α-Conotoxin GI-FITC

SKU:BHP21300171 Toxins and Venom Peptides
Suppliers
Alomone Labs
Alomone Labs
Details Products
Overview
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α-Conotoxin GI-FITC is a reagent targeting GI-FITC. Key specifications include Source: Conus geographus (Geography cone) (Nubecula geographus); Conjugate: FITC; Form: Lyophilized; MW: 1827 Da. Commonly used in neuroscience studies, including measure gi-fitc modulation in patch-clamp electrophysiology (dose–response) and profile gi-fitc pharmacology in cell-based assays (concentration–response + time-course).
Target GI-FITC
conjugate(s) FITC
Species Conus geographus (Geography cone) (Nubecula geographus)
Molecular Weight 1827 Da
Form Lyophilized
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options:
    Size (2) - 10 mcg, 5 mcg
    Quantity (4) - 1, 2, 5, 10
  • Lead time: typically ships in ~1-2 business days; timing may vary by selected option.
  • Storage: Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Avoid exposure to light. Storage after reconstitution: Store the reconstituted solution at -20°C for the shortest time possible. Avoid multiple freeze-thaw cycles. We do not recommend storing the product in working solutions for longer than a day. Avoid exposure to light. Storage of solutions: Store the reconstituted solution at -20°C for the shortest time possible. Avoid multiple freeze-thaw cycles. We do not recommend storing the product in working solutions for longer than a day. Avoid exposure to light.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No STC-500-F
Activity
  • α-Conotoxin GI inhibits α/δ site on mouse muscle-derived BC3H-1 nicotinic acetylcholine receptors (nAChR) expressed on postsynaptic membranes. Other site (α/γ site) on nicotinic receptors from Torpedo californica electric organ is also inhibited by α-Conotoxin GI1
  • 2.
Alternative Names G1, Alpha-conotoxin GI
Concentration 400 nM- 4 µM
Conjugate
  • FITC
Form Lyophilized
Formulation Lyophilized from double distilled water (ddH2O). May contain TFA as a residual counter ion.
Gene ID CHRNA1,CHRNB1,CHRND,CHRNG, CHRNE
Molecular Weight 1827 Da
Product Type
  • Proteins & Peptides
  • Proteins
  • Toxins
Reconstitution Centrifuge the vial (10,000 × g for 5 minutes) before adding solvent to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Gently tap, tilt, and roll the vial to aid dissolution. Avoid vigorous vortexing; light vortexing for up to 3 seconds is acceptable if needed. The product is lyophilized in 0.5 ml conical vial. The product is soluble in pure water to high-micromolar concentrations (5 µM - 1 mM). For long-term storage in solution, we recommend preparing 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 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 Conus geographus (Geography cone) (Nubecula geographus)
Storage Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Avoid exposure to light. Storage after reconstitution: Store the reconstituted solution at -20°C for the shortest time possible. Avoid multiple freeze-thaw cycles. We do not recommend storing the product in working solutions for longer than a day. Avoid exposure to light. Storage of solutions: Store the reconstituted solution at -20°C for the shortest time possible. Avoid multiple freeze-thaw cycles. We do not recommend storing the product in working solutions for longer than a day. Avoid exposure to light.
Target α1/β1/δ/γ nAChR

Overview

α-Conotoxin GI-FITC is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to α1/β1/δ/γ nAChR biology and/or assay development. The reagent is provided as a FITC 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, Immunofluorescence, Fluorescence staining, Direct flow cytometry.

Key elements and design rationale

  • Molecular identity: MW: 1827 Da.
  • Source / origin: Conus geographus (Geography cone) (Nubecula geographus).
  • Quality attributes: Bioassay tested: Yes; Sterile / endotoxin-free: No.

Modifications

Cys13 - C-terminal amidation Disulfide bonds between: Cys2-Cys7, Cys3-Cys13FITC

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-Conotoxin GI is a 13 amino acid peptidyl toxin isolated from the Conus geographus (Geography cone) venom1,2,3. It belongs to the Conotoxin A superfamily and reversibly blocks α/δ nicotinic ACh channel receptors (nAChR). α-Conotoxin GI reversibly inhibits the high affinity α/δ site on mouse muscle-derived BC3H-1 receptor, a nAChR expressed on postsynaptic membranes4,5. Other low site (α/γ site) on nicotinic receptors from Torpedo californica electric organ is also inhibited by α-Conotoxin GI5.

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.
  • 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.

Groebe, D.R.

et al. (1997) Biochemistry 36, 6469.

Gray, W.R.

et al. (1981) The J. Biol. Chem. 256, 4734.

Nishiuchi, Y. and Sakakibara, S.

(1982) FEBS LETT.148, 260.

Guddat, L.W.

et al. (1996) Biochemistry35, 11329.

Groebe, D.R.

et al. (1995) Mol. Pharmacol.48, 105.

Groebe, D.R.

et al. (1997) Biochemistry 36, 6469.

Groebe, D.R.

et al. (1995) Mol. Pharmacol. 48, 105.

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