protx i  (Alomone Labs)


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    Alomone Labs protx i
    A,B,C, <t>ProTx</t> I Dose response (left), steady state inactivation (middle) and current voltage relations (right) for hCav3.1, hCav3.2 and hCav3.3, respectively. Steady state inactivation and current voltage relations were recorded prior and after application of 1 μM ProTx I. Ensemble dose response curves for tonic channel inhibition by ProTx I were fitted via the Hill equation and IC50’s for hCav3.1, 3.2 and 3.3 were 0.64, 94.6 and 5.4 μM respectively. Insets are representative current traces of each calcium channel before and after (red trace) application of 1 μM ProTx I (Note that the trace for hCav3.1 is the same as in figure 1 ). All other data were fitted with the Boltzmann equation and are from multiple paired experiments [n = 5-6 per channel]. Note the negative shift in both the half activation and steady state inactivation potential in the presence of 1 μM ProTx I for hCav3.2 despite this concentration having minimal effect on tonic block.
    Protx I, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protx i/product/Alomone Labs
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    protx i - by Bioz Stars, 2022-07
    85/100 stars

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    1) Product Images from "Block of T-type calcium channels by protoxins I and II"

    Article Title: Block of T-type calcium channels by protoxins I and II

    Journal: Molecular Brain

    doi: 10.1186/1756-6606-7-36

    A,B,C, ProTx I Dose response (left), steady state inactivation (middle) and current voltage relations (right) for hCav3.1, hCav3.2 and hCav3.3, respectively. Steady state inactivation and current voltage relations were recorded prior and after application of 1 μM ProTx I. Ensemble dose response curves for tonic channel inhibition by ProTx I were fitted via the Hill equation and IC50’s for hCav3.1, 3.2 and 3.3 were 0.64, 94.6 and 5.4 μM respectively. Insets are representative current traces of each calcium channel before and after (red trace) application of 1 μM ProTx I (Note that the trace for hCav3.1 is the same as in figure 1 ). All other data were fitted with the Boltzmann equation and are from multiple paired experiments [n = 5-6 per channel]. Note the negative shift in both the half activation and steady state inactivation potential in the presence of 1 μM ProTx I for hCav3.2 despite this concentration having minimal effect on tonic block.
    Figure Legend Snippet: A,B,C, ProTx I Dose response (left), steady state inactivation (middle) and current voltage relations (right) for hCav3.1, hCav3.2 and hCav3.3, respectively. Steady state inactivation and current voltage relations were recorded prior and after application of 1 μM ProTx I. Ensemble dose response curves for tonic channel inhibition by ProTx I were fitted via the Hill equation and IC50’s for hCav3.1, 3.2 and 3.3 were 0.64, 94.6 and 5.4 μM respectively. Insets are representative current traces of each calcium channel before and after (red trace) application of 1 μM ProTx I (Note that the trace for hCav3.1 is the same as in figure 1 ). All other data were fitted with the Boltzmann equation and are from multiple paired experiments [n = 5-6 per channel]. Note the negative shift in both the half activation and steady state inactivation potential in the presence of 1 μM ProTx I for hCav3.2 despite this concentration having minimal effect on tonic block.

    Techniques Used: Inhibition, Activation Assay, Concentration Assay, Blocking Assay

