Overview
Lyophilized Powder yes
Origin Synthetic peptide
MW: 1601.8 Da
Purity: >98% (HPLC)
Effective concentration 1-10 µM.
Sequence GCCARAACAGIHQELC.
Modifications Disulfide bonds between Cys2-Cys8 and Cys3-Cys16.
Structure
Molecular formula C62H100N22O20S4.
Activity α-Conotoxin LtIA reversibly blocks α3/β2 nicotinic ACh channel receptor1. Little or no block was obtained by 10 fold concentrations of the toxin on α4/β2 and α3/β4 nicotinic ACh receptors.1
References-Activity
- Luo, S. et al. (2010) The J. Biol. Chem. 285, 12355.
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 aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
Storage of solutions Up to two week at 4°C or three months at -20°C.
Our bioassay
Alomone Labs α-Conotoxin LtIA inhibits α3/β2 nAChR channels heterologously expressed in Xenopus oocytes.A. Time course of α-Conotoxin LtIA (#STC-550) action on α3/β2 nAChR channels. Current amplitudes were plotted as a function of time. Membrane potential was held at –60 mV and oocytes were stimulated by exposure to 100 μM acetylcholine and 1 μM atropine, for 1 second every 50 seconds. 2 µM α-Conotoxin LtIA was perfused during the period marked by the bar. B. Superimposed traces of α3/β2 nAChR channel current in the absence and presence of 2 μM α-Conotoxin LtIA (taken from the experiment in A).
Scientific background
α-Conotoxin LtIA is a 16 amino acid peptidyl toxin isolated from the Conus litteratus (Lettered cone) venom1. It belongs to the α-Conotoxin superfamily, although it lacks the highly conserved Ser-Xaa-Pro sequence. It reversibly blocks α3/β2 nicotinic ACh channel receptor with an IC50 of 9.8 nM1.
Little or no block was obtained by 10 fold concentrations of the toxin on α4/β2 and α3/ß4 nicotinic ACh receptors1.
α-Conotoxin LtIA was substantially less potent on α6/α3/β4 versus α6/α3/β2/β3 nAChRs. In contrast, there was little or no block by α-Conotoxin LtIA at 10 µM on other nAChR, including α1/β1/δ/ε, α2/β2, α2/β4, α4/β2, α4/β4, α7, and α9/α101.
Target α3/β2 nAChR
Peptide Content: 100%
Lyophilized Powder
For research purposes only, not for human use
Last Update: 02/01/2024
Specifications
Citations
Citations
