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ca v 2.1 n283q mutant channel  (GenScript corporation)

 
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    GenScript corporation ca v 2.1 n283q mutant channel
    <t>N283Q</t> glycosylation site mutation reduces Ca 2+ current density through Ca V 2.1 channels heterologously expressed in HEK293 cells, without altering their voltage-dependent activation. ( A ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the decrease in Ca 2+ current density through Ca V 2.1 channels containing the mutation at the α 1A glycosylation site N283, which exhibit voltage dependence of activation similar to that of WT channels. Dotted lines mark the zero current level. Average Ca 2+ current density-voltage relationships ( B ) and normalized I-V curves ( C ) for WT (open circles, n = 13) and N283Q (filled dark cyan triangles, n = 19) Ca V 2.1 channels. N283Q reduces maximal Ca 2+ current density (obtained by membrane depolarization to +15 mV) from −69.4 ± 12.9 pA/pF ( n = 13) to −19.5 ± 3.2 pA/pF ( n = 19) ( p < 0.001, Mann-Whitney U -test). ( D ) N283Q mutation has no significant effect on the V 1/2 for Ca V 2.1 channel activation (estimated from normalized I-V curves shown in C as indicated in Materials and Methods, p = 0.798, Student’s t -test). ( E ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the shift of activation to lower depolarization induced by 0.6 μg/mL tunicamycin on N283Q mutant Ca V 2.1 channels containing β 3 and α 2 δ 1 subunits. The zero current level is indicated by dotted lines. Average Ca 2+ current density-voltage relationships ( F ) and normalized I-V curves ( G ) for N283Q mutant Ca V 2.1 channels expressed in DMSO-treated cells (filled cyan triangles, n = 10) and in cells treated with 0.6 μg/mL tunicamycin (filled green circles, n = 8). Peak Ca 2+ current density through N283Q Ca V 2.1 channels after vehicle (DMSO) and tunicamycin treatments were −23.3 ± 5.6 pA/pF ( n = 10) and −11.6 ± 3.6 pA/pF ( n = 8), respectively ( p = 0.06, Student’s t -test). ( H ) Reduction in V 1/2 for activation of Ca V 2.1 channels composed by N283Q mutant α 1A , β 3 and α 2 δ 1 subunits (estimated from normalized I-V curves shown in ( G ) as indicated in Materials and Methods) produced by 0.6 μg/mL tunicamycin ( n = 8). ** p < 0.01 versus the control condition (vehicle, n = 10; Student’s t -test).
    Ca V 2.1 N283q Mutant Channel, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ca v 2.1 n283q mutant channel/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    ca v 2.1 n283q mutant channel - by Bioz Stars, 2026-05
    90/100 stars

    Images

    1) Product Images from "Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy"

    Article Title: Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms19020619

    N283Q glycosylation site mutation reduces Ca 2+ current density through Ca V 2.1 channels heterologously expressed in HEK293 cells, without altering their voltage-dependent activation. ( A ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the decrease in Ca 2+ current density through Ca V 2.1 channels containing the mutation at the α 1A glycosylation site N283, which exhibit voltage dependence of activation similar to that of WT channels. Dotted lines mark the zero current level. Average Ca 2+ current density-voltage relationships ( B ) and normalized I-V curves ( C ) for WT (open circles, n = 13) and N283Q (filled dark cyan triangles, n = 19) Ca V 2.1 channels. N283Q reduces maximal Ca 2+ current density (obtained by membrane depolarization to +15 mV) from −69.4 ± 12.9 pA/pF ( n = 13) to −19.5 ± 3.2 pA/pF ( n = 19) ( p < 0.001, Mann-Whitney U -test). ( D ) N283Q mutation has no significant effect on the V 1/2 for Ca V 2.1 channel activation (estimated from normalized I-V curves shown in C as indicated in Materials and Methods, p = 0.798, Student’s t -test). ( E ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the shift of activation to lower depolarization induced by 0.6 μg/mL tunicamycin on N283Q mutant Ca V 2.1 channels containing β 3 and α 2 δ 1 subunits. The zero current level is indicated by dotted lines. Average Ca 2+ current density-voltage relationships ( F ) and normalized I-V curves ( G ) for N283Q mutant Ca V 2.1 channels expressed in DMSO-treated cells (filled cyan triangles, n = 10) and in cells treated with 0.6 μg/mL tunicamycin (filled green circles, n = 8). Peak Ca 2+ current density through N283Q Ca V 2.1 channels after vehicle (DMSO) and tunicamycin treatments were −23.3 ± 5.6 pA/pF ( n = 10) and −11.6 ± 3.6 pA/pF ( n = 8), respectively ( p = 0.06, Student’s t -test). ( H ) Reduction in V 1/2 for activation of Ca V 2.1 channels composed by N283Q mutant α 1A , β 3 and α 2 δ 1 subunits (estimated from normalized I-V curves shown in ( G ) as indicated in Materials and Methods) produced by 0.6 μg/mL tunicamycin ( n = 8). ** p < 0.01 versus the control condition (vehicle, n = 10; Student’s t -test).
    Figure Legend Snippet: N283Q glycosylation site mutation reduces Ca 2+ current density through Ca V 2.1 channels heterologously expressed in HEK293 cells, without altering their voltage-dependent activation. ( A ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the decrease in Ca 2+ current density through Ca V 2.1 channels containing the mutation at the α 1A glycosylation site N283, which exhibit voltage dependence of activation similar to that of WT channels. Dotted lines mark the zero current level. Average Ca 2+ current density-voltage relationships ( B ) and normalized I-V curves ( C ) for WT (open circles, n = 13) and N283Q (filled dark cyan triangles, n = 19) Ca V 2.1 channels. N283Q reduces maximal Ca 2+ current density (obtained by membrane depolarization to +15 mV) from −69.4 ± 12.9 pA/pF ( n = 13) to −19.5 ± 3.2 pA/pF ( n = 19) ( p < 0.001, Mann-Whitney U -test). ( D ) N283Q mutation has no significant effect on the V 1/2 for Ca V 2.1 channel activation (estimated from normalized I-V curves shown in C as indicated in Materials and Methods, p = 0.798, Student’s t -test). ( E ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the shift of activation to lower depolarization induced by 0.6 μg/mL tunicamycin on N283Q mutant Ca V 2.1 channels containing β 3 and α 2 δ 1 subunits. The zero current level is indicated by dotted lines. Average Ca 2+ current density-voltage relationships ( F ) and normalized I-V curves ( G ) for N283Q mutant Ca V 2.1 channels expressed in DMSO-treated cells (filled cyan triangles, n = 10) and in cells treated with 0.6 μg/mL tunicamycin (filled green circles, n = 8). Peak Ca 2+ current density through N283Q Ca V 2.1 channels after vehicle (DMSO) and tunicamycin treatments were −23.3 ± 5.6 pA/pF ( n = 10) and −11.6 ± 3.6 pA/pF ( n = 8), respectively ( p = 0.06, Student’s t -test). ( H ) Reduction in V 1/2 for activation of Ca V 2.1 channels composed by N283Q mutant α 1A , β 3 and α 2 δ 1 subunits (estimated from normalized I-V curves shown in ( G ) as indicated in Materials and Methods) produced by 0.6 μg/mL tunicamycin ( n = 8). ** p < 0.01 versus the control condition (vehicle, n = 10; Student’s t -test).

