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α-Conotoxin MrIC


An Antagonist and Partial Agonist of α7 nAChR

Cat #: STC-320
Alternative Name Mr1.7c
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 1835 Da
    Purity: >98% (HPLC)
    Form Lyophilized powder
    Effective concentration 1-10 µM
    Modifications Disulfide bonds between Cys3-Cys9 and Cys4-Cys17, C-terminal amidation at Cys17.
    Molecular formula C74H115N23O24S4
    Activity α-Conotoxin MrIC is a selective antagonist of α7 nAChR heterologously expressed in Xenopus oocytes, while acting as an agonist of endogenous α7 nAChR in the prescence of PNU-1205961.
    1. Jin, A.H. et al. (2014) Biochemistry 53, 1.
    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 Any aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
    Storage of solutions Up to two weeks at 4°C or three months at -20°C.
    Our bioassay
    • Alomone Labs α-Conotoxin MrIC inhibits α7 nAChR heterologously expressed in Xenopus oocytes.
      Alomone Labs α-Conotoxin MrIC inhibits α7 nAChR heterologously expressed in Xenopus oocytes.
      A. Time course of α-Conotoxin MrIC (#STC-320) action on α7 nAChR currents, elicited every 50 sec by a transient applications of 100 µM ACh + 0.3 μM PNU-120596, while membrane potential was held at -80 mV. Application of 2 µM and 10 µM α-Conotoxin MrIC (as indicated by bars) significantly inhibits the currents. B. Superimposed traces of α7 nAChR currents upon application of control, 2 µM and 10 µM α-Conotoxin MrIC (taken from the experiment in A).
    References - Scientific background
    1. Jin, A.H. et al. (2014) Biochemistry 53, 1.
    2. Mueller, A. et al. (2015) Biochem. Pharmacol. 94, 155.
    3. Lustig, L.R. (2006) Anat. Rec. A Discov. Mol. Cell. Evol. Biol. 288, 424.
    4. McIntosh, J.M. et al. (2009) Biochem. Pharmacol. 78, 693.
    Scientific background

    α-Conotoxin MrIC is peptide toxin originally isolated from Conus marmoreus. It is a competitive and selective antagonist of α7 nicotinic acetylcholine receptor (nAChRα7). Peptide toxins belonging to α-conotoxin family are relatively short peptides, between 12−19 amino acid residues and demonstrate high affinity towards nAChRs. They are stabilized by two disulfide bonds1,2.

    In Ca2+ responses assay to α-Conotoxin MrIC in SH-SY5Y cells endogenously expressing α7 nAChR, α-Conotoxin MrIC elicits concentration-dependent increases in intracellular Ca2+ in the presence of the α7 nAChR-specific positive allosteric modulator PNU120596 with an EC50 value of 1.9 µM2. Interestingly, α-Conotoxin MrIC antagonizes nAChRα7 heterologously expressed in Xenopus oocytes1.

    nAChRs receptors are responsible for mediating the effects of the neurotransmitter acetylcholine (ACh). They play critical physiologic roles in the central and peripheral nervous system where they regulate neurotransmitter release, cell excitability, neuronal integration, and are involved in functions such as sleep and arousal patterns, fatigue, hunger, anxiety, and pain processing3,4.

    Target α7 nAChR
    Peptide Content: 100%
    Last update: 06/11/2022

    α-Conotoxin MrIC (#STC-320) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
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