Overview
Alternative Name Long neurotoxin 1, α-Bgtx, α-BuTX
Lyophilized Powder yes
Origin Natural peptide isolated from Bungarus multicinctus (Many-banded krait).
MW: 7984 Da
Purity: >99% (HPLC)
Effective concentration 1 nM - 3 μM.
Sequence IVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCCSTDKCNPHPKQRPG.
Modifications Disulfide bonds between Cys3-Cys23, Cys16-Cys44, Cys29-Cys33, Cys48-Cys59 and Cys60-Cys65.
Structure
Molecular formula C338H529N97O105S11.
CAS No.: 11032-79-4
Activity α-Bungarotoxin blocks postsynaptic neuromuscular transmission via competitive inhibition of nicotinic ACh receptors (nAChRs), thereby preventing the depolarizing action on postsynaptic membranes and blocking neuromuscular transmission. Selective for α7 receptors (IC50 value of 1.6 nM) and α3/β4 receptors (IC50 value of >3 μM)1,2. The toxin also blocks GABA(A) receptor subtypes3.
References-Activity
- Wilson, S.P. and Kirshner, N. (1977) J. Neurochem. 28, 687.
- Garcia-Guzman, M. et al. (1995) Eur. J. Neurosci. 7, 647.
- McCann, C.M. et al. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 5149.
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 weeks at 4°C or three months at -20°C.
Our bioassay
Alomone Labs α-Bungarotoxin inhibits α7 nicotinic ACh channels heterologously expressed in Xenopus oocytes.Time course of α7 nicotinic ACh channel current recording. Membrane potential was held at -60 mV and constantly perfused with a solution containing 10 mM Ca2+ and 1 μM PNU-120596. 1 μM ACh was applied for 2 seconds every 200 seconds in order to stimulate channel current. 50 nM α-Bungarotoxin (#B-100) was applied (green trace) during the ACh application and inhibited channel current.
Alomone Labs α-Bungarotoxin inhibits muscle nAChR heterologously expressed in Xenopus oocytes.A. Time course of α-Bungarotoxin (#B-100) action on muscle nicotinic ACh channel current (expressing α1/β1/γ/δ nAChRs). Membrane potential was held at -80 mV and oocytes were constantly perfused with a solution containing 0.3 μM PNU-120596. 10 μM ACh was applied every 100 seconds in order to stimulate channel current. 10 nM (red trace) or 50 nM (green trace) α-Bungarotoxin were applied for 4.5 min each during the ACh application and inhibited channel current, as indicated. B. Superimposed traces of muscle nAChR currents in the absence (control) and the presence of 10 nM (red trace) or 50 nM (green trace) α-Bungarotoxin.
References - Scientific background
- Ohta, M. et al. (1987) FEBS Lett. 222, 79.
- Wilson, P.T. et al. (1988) Mol. Pharmacol. 34, 643.
- Wilson, S.P. and Kirshner, N. (1977) J. Neurochem. 28, 687.
- Garcia-Guzman, M. et al. (1995) Eur. J. Neurosci. 7, 647.
- McCann, C.M. et al. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 5149.
Scientific background
α-Bungarotoxin isoform A31 is a 74 amino acid peptidyl toxin isolated from the venom of the banded krait snake, Bungarus multicinctus1.
α-Bungarotoxin blocks postsynaptic neuromuscular transmission via competitive inhibition of nicotinic ACh receptors (nAChRs) with an IC50 of 3.5 x 10-10 M, thereby preventing the depolarizing action on postsynaptic membranes and blocking neuromuscular transmission2.
The toxin is selective for α7 receptors (IC50 value of 1.6 nM) and α3/β4 receptors (IC50 value of >3 µM)3,4.
α-Bungarotoxin also binds to and blocks a subset of GABAA receptors (GABAARs) that contain the GABAAR β3 subunit. In particular, α-Bungarotoxin blocks GABAARs that contain interfaces between adjacent β3 subunits5.
Target α7, α1/β1/γ/δ nAChR, GABA(A) receptor subtypes
Peptide Content: 100%
Lyophilized Powder
α-Bungarotoxin (#B-100) is a highly pure, natural, and biologically active peptide toxin.
For research purposes only, not for human use
Last Update: 18/11/2024
Applications
Citations
Citations
Powered by BiozProduct citations
- Nishioka, T. et al. (2019) Biochem. Biophys. Res. Commun. 509, 514.
- Kiss, T. et al. (2014) PLoS ONE 9, e109538.
- Wen, H. et al. (2013) eLife 2, e01206.
