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α-Conotoxin SI

Alpha-conotoxin S1, SI

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

Cat #: STC-825
Alternative Name Alpha-conotoxin S1, SI
Lyophilized Powder yes
  • Bioassay Tested
    • Origin Synthetic peptide
    MW: 1354 Da
    Purity: >98% (HPLC)
    Form Lyophilized powder.
    Effective concentration 200-1000 nM.
    Sequence ICCNPACGPKYSC.
    Modifications Disulfide bonds between Cys2- Cys7, Cys3- Cys13. Cys13 - C-terminal amidation.
    Structure
    Molecular formula C55H84N16O16S4.
    CAS No.: 115797-06-3
    Activity α-Conotoxin SI inhibits muscle type α1/β1/δ/γ nicotinic acetylcholine receptors (nAChRs) at 200-1000 nM1 .
    References-Activity
    1. Zafaralla, G.C. et al. (1988) Biochemistry 27, 7102.
    Accession number P15471.
    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 for 5 min).
    Storage of solutions Up to two weeks at 4°C or three months at -20°C.
    Our bioassay
    • Alomone Labs α-Conotoxin SI inhibits muscle nicotinic ACh receptors expressed in Xenopus oocytes.
      Alomone Labs α-Conotoxin SI inhibits muscle nicotinic ACh receptors expressed in Xenopus oocytes.
      A. Representative time course of α-Conotoxin SI (#STC-825) inhibition of α1/β1/γ/δ nAChR currents, elicited every 50 sec by transient application of 20 µM acetylcholine, while membrane potential was held at -80 mV, and reversibly inhibited by 0.2 µM and 1 µM α-Conotoxin SI (top horizontal bars). B. Superimposed traces of α1/β1/γ/δ nAChR currents upon application of control, 0.2 µM and 1 µM α-Conotoxin SI (taken from the recording in A).
    References - Scientific background
    1. Benie, A.J. et al. (2000) FEBS Lett. 476, 287.
    2. Lustig, L.R. (2006) Anat. Rec. A Discov. Mol. Cell. Evol. Biol. 288, 424.
    Scientific background

    α-Conotoxin SI is a 13-amino acid residue peptide toxin originally isolated from Conus striatus venom. The toxin’s structure is stabilized by six hydrogen bonds and disulfides between cysteine residues 2 and 7 and 3 and 131. It is a potent and selective antagonist of α1/β1/δ/γ nicotinic acetylcholine receptors (nAChRs).

    Nicotinic acetylcholine receptors are ionotropic multi-subunit, neurotransmitter-gated receptors of the cholinergic system. They are responsible for mediating the effects of the neurotransmitter acetylcholine (ACh). nAChRs are assembled from one or more α subunits (α1-α10) alone or together with one or more β subunits (β1–β4)2.

    Target Muscle nAChR
    Net Peptide Content: 100%
    Lyophilized Powder
    Last update: 08/06/2021

    α-Conotoxin SI (#STC-825) is a highly pure, synthetic, and biologically active peptide toxin.

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

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