Overview
Alternative Name α-MI, CtxMI, M1
Lyophilized Powder yes
Origin Synthetic peptide
MW: 1494 Da
Purity: >98% (HPLC)
Effective concentration 2-20 nM.
Sequence GRCCHPACGKNYSC.
Modifications Disulfide bonds between Cys3-Cys8, Cys4-Cys14. Cys14 – C-terminal amidation.
Structure
Molecular formula C58H88N22O17S4.
CAS No.: 83481-45-2
Activity α-Conotoxin MI reversibly blocks fetal muscle α1/β1/γ/δ nicotinic ACh receptor1,2,3.
References-Activity
- McIntosh, M. et al. (1982) Arch. Biochem. Biophys. 218, 329.
- Bren, N. and Sine, S.M. (2000) J. Biol. Chem. 275, 12692.
- Jacobsen, R.B. et al. (1999) Biochemistry 38, 13310.
Accession number
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 other 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 MI inhibits muscle fetal α1/β1/γ/δ nAChR heterologously expressed in Xenopus oocytes.A. Time course of α-Conotoxin MI (#STC-370) 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 50 µM acetylcholine every 50 seconds. 20 nM (green) α-Conotoxin MI significantly inhibits the currents. B. Superimposed traces of α1/β1/γ/δ nAChR currents evoked by ACh (arrow) after application of control (black) and 20 nM (green) α-Conotoxin MI (taken from the recording in A).
Scientific background
α-Conotoxin MI is a 14 amino acid peptidyl toxin isolated from the Conus magus (Magus cone, Magician’s cone snail venom)1. It acts on postsynaptic membranes on muscles and blocks mammalian nicotinic ACh channel receptor composed of α1/δ subunits with high potency and α1/γ with a low potency2.
Structure activity relationship studies were done in order to map the major amino acids in α-Conotoxin MI and the overall results show that primarily hydrophobic interactions stabilize the complex between the toxin and the α-δ interface of the nAChR3. Proline-6 and Tyrosine-12 dramatically reduced toxin potency at the high-affinity α/δ site while having comparatively little effect on low-affinity α/γ binding4.
Target α1/β1/γ/δ nAChR
Peptide Content: 100%
Lyophilized Powder
For research purposes only, not for human use
Last Update: 12/09/2024
Specifications
Citations
Citations
