Every lot is tried & tested in a relevant biological assay.
- Alomone Labs ω-Agatoxin-IVA inhibits CaV2.1 currents heterologously expressed in Xenopus oocytes.A. Time course of ω-Agatoxin IVA (#STA-500) action on CaV2.1 currents. Maximum current amplitudes were plotted as a function of time. Membrane potential was held at -100 mV and cells were stimulated by a 100 ms voltage ramp to +40 mV. 500 nM ω-Agatoxin IVA were perfused as indicated by the bar (green) during 200 sec application. B. Superimposed examples of CaV2.1 channel current in the absence (control) and presence (green) of 500 nM ω-Agatoxin-IVA (taken from the experiment in A).
- Alomone Labs ω-Agatoxin IVA potently inhibits CaV2.1 channel currents expressed in HEK 293 cells.CaV2.1 currents were elicited by 40 ms voltage ramp from a holding potential of -100 mV to +60 mV, applied every 10 sec using whole-cell voltage clamp technique. Left: Superimposed traces of CaV2.1 currents under control conditions (black) and following 2 min perfusion with Alomone Labs 200 nM ω-Agatoxin IVA (red). Right: Time course of CaV2.1 peak current amplitude change as a result of the application of 200 nM ω-Agatoxin IVA (duration of perfusion indicated by horizontal bar).
- Mintz, I.M. et al. (1992) Nature 355, 827.
- Moreno, H. et al. (1997) Proc. Natl. Acad. Sci. 94, 14042.
- Bourinet, E. et al. (1999) Nat. Neurosci. 2, 407.
- Meir, A. et al. (1999) Physiol. Rev. 79, 1019.
- Stephens, G.J. et al. (2001) Eur. J. Neurosci. 13, 1902.
- Berrow, N.S. et al. (1997) Eur. J. Neurosci. 9, 739.
- Pearson, H.A. et al. (1995) J. Physiol. 482, 493.
- Nakanishi, S. et al. (1995) J. Neurosci. Res. 41, 532.
Native ω-Agatoxin IVA (ω-Aga-IVA) was originally isolated from Agelenopsis aperta spider venom, and was shown to be a selective blocker of CaV2.1 (P/Q type) channels1. However, the sensitivity depends on the auxiliary b subunit isoform2 and on the splice variant3. Therefore, the effective concentration varies between systems. In accordance, the toxin blocks presynaptic Ca2+ currents and synaptic transmission in a variety of synapses4,5.
ω-Agatoxin IVA is widely used in electrophysiological measurements of cloned and native channels6,7. It is used to assess the role of CaV2.1 channels in synaptic transmission4. In addition, it was used to map the spatial distribution of CaV2.1 channels in mouse cerebellar and hippocampal brain slices8.
Alomone Labs ω-Agatoxin IVA blocks CaV2.1 channel in mouse calyx of Held.Calyxes were whole-cell voltage-clamped at -80 mV. Traces were recorded in the presence of 1 mM CaCl2, pharmacological isolation of VGCC subtypes was performed in 2 mM CaCl2. 200 nM ω-Agatoxin IVA (#STA-500) was applied to selectively block CaV2.1.Adapted from Lubbert, M. et al. (2017) eLife 6, e28412. with permission of eLife Sciences.
ω-Agatoxin IVA (#STA-500) is a highly pure, synthetic, and biologically active peptide toxin.
- Knockdown of FMRP enhances synaptic vesicle exocytosis in presynaptic terminals of DRG neurons via CaV2.2 channels.A and B. vGpH response to 40 AP at 10 Hz from presynaptic terminals of DRG neurons transfected with Ctrl shRNA (A) or FMRP shRNA (B) before and after treatment with ω-Conotoxin GVIA (#C-300) and ω-Agatoxin IVA (#STA-500). Fluorescence intensities were normalized to the peak of a brief application of NH4Cl. C. Normalized vGpH responses to 40 AP at 10 Hz from presynaptic terminals of DRG neurons transfected with Ctrl shRNA (black-filled bar, 100±10.6%, n = 38) or FMRP shRNA (red open bar, 137.0±12.6%, n = 25, P = 0.027). ω-Conotoxin GVIA (ConoTx) reduces Ctrl shRNA and FMRP shRNA responses to a similar level (44.7±4.9%, n = 15 and 41.6±3.3%, n = 24, respectively). ω-Conotoxin GVIA and ω-Agatoxin IVA (AgaTx) application reduces further the responses: Ctrl shRNA = 17.3±3.2%, n = 38, and FMRP shRNA = 18.1±5.0%, n = 27. D. Average vGpH response to a 40 Hz stimulation for 30 s from presynaptic terminals of DRG neurons transfected with Ctrl shRNA (blackfilled squares) or FMRP shRNA (open red squares).
