r bayk 8644  (Alomone Labs)


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    Alomone Labs r bayk 8644
    The TCa V 1 channel has similar sensitivity to cadmium (Cd 2+ ) block as the rCa V 1.2 channel but is relatively insensitive to dihydropyridines. A , dose–response curve for block of average TCa V 1 and rCa V 1.2 peak macroscopic currents ±SD ( error bars ) with increasing concentrations of perfused external Cd 2+ ions. IC 50 and Hill coefficients ±SD are shown and were statistically indistinguishable between the two channels. B , plot of average percent block ±SD of peak macroscopic currents elicited by voltage steps to 0 mV for TCa V 1 and rCa V 1.2 upon external perfusion of 10 μM nifedipine, revealing complete block (99.7 ± 0.1%) for the rCa V 1.2 channel, as opposed to only 5.8 ± 3.6% block for TCa V 1 ( p = 0.029 using a two-tailed t test). C , plot of average percent block ±SD of peak macroscopic currents at 0 mV for TCa V 1 and rCa V 1.2 by external perfusion of 10 μM isradipine, revealing nearly complete block (95.0 ± 6.1%) for the rCa V 1.2 channel, as opposed to only 11.5 ± 2.2% block for TCa V 1 ( p = 0.003 using a two-tailed t test). D , top left , illustration of Ca V 1 channel protein highlighting regions that bear residues associated with high-affinity dihydropyridine binding ( red ). Top right , color-coding of phyla corresponding to the aligned Ca V 1 channel protein sequences shown below. Bottom , protein alignment of the DIII-S5, DIII pore-loop, DIII-S6, DIV pore-loop, and DIV-S6 regions of various Ca V 1 channels reveals presence/absence of key residues important for dihydropyridine binding. Blue and red chevrons reflect positions determined to be important for dihydropyridine block of mammalian and Lymnaea stagnalis channels, whereas green chevrons denote positions where TCa V 1 and cnidarian Ca V 1 channels differ from the mammalian and Lymnaea homologues. E , sample TCa V 1 and rCa V 1.2 current traces elicited by a voltage step from −100 mV to 0 mV with extracellular perfusion of 0 ( black ) or 5 μM S <t>(-)BayK</t> 8644 ( red ). F , plot of average fold-increase in current amplitude ±SD for TCa V 1 and rCa V 1.2 channels after application of 5 μM extracellular S (-)BayK 8644 agonist. Current amplitudes with 5 μM S (-)BayK 8644 were normalized to currents from the same cell prior to addition of the drug. Application of S (-)BayK 8644 caused a significantly greater increase in current for rCa V 1.2 compared to TCa V 1 ( p = 0.004 for two-tailed t test). G , dose–response curve for change in mean TCa V 1 and rCa V 1.2 peak macroscopic currents ±SD with increasing concentrations of R (+)BayK 8644, revealing that TCa V 1 is only blocked by this stereoisomer at high concentrations. Current amplitudes with R (+)BayK perfusion were normalized to currents from the same cell perfused with external solution lacking R (+)BayK. Uppercase and lowercase letters denote within-group significant differences ( p ≤ 0.003) and asterisks denote between-group ( i.e. , TCa V 1 versus rCa V 1.2) significant differences ( p ≤ 0.001) as determined by Holm–Sidak tests after a two-way ANOVA ( <xref ref-type=Table S1 ). For all experiments, the holding potential was −100 mV. DI to DIV, domains I to IV; rCa V , Rattus norvegicus voltage-gated calcium channel; TCa V , T. adhaerens voltage-gated calcium channel. " width="250" height="auto" />
    R Bayk 8644, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/r bayk 8644/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    r bayk 8644 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Divergent Ca 2+ /calmodulin feedback regulation of Ca V 1 and Ca V 2 voltage-gated calcium channels evolved in the common ancestor of Placozoa and Bilateria"

    Article Title: Divergent Ca 2+ /calmodulin feedback regulation of Ca V 1 and Ca V 2 voltage-gated calcium channels evolved in the common ancestor of Placozoa and Bilateria

