screening platforms ensures reproducibility and accuracy in quantifying orexinergic activity. This supports the broader research community in establishing robust methodologies for investigating neuropeptide signaling and evaluating the efficacy of experimental compounds that modulate orexin pathways.
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