Effective and selective Cav2.3 (R-type) channel blocker. It inhibits nociceptive c-fibre and aδ-fibre-evoked neuronal responses, and shows antinociceptive effects.
CAT No: R0955
CAS No:203460-30-4
Synonyms/Alias:203460-30-4;H-Gly-DL-Val-DL-Asp-DL-Lys-DL-Ala-Gly-DL-Cys(1)-DL-Arg-DL-Tyr-DL-Met-DL-Phe-Gly-Gly-DL-Cys(2)-DL-Ser-DL-Val-DL-Asn-DL-Asp-DL-Asp-DL-Cys(3)-DL-Cys(1)-DL-Pro-DL-Arg-DL-Leu-Gly-DL-Cys(2)-DL-His-DL-Ser-DL-Leu-DL-Phe-DL-Ser-DL-Tyr-DL-Cys(3)-DL-Ala-DL-Trp-DL-Asp-DL-Leu-DL-xiThr-DL-Phe-DL-Ser-DL-Asp-OH;SNX 482;PCB-4363-S;HB1235;AKOS024457349;C192H274N52O60S7;
SNX 482 is a peptide toxin originally isolated from the venom of the tarantula Hysterocrates gigas, recognized for its potent and selective modulation of voltage-gated calcium channels, particularly Cav2.3 (R-type) channels. As a disulfide-rich peptide, SNX 482 has become a valuable tool in neurophysiological research, enabling the precise interrogation of ion channel function and synaptic transmission. Its unique structural and pharmacological properties have positioned it as an important molecular probe for dissecting the roles of specific calcium channel subtypes in neuronal signaling and excitability. The compound's specificity and reversible binding characteristics allow for nuanced experimental control, making it indispensable for researchers investigating calcium channel pharmacology and neuronal communication.
Ion Channel Characterization: SNX 482 is widely employed in the functional characterization of voltage-gated calcium channels, with a particular focus on distinguishing the contributions of Cav2.3 (R-type) channels from other high-voltage-activated calcium channel subtypes. By selectively inhibiting these channels, the peptide enables detailed electrophysiological studies that elucidate channel kinetics, pharmacological sensitivities, and subunit composition. This application provides critical insights into the molecular diversity of calcium channels, supporting the development of more selective modulators and advancing understanding of channelopathies.
Neurotransmission Research: The peptide's ability to modulate synaptic calcium influx makes it a powerful reagent for investigating the mechanisms underlying neurotransmitter release. In central and peripheral nervous system preparations, SNX 482 facilitates the dissection of presynaptic calcium channel contributions to synaptic vesicle exocytosis and short-term plasticity. Its use helps clarify the specific involvement of R-type channels in neurotransmission, enabling researchers to parse out the functional hierarchy among calcium channel subtypes during neuronal communication.
Neuronal Excitability Studies: SNX 482 serves as an essential tool for probing the role of R-type calcium channels in shaping neuronal excitability and firing patterns. Through precise application in patch-clamp or field potential recordings, the peptide allows researchers to assess how targeted inhibition of Cav2.3 channels alters action potential generation, repetitive firing, and afterhyperpolarization dynamics. These studies contribute to a deeper understanding of the cellular mechanisms governing excitability in diverse neuronal populations and are instrumental in mapping the physiological relevance of specific ion channel subtypes.
Calcium Signaling Pathway Analysis: The compound is frequently utilized to dissect the contributions of distinct calcium channel populations to intracellular calcium signaling cascades. By selectively blocking R-type channels, SNX 482 enables the partitioning of calcium entry sources during processes such as gene transcription, enzyme activation, and synaptic plasticity. This targeted approach aids in elucidating the spatial and temporal dynamics of calcium signals in neurons and other excitable cells, fostering advances in the study of calcium-dependent regulatory mechanisms.
Pharmacological Screening: SNX 482 is incorporated into high-content screening assays and structure-activity relationship studies aimed at identifying novel modulators of voltage-gated calcium channels. Its well-defined specificity and potency make it an ideal reference compound for benchmarking the activity of new small molecules, peptides, or biologics targeting Cav2.3 channels. This application supports the rational design and optimization of next-generation ion channel modulators for basic research and preclinical discovery, enhancing the toolkit available for ion channel drug development and mechanistic studies.
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