| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Omega-agatoxin-Aa4a, ω-AGTX-Aa4a, ω-Aga-IVA, ω-agatoxin-4A |
| Concentration | |
| Conjugate | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Reconstitution | |
| Solubility | The product is lyophilized in 0.5 ml conical vial.Centrifuge the vial before adding solvent (10,000 x g for 5 minutes). The lyophilizate may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. Soluble in pure water at 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 100-1000x of the final working concentration. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. Centrifuge all product preparations at 10,000 x g for 5 minutes before use. It is recommended to prepare fresh solutions in working buffers just before use. Avoid multiple freeze-thaw cycles to maintain biological activity. Avoid exposure to light |
| Source | Modified synthetic peptide |
| Species | |
| Storage | |
| Target |
Overview
ω-Agatoxin IVA-ATTO Fluor-647N is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to P-type Ca2+ channels 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: ~6144 Da.
- Source / origin: Agelenopsis aperta (North American funnel-web spider) (Agelenopsis gertschi).
- Quality attributes: Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys4-Cys20, Cys12-Cys25, Cys19-Cys36 and Cys27-Cys34 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
Native ω-Agatoxin IVA (ω-Aga-IVA) was originally isolated from Agelenopsis aperta spider venom, and was shown to be a selective blocker of CaV2.1 (P/Q type) channels1. However, the sensitivity depends on the auxiliary b subunit isoform2 and on the splice variant3. Therefore, the effective concentration varies between systems. In accordance, the toxin blocks presynaptic Ca2+ currents and synaptic transmission in a variety of synapses4,5. ω-Agatoxin IVA is widely used in electrophysiological measurements of cloned and native channels6,7. It is used to assess the role of CaV2.1 channels in synaptic transmission4. In addition, it was used to map the spatial distribution of CaV2.1 channels in mouse cerebellar and hippocampal brain slices8.
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.
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Stephens, G.J.
et al. (2001) Eur. J. Neurosci. 13, 1902.
Mintz, I.M.
et al. (1992) Nature 355, 827.
Moreno, H.
et al. (1997) Proc. Natl. Acad. Sci. 94, 14042.
Bourinet, E.
et al. (1999) Nat. Neurosci. 2, 407.
Meir, A.
et al. (1999) Physiol. Rev. 79, 1019.
Stephens, G.J.
et al. (2001) Eur. J. Neurosci. 13, 1902.
Berrow, N.S.
et al. (1997) Eur. J. Neurosci. 9, 739.
Pearson, H.A.
et al. (1995) J. Physiol. 482, 493.
Nakanishi, S.
et al. (1995) J. Neurosci. Res. 41, 532.
Mintz, I.
et al. (1992) Nature 355, 827.
Meir, A.
et al. (1999) Physiol. Rev.79, 1019.
