ns309 (Alomone Labs)
Structured Review

Ns309, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ns309/NS-309/pmc12804778-222-0-8
Average 94 stars, based on 9 article reviews
Images
1) Product Images from "Structural basis for the subtype-selectivity of K Ca 2.2 channel activators"
Article Title: Structural basis for the subtype-selectivity of K Ca 2.2 channel activators
Journal: Nature Communications
doi: 10.1038/s41467-025-67232-3
Figure Legend Snippet: a Cryo-EM densities for Ca 2+ and NS309 bound to one CaM molecule in NS309_K Ca 2.2 are shown as blue and green mesh contoured at σ = 6, respectively. b Cryo-EM densities for Ca 2+ and NS309 bound to one CaM molecule in NS309_K Ca 3.1 are shown as magenta mesh contoured at σ = 6. c Intracellular view of NS309_K Ca 2.2 (K Ca 2.2: purple cartoon/CaM: light blue surface). The CaM N-lobes are positioned far apart, and the HC helices are not visible probably due to flexibility. d Intracellular view of NS309_K Ca 3.1 (K Ca 3.1: salmon cartoon/CaM: cyan surface). The CaM N-lobes are positioned close to each other, which stabilize the HC helices in the center.
Techniques Used: Cryo-EM Sample Prep
Figure Legend Snippet: a Binding energy between NS309 and amino acid residues in CaM and the S 45 A helix of K Ca 2.2. b Binding energy between NS309 and amino acid residues in CaM and the S 45 A helix of K Ca 3.1. The binding energy between NS309 and the four subunits of the activator-bound structure include van der Waals forces (VDW, black) and electrostatic interactions (Electrostatic, red). Data are presented as mean ± SD (n = 4 channel subunits). c Responses of WT and mutant K Ca 2.2 channels to NS309 in whole-cell patch-clamp recordings in the presence of 0.25 μM Ca 2+ . d Responses of WT and mutant K Ca 3.1 channels to NS309 in whole-cell patch clamp recordings in the presence of 0.25 μM Ca 2+ . Data are presented as mean ± SD (n = 4 transfected cells). e Total binding energy of NS309 to binding pockets in NS309_K Ca 2.2 and NS309_K Ca 3.1, including van der Waals forces (VDW, black) and electrostatic interactions (Electrostatic, red). Data are presented as mean ± SD (n = 4 channel subunits). f Chemical structure of NS309.
Techniques Used: Binding Assay, Mutagenesis, Patch Clamp, Transfection
Figure Legend Snippet: a Chemical structures of rimtuzalcap and CyPPA. b The binding pocket of rimtuzalcap in rimtuzalcap_K Ca 2.2_I (K Ca 2.2: green/CaM: yellow) superimposed onto the binding pocket of NS309 in NS309_K Ca 2.2 (K Ca 2.2: purple/CaM: light blue). Rimtuzalcap forms contacts with both the S 45 A and HA helices, while NS309 primarily interacts with the S 45 A helix. c Binding energy between rimtuzalcap and amino acid residues in CaM and the S 45 A helix of K Ca 2.2. The binding energy between rimtuzalcap and the four subunits of the activator-bound structure include van der Waals forces (VDW, black) and electrostatic interactions (Electrostatic, red). Data are presented as mean ± SD (n = 4 channel subunits).
Techniques Used: Binding Assay
Figure Legend Snippet: In side views, dimensions of the inner gate are measured as distances between Val391 in the transmembrane S6 helices of opposite K Ca 2.2 subunits in a apo_K Ca 2.2, b NS309_K Ca 2.2, c rimtuzalcap_K Ca 2.2_I, and d AP14145_K Ca 2.2 structures. Two opposite channel subunits are shown for clarity.
Techniques Used:
Related Articles
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