Adapted from Ferron, L. et al. (2014) with permission of Springer Nature.
- Torturo, C.L. et al. (2019) eNeuro 6, e0278.
- Folci, A. et al. (2018) J. Biol. Chem. 293, 1040.
- Goldspink, D.A. et al. (2018) Mol. Metab. 7, 90.
- Casas-Torremocha, D. et al. (2017) Front. Neural Circuits 11, 69.
- Chamberland, S. et al. (2017) J. Neurosci. 37, 4913.
- de Juan-Sanz, J. et al. (2017) Neuron 93, 867.
- Liang, M. et al. (2017) Sci. Rep. 7, 431.
- Lubbert, M. et al. (2017) eLife 6, e28412.
- Margolis, E.B. et al. (2017) Neuropharmacology 123, 420.
- Nagy, B. et al. (2017) PLoS Biol. 15, e2001993.
- Thuesen, A.D. et al. (2017) Acta Physiol. 219, 642.
- Weon, H. et al. (2017) Life Sci. 188, 110.
- Xie, R. and Manis, P.B. (2017) J. Physiol. 595, 919.
- D’Onofrio, S. et al. (2016) Physiol. Rep. 4, e12740.
- Luster, B.R. et al. (2016) Physiol. Rep. 4, e12787.
- Pennock, R.L. and Hentges, S.T. (2016) J. Neurophysiol. 115, 2376.
- Squecco, R. et al. (2016) Mol. Cell. Neurosci. 75, 50.
- Sugino, S. et al. (2016) J. Neurophysiol. 115, 1577.
- Gan, K.J. et al. (2015) Mol. Biol. Cell. 26, 1058.
- Gerencser, A.A. et al. (2015) Biochem. J. 471, 111.
- Pais, R. et al. (2015) Peptides 77, 9.
- Zhou, L. et al. (2015) Proc. Natl. Acad. Sci. U.S.A. 112, 15474.
- Ferron, L. et al. (2014) Nat. Commun. 5, 3628.
- He, S. et al. (2014) J. Neurosci. 34, 5261.
- Alamilla, J. et al. Gillespie, D.C. (2013) PLoS ONE 8, e75688.
- Alvarez, Y.D. et al. (2013) PLoS ONE 8, e54846.
- Hermann, D. et al. (2013) Eur. J. Pharmacol. 702, 44.
- Koch, H. et al. (2013) J. Neurosci. 33, 3633.
- Lowe, M. et al. (2013) Exp. Physiol. 98, 1199.
- Radzicki, D. et al. (2013) J. Neurosci. 33, 9920.
- Tzour, A. et al. (2013) J. Neuroendocrinol. 25, 76.
- Izquierdo-Serra, M. et al. (2013) Biochim. Biophys. Acta 1830, 2853.
- Jones, S.L. and Stuart, G.J. (2013) J. Neurosci. 33, 19396.
- Baillie, L.D. et al. (2012) Neuropharmacology 63, 362.
- Kailey, B. et al. (2012) Am. J. Physiol. 303, E1107.
- Liu, S. et al. (2012) J. Neurophysiol. 107, 473.
- Lv, P. et al. (2012) J. Neurosci. 32, 16314.
- Wang, S. et al. (2012) Cerebral Cortex 3, 584.
- Williams, C. et al. (2012) Nat. Neurosci. 15, 1195.
- Alle, H. et al. (2011) J. Neurosci. 31, 8001.
- Rogers, G.J. et al. (2011) J. Physiol. 589.5, 1081.
- Martel, P. et al. (2011) PLoS ONE 6, e20402.
- Craviso, G.L. et al. (2010) Cell. Mol. Neurobiol. 30, 1259.
- Inoue, T. and Bryant, B.P. (2010) Cell. Mol. Neurobiol. 30, 35.
- Braun, M. et al. (2008) Diabetes 57, 1618.