Overview
- 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.
- Live cell imaging of α-Bungarotoxin-ATTO Fluor-647N in differentiated PC-12 cells.Neurite outgrowth was induced in PC12 cells through 8 days exposure to 100 ng/ml Native mouse NGF 2.5S protein (99%) (#N-240). (A) CellMask™ Actin 1X solution was applied for 30 minutes, resulting in a green fluorescence to visualize cellular membrane. (B) Following this, the same cells underwent incubation with 0.1 µM of α-Bungarotoxin-ATTO Fluor-647N for 60 minutes at 37ºC, followed by PBSX1 wash, leading to red fluorescence indicative of the distribution of nicotinic ACh channels. (C) Live imaging of the differentiated PC-12 cells allowed observation of α-Bungarotoxin distribution among the cells.
- Unlabeled α-Bungarotoxin successfully blocks nicotinic ACh channels access.Neurite outgrowth was induced in PC12 cells through 8 days exposure to 100 ng/ml Native mouse NGF 2.5S protein (99%) (#N-240). (A) CellMask™ Actin 1X solution was applied for 30 minutes, resulting in a green fluorescence to visualize cellular membrane. (B) Following this, the same cells underwent incubation with 10 µM of α-Bungarotoxin (#B-100) for 30 minutes at 37ºC, followed by incubation with 0.1 µM of α-Bungarotoxin-ATTO Fluor-647N for 60 minutes at 37ºC, followed by PBSX1 wash. (C) Live imaging of differentiated PC-12 cells demonstrates that α-Bungarotoxin successfully competes with α-Bungarotoxin-ATTO Fluor-647N for binding sites of nicotinic ACh channels.
- Direct flow cytometry of α-Bungarotoxin in live intact rat PC-12 cells.___ PC-12 cells.
___ PC-12 cells + 0.1 µM α-Bungarotoxin (#B-100).
___ PC-12 cells + 0.1 µM α-Bungarotoxin-ATTO Fluor-647N (#B-100-FRN). - Direct flow cytometry of α-Bungarotoxin in PC-12-derived extracellular vesicles (EVs).___ PC-12-derived EVs.
___ PC-12-derived EVs + 0.1 µM α-Bungarotoxin (#B-100).
___ PC-12-derived EVs + 0.1 µM α-Bungarotoxin-ATTO Fluor-647N (#B-100-FRN). - Alomone Labs α-Bungarotoxin-ATTO Fluor-647N inhibits α7 nAChR heterologously expressed in Xenopus oocytes.A. Time course of α-Bungarotoxin-ATTO Fluor-647N (#B-100-FRN) action on α7 nAChR currents, elicited every 50 sec by a transient application of 400 µM ACh + 0.3 µM PNU-120596, while membrane potential was held at -80 mV. Application of 10 nM (green) α-Bungarotoxin-ATTO Fluor-647N significantly inhibits the currents. B. Superimposed traces of α7 nAChR currents upon application of control and 10nM (green) α-Bungarotoxin-ATTO Fluor-647N (taken from the recording in A).
- 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.
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.
α-Bungarotoxin-ATTO Fluor-647N (#B-100-FRN) is a highly pure, natural, and biologically active conjugated peptide toxin.
Benefits of α-Bungarotoxin-ATTO Fluor-647N:
✓ Localization and distribution
✓ Live cell imaging
✓ Single cell detection
✓ Direct flow cytometry
✓ Binding kinetics
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