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αA-Conotoxin PIVA

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

Cat #: STC-600
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 2651 Da
    Purity: >98% (HPLC)
    Effective concentration 1-20 nM
    Sequence GCCGSYXNAACHXCSCKDRXSYCGQ
    Modifications Disulfide bonds between Cys2-Cys16, Cys3-Cys11 and Cys14-Cys23. X = Hydroxyproline. Glu25 – Glutamine amide.
    Structure
    Molecular formula C103H152N34O37S6
    Activity αA-Conotoxin PIVA reversibly blocks muscle α1/β1/γ/δ nicotinic ACh receptor1,2.
    References-Activity
    1. Hopkins, C. et al. (1995) J. Biol. Chem. 270, 22361.
    2. Teichert, R.W. et al. (2006) Biochemistry 45, 1304.
    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 αA-Conotoxin PIVA inhibits muscle fetal α1/β1/γ/δ nAChR heterologously expressed in Xenopus oocytes.
      Alomone Labs αA-Conotoxin PIVA inhibits muscle fetal α1/β1/γ/δ nAChR heterologously expressed in Xenopus oocytes.
      A. Time course of αA-Conotoxin PIVA (#STC-600) action on muscle α1/β1/γ/δ nAChR. Current amplitudes were plotted as a function of time. Membrane potential was held at –80 mV and oocytes were stimulated by exposure to 10 µM acetylcholine every 50 seconds. 5 nM (green) and 25 nM (magenta) αA-Conotoxin PIVA significantly inhibits the currents.
      B. Superimposed traces of α1/β1/γ/δ nAChR currents evoked by ACh (arrow) after application of control, 5 nM (green) and 25 nM (magenta) αA-Conotoxin PIVA (taken from the recording in A).
    References - Scientific background
    1. Hopkins, C. et al. (1995) J. Biol. Chem. 270, 22361.
    2. Teichert, R.W. et al. (2006) Biochemistry 45, 1304.
    Scientific background

    αA-Conotoxin PIVA is the first member of a new family of nAChR-targeted Conus peptides, named short αA-conotoxins1. It is a peptide toxin originally isolated from Conus Purpurascens (Purple cone) venom1.

    This peptide reversibly blocks postsynaptic muscle fetal α1/β1/γ/δ nicotinic ACh receptor1,2 . It also blocks postsynaptic muscle adult α1/β1/ε/δ nicotinic ACh receptor, with lower affinity (IC50 of 22 nM to the adult compared to 2.3 nM to the fetal nAChR)2.

    αA-conotoxin PIVA has a strikingly different amino acid sequence and a Cys framework from all other nAChR-targeted peptides previously characterized from Conus venoms. Despite the striking structural divergence, the peptide blocks the ACh binding site of the nAChR at the neuromuscular junction, similar to the well known typical of a-conotoxins1.

    The characterization of the short αA-conotoxins revealed diverse kinetics of a block of the fetal muscle nAChR, particularly in dissociation rates. The structure-function relationships of native αA-conotoxins revealed a single amino acid locus (alternatively either His or Pro) that is a critical determinant of the dissociation kinetics2.

    Target α1/β1/γ/δ nAChR
    Net Peptide Content: 100%
    Last update: 08/06/2021

    αA-Conotoxin PIVA (#STC-600) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use

    Applications

    Specifications

    Scientific Background

    Citations

    Citations
    Product citations
    1. Kiss, T. et al. (2014) PLoS ONE 9, e109538.
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