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α-Conotoxin EIIB

Alpha-conotoxin EIIB

A Potent Antagonist of α1/β1/δ/γ nAChR

Cat #: STC-230
Alternative Name Alpha-conotoxin EIIB
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 1754.5 Da
    Purity: >99% (HPLC)
    Form Lyophilized powder.
    Effective concentration 1-50 nM.
    Modifications Disulfide bonds between Cys5-11, Cys6-16. Cys16 – C-terminal amidation. Hydroxyprolines at Pro3 and Pyrrolidone carboxylic acid at Q1.
    Molecular formula C71H105N25O20S4.
    Activity α-Conotoxin EIIB is a potent α1/β1/δ/γ nAChR antagonist1.
    1. Echterbille, J. et al. (2017) Toxicon 130, 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 EIIB inhibits muscle nicotinic ACh receptors expressed in Xenopus oocytes.
      Alomone Labs α-Conotoxin EIIB inhibits muscle nicotinic ACh receptors expressed in Xenopus oocytes.
      A. Representative time course of α-Conotoxin EIIB (#STC-230) inhibition of α1/β1/γ/δ nAChR. Currents were elicited every 50 sec by transient application of 20 µM ACh, while membrane potential was held at -80 mV, and inhibited by 50 nM α-Conotoxin-EIIB (horizontal bar). B. Superimposed traces of α1/β1/γ/δ nAChR currents upon application of control and of 50 nM α-Conotoxin-EIIB (taken from the recording in A).
    References - Scientific background
    1. Echterbille, J. et al. (2017) Toxicon 130, 1.
    2. Benie, A.J. et al. (2000) FEBS Lett. 476, 287.
    3. Lustig, L.R. et al. (2006) Anat. Rec. A Discov. Mol. Cell. Evol. Biol. 288, 424.
    Scientific background

    α-Conotoxin EIIB is a peptide toxin originally isolated from Conus ermineus (Atlantic fish-hunting cone) venom. It is a potent α1/β1/δ/γ nicotinic acetylcholine receptor antagonist and displays a Ki of 2.2 ± 0.7 nM1. The peptide toxin is stabilized by six hydrogen bonds and disulfides between residues 2 and 7 and 3 and 132.

    Nicotinic acetylcholine receptors (nAChRs) are ionotropic multisubunit, neurotransmitter-gated receptors of the cholinergic system. They are assembled from one or more α subunits (α1-α10) alone or together with one or more β subunits (β1–β4)3. Other subunits also co-assemble in the formation of the receptor channel.

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

    α-Conotoxin EIIB (#STC-230) is a highly pure, synthetic and biologically active peptide toxin.

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