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2022.101741

    The TCa V 1 channel has similar sensitivity to cadmium (Cd 2+ ) block as the rCa V 1.2 channel but is relatively insensitive to dihydropyridines. A , dose–response curve for block of average TCa V 1 and rCa V 1.2 peak macroscopic currents ±SD ( error bars ) with increasing concentrations of perfused external Cd 2+ ions. IC 50 and Hill coefficients ±SD are shown and were statistically indistinguishable between the two channels. B , plot of average percent block ±SD of peak macroscopic currents elicited by voltage steps to 0 mV for TCa V 1 and rCa V 1.2 upon external perfusion of 10 μM nifedipine, revealing complete block (99.7 ± 0.1%) for the rCa V 1.2 channel, as opposed to only 5.8 ± 3.6% block for TCa V 1 ( p = 0.029 using a two-tailed t test). C , plot of average percent block ±SD of peak macroscopic currents at 0 mV for TCa V 1 and rCa V 1.2 by external perfusion of 10 μM isradipine, revealing nearly complete block (95.0 ± 6.1%) for the rCa V 1.2 channel, as opposed to only 11.5 ± 2.2% block for TCa V 1 ( p = 0.003 using a two-tailed t test). D , top left , illustration of Ca V 1 channel protein highlighting regions that bear residues associated with high-affinity dihydropyridine binding ( red ). Top right , color-coding of phyla corresponding to the aligned Ca V 1 channel protein sequences shown below. Bottom , protein alignment of the DIII-S5, DIII pore-loop, DIII-S6, DIV pore-loop, and DIV-S6 regions of various Ca V 1 channels reveals presence/absence of key residues important for dihydropyridine binding. Blue and red chevrons reflect positions determined to be important for dihydropyridine block of mammalian and Lymnaea stagnalis channels, whereas green chevrons denote positions where TCa V 1 and cnidarian Ca V 1 channels differ from the mammalian and Lymnaea homologues. E , sample TCa V 1 and rCa V 1.2 current traces elicited by a voltage step from −100 mV to 0 mV with extracellular perfusion of 0 ( black ) or 5 μM S (-)BayK 8644 ( red ). F , plot of average fold-increase in current amplitude ±SD for TCa V 1 and rCa V 1.2 channels after application of 5 μM extracellular S (-)BayK 8644 agonist. Current amplitudes with 5 μM S (-)BayK 8644 were normalized to currents from the same cell prior to addition of the drug. Application of S (-)BayK 8644 caused a significantly greater increase in current for rCa V 1.2 compared to TCa V 1 ( p = 0.004 for two-tailed t test). G , dose–response curve for change in mean TCa V 1 and rCa V 1.2 peak macroscopic currents ±SD with increasing concentrations of R (+)BayK 8644, revealing that TCa V 1 is only blocked by this stereoisomer at high concentrations. Current amplitudes with R (+)BayK perfusion were normalized to currents from the same cell perfused with external solution lacking R (+)BayK. Uppercase and lowercase letters denote within-group significant differences ( p ≤ 0.003) and asterisks denote between-group ( i.e. , TCa V 1 versus rCa V 1.2) significant differences ( p ≤ 0.001) as determined by Holm–Sidak tests after a two-way ANOVA ( <xref ref-type=Table S1 ). For all experiments, the holding potential was −100 mV. DI to DIV, domains I to IV; rCa V , Rattus norvegicus voltage-gated calcium channel; TCa V , T. adhaerens voltage-gated calcium channel. " title="... 0 ( black ) or 5 μM S (-)BayK 8644 ( red ). F , plot of ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: The TCa V 1 channel has similar sensitivity to cadmium (Cd 2+ ) block as the rCa V 1.2 channel but is relatively insensitive to dihydropyridines. A , dose–response curve for block of average TCa V 1 and rCa V 1.2 peak macroscopic currents ±SD ( error bars ) with increasing concentrations of perfused external Cd 2+ ions. IC 50 and Hill coefficients ±SD are shown and were statistically indistinguishable between the two channels. B , plot of average percent block ±SD of peak macroscopic currents elicited by voltage steps to 0 mV for TCa V 1 and rCa V 1.2 upon external perfusion of 10 μM nifedipine, revealing complete block (99.7 ± 0.1%) for the rCa V 1.2 channel, as opposed to only 5.8 ± 3.6% block for TCa V 1 ( p = 0.029 using a two-tailed t test). C , plot of average percent block ±SD of peak macroscopic currents at 0 mV for TCa V 1 and rCa V 1.2 by external perfusion of 10 μM isradipine, revealing nearly complete block (95.0 ± 6.1%) for the rCa V 1.2 channel, as opposed to only 11.5 ± 2.2% block for TCa V 1 ( p = 0.003 using a two-tailed t test). D , top left , illustration of Ca V 1 channel protein highlighting regions that bear residues associated with high-affinity dihydropyridine binding ( red ). Top right , color-coding of phyla corresponding to the aligned Ca V 1 channel protein sequences shown below. Bottom , protein alignment of the DIII-S5, DIII pore-loop, DIII-S6, DIV pore-loop, and DIV-S6 regions of various Ca V 1 channels reveals presence/absence of key residues important for dihydropyridine binding. Blue and red chevrons reflect positions determined to be important for dihydropyridine block of mammalian and Lymnaea stagnalis channels, whereas green chevrons denote positions where TCa V 1 and cnidarian Ca V 1 channels differ from the mammalian and Lymnaea homologues. E , sample TCa V 1 and rCa V 1.2 current traces elicited by a voltage step from −100 mV to 0 mV with extracellular perfusion of 0 ( black ) or 5 μM S (-)BayK 8644 ( red ). F , plot of average fold-increase in current amplitude ±SD for TCa V 1 and rCa V 1.2 channels after application of 5 μM extracellular S (-)BayK 8644 agonist. Current amplitudes with 5 μM S (-)BayK 8644 were normalized to currents from the same cell prior to addition of the drug. Application of S (-)BayK 8644 caused a significantly greater increase in current for rCa V 1.2 compared to TCa V 1 ( p = 0.004 for two-tailed t test). G , dose–response curve for change in mean TCa V 1 and rCa V 1.2 peak macroscopic currents ±SD with increasing concentrations of R (+)BayK 8644, revealing that TCa V 1 is only blocked by this stereoisomer at high concentrations. Current amplitudes with R (+)BayK perfusion were normalized to currents from the same cell perfused with external solution lacking R (+)BayK. Uppercase and lowercase letters denote within-group significant differences ( p ≤ 0.003) and asterisks denote between-group ( i.e. , TCa V 1 versus rCa V 1.2) significant differences ( p ≤ 0.001) as determined by Holm–Sidak tests after a two-way ANOVA ( Table S1 ). For all experiments, the holding potential was −100 mV. DI to DIV, domains I to IV; rCa V , Rattus norvegicus voltage-gated calcium channel; TCa V , T. adhaerens voltage-gated calcium channel.

    Techniques Used: Blocking Assay, Two Tailed Test, Binding Assay

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