High affinity ClC-2 blocker (apparent KD ~ 50 pM) that slows ClC-2 activation and inhibits slow-gating, but does not inhibit open ClC-2 channels.
CAT No: R1060
CAS No:194665-85-5
Synonyms/Alias:GaTx2;194665-85-5;AKOS024458412;DA-63710;S-194665-85-5;
GaTx2, also known as Grammotoxin SIA, is a peptide toxin derived from the venom of the tarantula Grammostola spatulata. As a member of the inhibitory cystine knot (ICK) peptide family, GaTx2 is characterized by its unique disulfide-rich structure, which imparts exceptional stability and specificity for voltage-gated ion channels. Its high affinity and selectivity for certain subtypes of voltage-gated calcium and potassium channels have made it a valuable molecular probe in neurophysiological research and ion channel pharmacology. The peptide's ability to modulate channel gating dynamics provides researchers with a precise tool for dissecting the functional roles of these channels in excitable tissues.
Electrophysiological studies: GaTx2 is widely utilized as a selective inhibitor in electrophysiological experiments focused on voltage-gated ion channels, particularly P/Q-type (Cav2.1) calcium channels and certain potassium channels. Its application enables detailed characterization of channel gating, ion selectivity, and pharmacological modulation, facilitating the identification of channel subtypes and their physiological contributions in neuronal and muscle cell preparations. By applying this peptide in patch-clamp assays or voltage-clamp recordings, researchers can elucidate the mechanisms underlying synaptic transmission, neuronal excitability, and signal propagation.
Ion channel pharmacology: The peptide serves as an essential reference compound in the field of ion channel drug discovery and pharmacological profiling. Its high specificity allows for the benchmarking of novel channel modulators and the validation of screening assays targeting calcium and potassium channels. The use of GaTx2 in these contexts aids in distinguishing direct channel interactions from off-target effects, thereby improving the reliability of lead compound identification and mechanistic studies in pharmaceutical research.
Structure-function analysis: GaTx2 is frequently employed in structural biology and biochemistry to investigate the molecular determinants of peptide-channel interactions. Its well-defined structure, coupled with potent biological activity, makes it an ideal template for mutagenesis studies and computational modeling. Researchers use it to map channel binding sites, analyze the contributions of specific amino acid residues to affinity and selectivity, and design engineered peptides with tailored properties for research or biotechnological applications.
Neuroscience research: The selective modulation of voltage-gated channels by GaTx2 provides a powerful approach to probing neuronal signaling pathways and synaptic physiology. By selectively inhibiting specific channel subtypes, scientists can dissect the roles of these channels in neurotransmitter release, action potential shaping, and network excitability. This targeted approach is invaluable for understanding the molecular basis of neurological processes and for developing experimental models of channelopathies.
Peptide engineering: Owing to its robust cystine knot framework and well-characterized channel interactions, GaTx2 is often used as a scaffold in peptide engineering efforts. Researchers leverage its stability and binding specificity to design novel peptide analogs with improved pharmacokinetic properties or altered channel selectivity. Such engineered peptides are valuable for expanding the toolkit available for ion channel research, developing new molecular probes, or exploring innovative biotechnological applications where precise channel modulation is required.
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