| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | SNX-230, Omega-CgTxMVIIC, Omega-conotoxin MVIIC, P/Q-type Ca2+ channels |
| Concentration | |
| Conjugate | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Reconstitution | |
| Source | Modified synthetic peptide |
| Species | |
| Storage | |
| Target |
Overview
ω-Conotoxin MVIIC-ATTO Fluor 647N is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to N-type and P/Q-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: 3376 Da.
- Source / origin: Conus magus (Magical cone).
- Quality attributes: Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys1-Cys16, Cys8-Cys20 and Cys15-Cys26Cys26 - C-terminal amidation 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
ω-Conotoxin MVIIC blocks CaV2.1 (α1A, P/Q-type) and CaV2.2 (α1B, N-type) channels.1 The toxin binds with high affinity to CaV2.1 and with lower affinity to CaV2.2 in rabbit brain.2 However, the block by ω-Conotoxin-MVIIC of N-type channels in DRG neurons developed much faster than the block of P-type currents in Purkinje cells.1 The effect of the toxin is modulated by voltage (i.e. it is more potent for inactivated channels).3 In addition, this toxin was reported to block nicotinic receptors (transiently expressed in Xenopus oocytes) with IC50 of 1.3 µM.4 It was also shown to inhibit K+-induced 3H-GABA release in hippocampus in vivo.5 This effect was with high affinity (50% block, 200 nM). The toxin was used to inhibit synaptic transmission in several peripheral preparations.6,7
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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Herrero, C.J.
et al. (1999) Br. J. Pharmacol.127, 1375.
McDonough, S.I.
et al. (1996) J. Neurosci.16, 2612.
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Herrero, C.J.
et al. (1999) Br. J. Pharmacol.127, 1375.
Newcomb, R. and Palma, A.
(1994) Brain. Res. 638, 95.
Vega, T.
et al. (1995) Eur. J. Pharmacol.276, 231.
Hirata, H.
et al. (1997) Eur. J. Pharmacol.321, 217.
McDonough, S.I.
et al. (1996) J. Neurosci.16, 2612.
