| Bioactivity | α-Conotoxin GID is a paralytic peptide neurotoxin and a selective antagonist of nAChR, with IC50s of 5 nM (α7), 3 nM (α3β2)， 150 nM (α4β2), respectively. α-Conotoxin GID is small disulfide-rich peptide, with potential to inhibit chronic pain. α-Conotoxin GID contains a C-terminal carboxylate, thus substitution with a C-terminal carboxamide results in loss of α4β2 nAChR. α-Conotoxin GID can be isolated from the Conus species[1][2][3]. |
| Target | IC50: 5 nM (α7), 3 nM (α3β2)， 150 nM (α4β2) |
| Name | α-Conotoxin GID |
| CAS | 547741-78-6 |
| Sequence | Ile-Arg-Asp-{Gla}-Cys-Cys-Ser-Asn-Pro-Ala-Cys-Arg-Val-Asn-Asn-{Hyp}-His-Val-Cys (Disulfide bridge：Cys5-Cys11, Cys6-Cys19) |
| Shortening | IRD-{Gla}-CCSNPACRVNN-{Hyp}-HVC (Disulfide bridge：Cys5-Cys11, Cys6-Cys19) |
| Formula | C84H132N30O31S4 |
| Molar Mass | 2186.39 |
| Transport | Room temperature in continental US; may vary elsewhere. |
| Storage | Please store the product under the recommended conditions in the Certificate of Analysis. |
| Reference | [1]. Armishaw CJ. Synthetic α-conotoxin mutants as probes for studying nicotinic acetylcholine receptors and in the development of novel drug leads. Toxins (Basel). 2010 Jun;2(6):1471-99. [2]. Millard EL, et al. Inhibition of neuronal nicotinic acetylcholine receptor subtypes by alpha-Conotoxin GID and analogues. J Biol Chem. 2009 Feb 20;284(8):4944-51. [3]. Nicke A, et al. Isolation, structure, and activity of GID, a novel alpha 4/7-conotoxin with an extended N-terminal sequence. J Biol Chem. 2003 Jan 31;278(5):3137-44. |
α-Conotoxin GID
CAS: 547741-78-6 F: C84H132N30O31S4 W: 2186.39
α-Conotoxin GID is a paralytic peptide neurotoxin and a selective antagonist of nAChR, with IC50s of 5 nM (α7), 3
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