| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Long neurotoxin 1, α-Bgtx, α-BuTX, α1/β1/γ/δ nAChR, GABA(A) receptor subtypes |
| Concentration | |
| Conjugate | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Reconstitution | |
| Solubility | The product is lyophilized in 0.5 ml conical vial.Centrifuge all products BEFORE adding solvent (10,000 x g for 5 minutes). The preparation of fresh solutions in working buffers before use is recommended. Soluble in pure water to high-micromolar concentrations (50 µM-1 mM). For long-term storage in solution, it is recommended to prepare a stock solution by dissolving the product in double distilled water (ddH2O) at a concentration between x100-1000 of the final working concentration. Divide the solution into single-use aliquots and store at -20°C. Before use, thaw the relevant vial(s) intended for use and dilute in the desired working buffer. Avoid multiple freeze-thaw cycles to maintain toxin activity |
| Source | Modified natural protein |
| Species | |
| Storage | |
| Target |
Overview
α-Bungarotoxin-ATTO Fluor-647N is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to α7, α1/β1/γ/δ nAChR and GABA(A) receptor subtypes biology and/or assay development. The reagent is provided as a ATTO Fluor-647N conjugate, supporting detection or imaging workflows where applicable. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Electrophysiology, Live cell imaging, Immunofluorescence, Fluorescence staining, Direct flow cytometry.
Key elements and design rationale
- Molecular identity: MW: ~ 8925 Da.
- Source / origin: Modified natural protein isolated from Bungarus multicinctus (Many-banded krait)..
- Quality attributes: Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys3-Cys23, Cys16-Cys44, Cys29-Cys33, Cys48-Cys and Cys60-Cys65 ATTO Fluor-647N
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological 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.
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Electrophysiology: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Live cell imaging: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Immunofluorescence: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Fluorescence staining: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Direct flow cytometry: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
McCann, C.M.
et al. (2006) Proc. Natl. Acad. Sci. U.S.A.103, 5149.
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.
Wilson, S.P. and Kirshner, N.
(1977) J. Neurochem.28, 687.
Garcia-Guzman, M.
et al. (1995) Eur. J. Neurosci.7, 647.
