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Mu-conotoxin SxIIIC

µ-conotoxin SxIIIC, SxIIIC peptide

A potent blocker of NaV Channels

Cat #: STC-130
Alternative Name µ-conotoxin SxIIIC, SxIIIC peptide
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Conus striolatus (Cone snail)
    Source Synthetic peptide
    MW: 2437 Da
    Purity: >98%
    Form Lyophilized Powder
    Effective concentration 15 – 200 nM
    Sequence RGCCNGRGGCSSRWCRDHARCC-NH2
    Modifications Disulfide bonds location - Cys3-Cys15, Cys4-Cys21 and Cys10-Cys22
    Structure
    Molecular formula C90H141N41O28S6
    Activity SxIIIC most potently blocks NaV1.4 channel, with 10-fold selectivity over NaV1.1, 1.3, 1.6 and 1.7, 24-fold selectivity over hNaV1.2.
    References-Activity
    1. McMahon, K.L. et al. (2020) Biomedicines, 8, 321.
    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. Protect from light and moisture.
    Solubility Soluble in water. It is recommended to prepare fresh solutions in working buffers before use, or aliquot stock solutions reconstituted in distilled water and keep at -20°C. Upon use, dilute the stock solution in the desired working buffer. Prevent repeated thawing and freezing cycles. Centrifuge all product preparations before use (10,000 g for 1 min).
    Storage of solutions Store up to one week at 4°C or up to 6 months at -20°C.
    Our bioassay
    • Alomone Labs μ-conotoxin SxIIIC inhibits NaV1.4 channel currents heterologously expressed in Xenopus oocytes.
      Alomone Labs μ-conotoxin SxIIIC inhibits NaV1.4 channel currents heterologously expressed in Xenopus oocytes.
      A. Representative time course of μ-conotoxin SxIIIC (#STC-130) inhibition of NaV1.4 channels current. Membrane potential was held at -100 mV, current was elicited by a 100 ms voltage step to 0 mV every 10 sec, and significantly inhibited by application of 50 nM μ-conotoxin SxIIIC (green).
      B. Superimposed traces of NaV1.4 channel currents in the absence (control) and presence (green) of 50 nM μ-conotoxin SxIIIC (taken from the recording in A).
    • Alomone Labs μ-conotoxin SxIIIC inhibits NaV1.7 channel currents heterologously expressed in Xenopus oocytes.
      Alomone Labs μ-conotoxin SxIIIC inhibits NaV1.7 channel currents heterologously expressed in Xenopus oocytes.
      A. Representative time course of μ-conotoxin SxIIIC (#STC-130) inhibition of NaV1.7 channels current. Membrane potential was held at -100 mV, current was elicited by a 100 ms voltage step to 0 mV every 10 sec, and significantly inhibited by application of 1 µM μ-conotoxin SxIIIC (green).
      B. Superimposed traces of NaV1.7 channel currents in the absence (control) and presence (green) of 1 µM μ-conotoxin SxIIIC (taken from the recording in A).
    References - Scientific background
    1. McMahon, K.L. et al. (2020) Biomedicines, 8, 321.
    2. Huang, W. et al. (2017) Protein Cell, 8, 401.
    3. Mackieh, R. et al. (2021) Mar. Drugs, 19, 562.
    Scientific background

    µ-conotoxin  SxIIIC (SxIIIC) is a 22 amino acid peptidyl toxin originally isolated from the venom of the cone snail, Conus striolatus1. SxIIIC  is a potent and irreversible blocker of voltage-gated sodium (Nav) channels, which displays a unique µ-conotoxin selectivity profile of human  (h)NaV1.4 > hNaV1.3 > hNaV1.1 ≈ hNaV1.6 ≈ hNaV1.7 > hNaV1.2 >> hNaV1.5 ≈ hNaV1.81.

    Voltage-gated sodium channels (VGSCs) are transmembrane proteins that control the voltage-dependent increase in sodium permeability. VGSCs play a fundamental role in normal neurological function, especially in the initiation and propagation of action potentials. Nav channels have been the topic of significant research and discussion for a considerable amount of time given their unique functions in electrical cell signaling. These channels are very important for homeostasis, thus specific genetic abnormalities in VGSC genes can result in a range of muscle, cardiac, and neurological disorders known as “channelopathies”2. Marine toxins appear to be an emerging source of therapeutic tools that can relieve pain or treat VGSC-related human channelopathies3.

    Target Nav1.4, Nav1.3, Nav1.1, Nav1.6 and Nav1.7 blocker
    Peptide Content: 100%
    Last update: 19/10/2021

    Mu-conotoxin SxIIIC (#STC-130) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use

    Applications

    Specifications

    Scientific Background

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