Iota-Conotoxin RXIA

R11.6, r11a
An Activator of NaV1.6, NaV1.2 and NaV1.7 Channels
  • New
Cat #: STI-300
Alternative Name R11.6, r11a
  • Lyophilized Powder
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 4975 Da.
    Purity: >98% (HPLC)
    Form Lyophilized powder
    Effective concentration 1-10 µM
    Sequence GPSFCKADEKPCEYHADCCNCCLSGICAPSTNWILPGCSTSSFFKI
    Modifications Disulfide bonds between: Cys5-Cys19, Cys12-Cys22, Cys18-Cys27, Cys21-Cys38 Hydroxylation: P2, P11, P29 D-amino acid: F - D-Phenylalanine 44.
    Structure
    • Iota-Conotoxin RXIA
    Molecular formula C212H318N54O66S8
    Activity Iota-Conotoxin RXIA activates NaV1.2, NaV1.6, and NaV1.7 by shifting the voltage-dependence of activation to more hyperpolarized levels1.
    References-Activity
    1. Buczek, O. et al. (2007) Biochemistry 46, 9929.
    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 DDW. Centrifuge all products before use (10000 x g 5 min).
    Storage of solutions Store at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing.
    Our bioassay
    • Iota-Conotoxin RXIA
      Alomone Labs Iota-Conotoxin RXIA affects the activation of NaV1.6 channels expressed in Xenopus oocytes.
      A. Representative traces of NaV1.6 channel currents before (black) and after the application of 1 µM (magenta) and 10 µM (green) Iota-Conotoxin RXIA (#STI-300). Iota-Conotoxin RXIA caused a significant current at a voltage that does not normally activates the channel. Membrane potential was held at -100 mV, and a voltage step to -20 mV was applied every 10 sec. B. Representative time course of current amplitude at -20 mV before, during application of 1 µM and 10 µM Iota-Conotoxin RXIA (as indicated by bars) and upon wash, demonstrating the current amplitude enhancement.
    References - Scientific background
    1. Deuis, J.R. et al. (2017) Neuropharmacology 127, 87.
    2. Buczek, O. et al. (2007) Biochemistry 46, 9929.
    Scientific background

    Iota-Conotoxin RXIA, a peptide toxin originally isolated from Conus radiatus, is a voltage-gated sodium channel activator. The peptide toxin belongs to of the I1-superfamily, which contains eight cysteine residues arranged in a -C-C-CC-CC-C-C- pattern. Iota-RXIA is one of three characterized I1 peptides in which the third to last residue is posttranslationally isomerized to the d configuration. Naturally occurring iota-Conotoxin RXIA with d-Phe44 is significantly more active as an excitotoxin than the l-Phe analogue both in vitro and in vivo although crystallography data has shown the overall structure is only slightly altered by this shift1.

    Iota-Conotoxin RXIA affects NaV1.6, Nav1.2 and Nav1.7 sodium channels by shifting their voltage dependence of activation to more hyperpolarized potentials2.

    NaV channel agonists have been isolated from the venom of different organisms and are also produced by plants, bacteria and algae. These compounds provide key insights into the molecular structure, function and pathophysiological roles of NaV channels and are important tools due to their specific subtype-selectivity1.

    Target Nav1.6, Nav1.2 and Nav1.7 channels
    Net Peptide Content: 100%

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    Last update: 28/06/2020

    Iota-Conotoxin RXIA (#STI-300) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
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