    Tonic block of mouse neuronal or human Cav3.X [T-type] calcium channels induced by either 1 μM application of ProTx I or 1 μM application of ProTx II. For recordings from native channels, ProTx I was tested on mouse thalamic neurons, ProTx II was tested on mouse DRG neurons, which respectively, expressed Cav3.1 and Cav3.2 channels. Shown are representative current traces from these experiments showing similar ProTx I block of native thalamic mouse T-type currents (first trace) and recombinant human Cav3.1 (second trace), and similar ProTx II block of mouse DRG T-type current (third trace) and recombinant human Cav3.2 (fourth trace) (control traces are depicted in black). Error bars reflect standard errors, asterisks denote statistical significance relative to either hCav3.1 [ProTx I] or hCav3.2 [ProTx II] [*p
    Figure Legend Snippet: Tonic block of mouse neuronal or human Cav3.X [T-type] calcium channels induced by either 1 μM application of ProTx I or 1 μM application of ProTx II. For recordings from native channels, ProTx I was tested on mouse thalamic neurons, ProTx II was tested on mouse DRG neurons, which respectively, expressed Cav3.1 and Cav3.2 channels. Shown are representative current traces from these experiments showing similar ProTx I block of native thalamic mouse T-type currents (first trace) and recombinant human Cav3.1 (second trace), and similar ProTx II block of mouse DRG T-type current (third trace) and recombinant human Cav3.2 (fourth trace) (control traces are depicted in black). Error bars reflect standard errors, asterisks denote statistical significance relative to either hCav3.1 [ProTx I] or hCav3.2 [ProTx II] [*p

    Techniques Used: Blocking Assay, Recombinant

    Tonic block of hCav3.1-hCav3.3chimeras by 1 μM application of ProTx I. Chimera nomenclature is as follows: hCav3.1 sequence in domains I-IV is denoted by “G”, hCav3.3 sequence is denoted by “I”. Note that block of hCav3.1 and Chimeras that contain Domain IV of hCav3.1 are similar (see top dashed line). The bottom slashed line represents percent tonic block of 1 μM ProTx I of wild type hCav3.3. [n = 5-6 per channel, at 1 μM]. Error bars reflect standard errors, asterisks denote statistical significance relative to hCav3.1 [*p
    Figure Legend Snippet: Tonic block of hCav3.1-hCav3.3chimeras by 1 μM application of ProTx I. Chimera nomenclature is as follows: hCav3.1 sequence in domains I-IV is denoted by “G”, hCav3.3 sequence is denoted by “I”. Note that block of hCav3.1 and Chimeras that contain Domain IV of hCav3.1 are similar (see top dashed line). The bottom slashed line represents percent tonic block of 1 μM ProTx I of wild type hCav3.3. [n = 5-6 per channel, at 1 μM]. Error bars reflect standard errors, asterisks denote statistical significance relative to hCav3.1 [*p

    Techniques Used: Blocking Assay, Sequencing

    A Sequence alignment of the human sodium channel 1.7 (hNav1.7) versus the three T-type calcium channels (sites targeted with mutagenesis highlighted in red). B , Tonic block of human Cav3.1 and Cav3.1 mutants induced by 1 μM application of ProTx I. Domain II mutations are denoted in blue, Domain IV mutations are shown in red [n = 5-6 per channel, at 1 μM]. Note that the last three mutations in Domain IV produced a non-functional channel (NF). Error bars reflect standard errors. Currents were elicited by stepping from a holding potential of −110 mV to a test potential of −20 mV.
    Figure Legend Snippet: A Sequence alignment of the human sodium channel 1.7 (hNav1.7) versus the three T-type calcium channels (sites targeted with mutagenesis highlighted in red). B , Tonic block of human Cav3.1 and Cav3.1 mutants induced by 1 μM application of ProTx I. Domain II mutations are denoted in blue, Domain IV mutations are shown in red [n = 5-6 per channel, at 1 μM]. Note that the last three mutations in Domain IV produced a non-functional channel (NF). Error bars reflect standard errors. Currents were elicited by stepping from a holding potential of −110 mV to a test potential of −20 mV.

    Techniques Used: Sequencing, Mutagenesis, Blocking Assay, Produced, Functional Assay

