Home>>8-DY547-cGMP

8-DY547-cGMP

目录号 : GC42625

通过结合环核苷酸激活,环核苷酸门控 (CNG) 离子通道介导光感受器和嗅觉细胞中的感觉信号转导。

8-DY547-cGMP Chemical Structure

规格 价格 库存 购买数量
50μg
¥2,091.00
现货
100μg
¥3,975.00
现货

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Sample solution is provided at 25 µL, 10mM.

产品文档

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产品描述

Through activation by the binding of cyclic nucleotides, cyclic nucleotide-gated (CNG) ion channels mediate sensory signal transduction in photoreceptors and olfactory cells. 8-DY547-cGMP is a fluorescently-labeled cyclic nucleotide that can be used to study CNGA2 channel activation. 8-DY547-cGMP and cGMP open the channel with equal efficiency and control of the channel activity is rapid and reversible. The difference in fluorescence (δF) can be determined by using DY647.

Chemical Properties

Cas No. N/A SDF
Canonical SMILES CC[N+](C(C=C(S(=O)([O-])=O)C=C1)=C1C2(C)C)=C2/C=C/C=C3C(CCCC(NCCSC4NC(C(NC(N)=N5)=O)C5N4C6OC(COP(O7)([O-])=O)C7C6O)=O)(C)C(C=C(S(=O)([O-])=O)C=C8)C8N/3CC.[Na+].[Na+]
分子式 C42H55N8O14PS3•2Na 分子量 1069.1
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 0.9354 mL 4.6768 mL 9.3537 mL
5 mM 0.1871 mL 0.9354 mL 1.8707 mL
10 mM 0.0935 mL 0.4677 mL 0.9354 mL
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Research Update

Relating ligand binding to activation gating in CNGA2 channels

Nature 2007 Mar 22;446(7134):440-3.PMID:17322905DOI:10.1038/nature05596

Cyclic nucleotide-gated (CNG) ion channels mediate sensory signal transduction in photoreceptors and olfactory cells. Structurally, CNG channels are heterotetramers composed of either two or three homologue subunits. Although it is well established that activation is a cooperative process of these subunits, it remains unknown whether the cooperativity is generated by the ligand binding, the gating, or both, and how the subunits interact. In this study, the action of homotetrameric olfactory-type CNGA2 channels was studied in inside-out membrane patches by simultaneously determining channel activation and ligand binding, using the fluorescent cGMP analogue 8-DY547-cGMP as the ligand. At concentrations of 8-DY547-cGMP < 1 microM, steady-state binding was larger than steady-state activation, whereas at higher concentrations it was smaller, generating a crossover of the steady-state relationships. Global analysis of these relationships together with multiple activation time courses following cGMP jumps showed that four ligands bind to the channels and that there is significant interaction between the binding sites. Among the binding steps, the second is most critical for channel opening: its association constant is three orders of magnitude smaller than the others and it triggers a switch from a mostly closed to a maximally open state. These results contribute to unravelling the role of the subunits in the cooperative mechanism of CNGA2 channel activation and could be of general relevance for the action of other ion channels and receptors.