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Alpha-conotoxin RgIA

RgIA, α-Conotoxin RgIA

A Potent Antagonist of α9α10 nAChR, a Weak Antagonist of α7, and A Blocker of N-Type Ca2+ Channels

Cat #: STC-010
Alternative Name RgIA, α-Conotoxin RgIA
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Conus regius (Crown cone)
    Source Synthetic peptide
    MW: 1571 Da
    Purity: >98% (HPLC)
    Form Lyophilized Powder
    Effective concentration 20 nM – 1 µM
    Sequence GCCSDPRCRYRCR-OH
    Modifications Disulfide bonds location - Cys2-Cys8, Cys3-Cys12
    Structure
    Molecular formula C59H95N25O18S4
    Activity A potent and selective antagonist of the α9α10 nAChR subtype, which also shows a weak activity towards α7 nAChR1,2. RgIA was also shown to inhibit HVA calcium channel currents in DRG neurons3.
    References-Activity
    1. Ellison, M. et al. (2006) Biochemistry, 45, 1511.
    2. Ellison, M. et al. (2008) J Mol. Biol., 377, 1216.
    3. Callaghan, B. et al. (2008) J Neurosci., 28, 10943.
    Shipping and storage Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.
    Solubility Soluble in water. It is recommended to prepare fresh solutions in working buffers before use, or aliquot stock solutions reconstituted in distilled water and keep at -20°C. Upon use, dilute the stock solution in the desired working buffer. Prevent repeated thawing and freezing cycles. Centrifuge all product preparations before use (10,000 g for 1 min).
    Storage of solutions Store at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C.
    Our bioassay
    • Alomone Labs α-Conotoxin RgIA inhibits α7 nAChR heterologously expressed in Xenopus oocytes.
      Alomone Labs α-Conotoxin RgIA inhibits α7 nAChR heterologously expressed in Xenopus oocytes.
      A. Time course of α-Conotoxin RgIA (#STC-010) action on α7 nAChR currents, elicited every 50 sec. by a transient application of 200 µM ACh + 0.3 µM PNU-120596, while membrane potential was held at -80 mV. Application of 1 µM (green) and 5 μM (magenta) α-Conotoxin RgIA significantly inhibits the currents.
      B. Superimposed traces of α7 nAChR currents upon application of control, 1 µM (green) and 5 μM (magenta) α-Conotoxin RgIA (taken from the recording in A).
    References - Scientific background
    1. Ellison, M. et al. (2006) Biochemistry, 45, 1511.
    2. Ellison, M. et al. (2008) J Mol. Biol., 377, 1216.
    3. Callaghan, B. et al. (2008) J Neurosci., 28, 10943.
    4. Azam, L. et al. (2009) Acta Pharmacol. Sin., 30, 771.
    5. Hone, A. J. et al. (2018) FEBS Lett., 592, 1045.
    6. Vincler, M. et al. (2006) PNAS, 103, 17780.
    7. Vincler, M. et al. (2007) Expert Opin. Ther. Targets, 11, 891.
    8. Pacini, A. et al. (2016) Exp. Neurol., 282, 37.
    Scientific background

    α-conotoxin RgIA (RgIA) is a 13 amino acid peptidyl toxin cloned from a genomic DNA library of the marine worm-hunting sea snail, Conus regius1. RgIA belongs to the α4/3 subfamily of conotoxins (i.e., a family of peptides with four amino acids in the first loop and three in the second loop) and is a potent and selective antagonist of the α9α10 nicotinic acetylcholine receptor (nAChR) subtype, which also shows a weak activity towards α7 nAChR1,2. RgIA was also shown to inhibit high-voltage-activated (HVA) calcium channel currents in rat dorsal root ganglion (DRG) neurons3.

    The nAChRs are acetylcholine-gated ion channels. Given the important physiological roles of nAChRs in pain, inflammation, nicotine addiction, Alzheimer's disease, and Parkinson's disease, specific targeting of the relevant nAChR subtypes is an attractive pharmaceutical strategy. α-conotoxins are among the most promising drug development leads for treating these diseases4,5. RgIA was shown to be an effective analgesic agent in a rat model of nerve injury and also reduced the immune response contributing to peripheral nerve damage6,7. Furthermore, RgIA was shown to prevent neuropathic pain induced by oxaliplatin treatment8.

    Target α9α10 nAChRs, α7, and N-Type Ca2+ Channels
    Peptide Content: 100%
    Last update: 29/08/2021

    Alpha-conotoxin RgIA (#STC-010) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
    Shipping and Ordering information