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    Alomone Labs protx i
    A,B,C, <t>ProTx</t> I Dose response (left), steady state inactivation (middle) and current voltage relations (right) for hCav3.1, hCav3.2 and hCav3.3, respectively. Steady state inactivation and current voltage relations were recorded prior and after application of 1 μM ProTx I. Ensemble dose response curves for tonic channel inhibition by ProTx I were fitted via the Hill equation and IC50’s for hCav3.1, 3.2 and 3.3 were 0.64, 94.6 and 5.4 μM respectively. Insets are representative current traces of each calcium channel before and after (red trace) application of 1 μM ProTx I (Note that the trace for hCav3.1 is the same as in figure 1 ). All other data were fitted with the Boltzmann equation and are from multiple paired experiments [n = 5-6 per channel]. Note the negative shift in both the half activation and steady state inactivation potential in the presence of 1 μM ProTx I for hCav3.2 despite this concentration having minimal effect on tonic block.
    Protx I, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protx i/product/Alomone Labs
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    protx i - by Bioz Stars, 2022-07
    85/100 stars
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    A,B,C, ProTx I Dose response (left), steady state inactivation (middle) and current voltage relations (right) for hCav3.1, hCav3.2 and hCav3.3, respectively. Steady state inactivation and current voltage relations were recorded prior and after application of 1 μM ProTx I. Ensemble dose response curves for tonic channel inhibition by ProTx I were fitted via the Hill equation and IC50’s for hCav3.1, 3.2 and 3.3 were 0.64, 94.6 and 5.4 μM respectively. Insets are representative current traces of each calcium channel before and after (red trace) application of 1 μM ProTx I (Note that the trace for hCav3.1 is the same as in figure 1 ). All other data were fitted with the Boltzmann equation and are from multiple paired experiments [n = 5-6 per channel]. Note the negative shift in both the half activation and steady state inactivation potential in the presence of 1 μM ProTx I for hCav3.2 despite this concentration having minimal effect on tonic block.

    Journal: Molecular Brain

    Article Title: Block of T-type calcium channels by protoxins I and II

    doi: 10.1186/1756-6606-7-36

    Figure Lengend Snippet: A,B,C, ProTx I Dose response (left), steady state inactivation (middle) and current voltage relations (right) for hCav3.1, hCav3.2 and hCav3.3, respectively. Steady state inactivation and current voltage relations were recorded prior and after application of 1 μM ProTx I. Ensemble dose response curves for tonic channel inhibition by ProTx I were fitted via the Hill equation and IC50’s for hCav3.1, 3.2 and 3.3 were 0.64, 94.6 and 5.4 μM respectively. Insets are representative current traces of each calcium channel before and after (red trace) application of 1 μM ProTx I (Note that the trace for hCav3.1 is the same as in figure 1 ). All other data were fitted with the Boltzmann equation and are from multiple paired experiments [n = 5-6 per channel]. Note the negative shift in both the half activation and steady state inactivation potential in the presence of 1 μM ProTx I for hCav3.2 despite this concentration having minimal effect on tonic block.

    Article Snippet: Both ProTx I and ProTx II were purchased from Alomone Labs (Jerusalem, Israel) and were dissolved in external recording solution at the stock concentration of 1 mM.

    Techniques: Inhibition, Activation Assay, Concentration Assay, Blocking Assay

    Tonic block of mouse neuronal or human Cav3.X [T-type] calcium channels induced by either 1 μM application of ProTx I or 1 μM application of ProTx II. For recordings from native channels, ProTx I was tested on mouse thalamic neurons, ProTx II was tested on mouse DRG neurons, which respectively, expressed Cav3.1 and Cav3.2 channels. Shown are representative current traces from these experiments showing similar ProTx I block of native thalamic mouse T-type currents (first trace) and recombinant human Cav3.1 (second trace), and similar ProTx II block of mouse DRG T-type current (third trace) and recombinant human Cav3.2 (fourth trace) (control traces are depicted in black). Error bars reflect standard errors, asterisks denote statistical significance relative to either hCav3.1 [ProTx I] or hCav3.2 [ProTx II] [*p

    Journal: Molecular Brain

    Article Title: Block of T-type calcium channels by protoxins I and II

    doi: 10.1186/1756-6606-7-36

    Figure Lengend Snippet: Tonic block of mouse neuronal or human Cav3.X [T-type] calcium channels induced by either 1 μM application of ProTx I or 1 μM application of ProTx II. For recordings from native channels, ProTx I was tested on mouse thalamic neurons, ProTx II was tested on mouse DRG neurons, which respectively, expressed Cav3.1 and Cav3.2 channels. Shown are representative current traces from these experiments showing similar ProTx I block of native thalamic mouse T-type currents (first trace) and recombinant human Cav3.1 (second trace), and similar ProTx II block of mouse DRG T-type current (third trace) and recombinant human Cav3.2 (fourth trace) (control traces are depicted in black). Error bars reflect standard errors, asterisks denote statistical significance relative to either hCav3.1 [ProTx I] or hCav3.2 [ProTx II] [*p

    Article Snippet: Both ProTx I and ProTx II were purchased from Alomone Labs (Jerusalem, Israel) and were dissolved in external recording solution at the stock concentration of 1 mM.

    Techniques: Blocking Assay, Recombinant

    Tonic block of hCav3.1-hCav3.3chimeras by 1 μM application of ProTx I. Chimera nomenclature is as follows: hCav3.1 sequence in domains I-IV is denoted by “G”, hCav3.3 sequence is denoted by “I”. Note that block of hCav3.1 and Chimeras that contain Domain IV of hCav3.1 are similar (see top dashed line). The bottom slashed line represents percent tonic block of 1 μM ProTx I of wild type hCav3.3. [n = 5-6 per channel, at 1 μM]. Error bars reflect standard errors, asterisks denote statistical significance relative to hCav3.1 [*p

    Journal: Molecular Brain

    Article Title: Block of T-type calcium channels by protoxins I and II

    doi: 10.1186/1756-6606-7-36

    Figure Lengend Snippet: Tonic block of hCav3.1-hCav3.3chimeras by 1 μM application of ProTx I. Chimera nomenclature is as follows: hCav3.1 sequence in domains I-IV is denoted by “G”, hCav3.3 sequence is denoted by “I”. Note that block of hCav3.1 and Chimeras that contain Domain IV of hCav3.1 are similar (see top dashed line). The bottom slashed line represents percent tonic block of 1 μM ProTx I of wild type hCav3.3. [n = 5-6 per channel, at 1 μM]. Error bars reflect standard errors, asterisks denote statistical significance relative to hCav3.1 [*p

    Article Snippet: Both ProTx I and ProTx II were purchased from Alomone Labs (Jerusalem, Israel) and were dissolved in external recording solution at the stock concentration of 1 mM.

    Techniques: Blocking Assay, Sequencing

    A Sequence alignment of the human sodium channel 1.7 (hNav1.7) versus the three T-type calcium channels (sites targeted with mutagenesis highlighted in red). B , Tonic block of human Cav3.1 and Cav3.1 mutants induced by 1 μM application of ProTx I. Domain II mutations are denoted in blue, Domain IV mutations are shown in red [n = 5-6 per channel, at 1 μM]. Note that the last three mutations in Domain IV produced a non-functional channel (NF). Error bars reflect standard errors. Currents were elicited by stepping from a holding potential of −110 mV to a test potential of −20 mV.

    Journal: Molecular Brain

    Article Title: Block of T-type calcium channels by protoxins I and II

    doi: 10.1186/1756-6606-7-36

    Figure Lengend Snippet: A Sequence alignment of the human sodium channel 1.7 (hNav1.7) versus the three T-type calcium channels (sites targeted with mutagenesis highlighted in red). B , Tonic block of human Cav3.1 and Cav3.1 mutants induced by 1 μM application of ProTx I. Domain II mutations are denoted in blue, Domain IV mutations are shown in red [n = 5-6 per channel, at 1 μM]. Note that the last three mutations in Domain IV produced a non-functional channel (NF). Error bars reflect standard errors. Currents were elicited by stepping from a holding potential of −110 mV to a test potential of −20 mV.

    Article Snippet: Both ProTx I and ProTx II were purchased from Alomone Labs (Jerusalem, Israel) and were dissolved in external recording solution at the stock concentration of 1 mM.

    Techniques: Sequencing, Mutagenesis, Blocking Assay, Produced, Functional Assay