    Techniques Used: Glycoproteomics, Mutagenesis, Activation Assay, Membrane, MANN-WHITNEY, Produced, Control

    N283Q glycosylation site mutation lessens Ca V 2.1 channel inactivation. Ca 2+ current traces (normalized to the corresponding peak amplitude) illustrating differential inactivation of WT (black traces) and N283Q (cyan traces) Ca V 2.1 channels, in response to a 3 s depolarizing pulse to +20 mV ( A ) or 0 mV ( D ). Dotted lines indicate the zero current level. ( B , E ) Average Ca 2+ current inactivation (in %) at the end of these 3s depolarizing pulses obtained from HEK293 cells expressing either WT or N283Q Ca V 2.1 channels. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test). ( C , F ) Average τ inactivation values of Ca 2+ currents through WT (open bars) and N283Q (cyan bars) Ca V 2.1 channels expressed in HEK293 cells, elicited by a 3 s depolarizing pulse to +20 mV or 0 mV, as indicated. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test).
    Figure Legend Snippet: N283Q glycosylation site mutation lessens Ca V 2.1 channel inactivation. Ca 2+ current traces (normalized to the corresponding peak amplitude) illustrating differential inactivation of WT (black traces) and N283Q (cyan traces) Ca V 2.1 channels, in response to a 3 s depolarizing pulse to +20 mV ( A ) or 0 mV ( D ). Dotted lines indicate the zero current level. ( B , E ) Average Ca 2+ current inactivation (in %) at the end of these 3s depolarizing pulses obtained from HEK293 cells expressing either WT or N283Q Ca V 2.1 channels. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test). ( C , F ) Average τ inactivation values of Ca 2+ currents through WT (open bars) and N283Q (cyan bars) Ca V 2.1 channels expressed in HEK293 cells, elicited by a 3 s depolarizing pulse to +20 mV or 0 mV, as indicated. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test).

    Techniques Used: Glycoproteomics, Mutagenesis, Expressing, MANN-WHITNEY



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    ca v 2.1 n283q mutant channel  (GenScript corporation)
    90
    GenScript corporation ca v 2.1 n283q mutant channel
    <t>N283Q</t> glycosylation site mutation reduces Ca 2+ current density through Ca V 2.1 channels heterologously expressed in HEK293 cells, without altering their voltage-dependent activation. ( A ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the decrease in Ca 2+ current density through Ca V 2.1 channels containing the mutation at the α 1A glycosylation site N283, which exhibit voltage dependence of activation similar to that of WT channels. Dotted lines mark the zero current level. Average Ca 2+ current density-voltage relationships ( B ) and normalized I-V curves ( C ) for WT (open circles, n = 13) and N283Q (filled dark cyan triangles, n = 19) Ca V 2.1 channels. N283Q reduces maximal Ca 2+ current density (obtained by membrane depolarization to +15 mV) from −69.4 ± 12.9 pA/pF ( n = 13) to −19.5 ± 3.2 pA/pF ( n = 19) ( p < 0.001, Mann-Whitney U -test). ( D ) N283Q mutation has no significant effect on the V 1/2 for Ca V 2.1 channel activation (estimated from normalized I-V curves shown in C as indicated in Materials and Methods, p = 0.798, Student’s t -test). ( E ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the shift of activation to lower depolarization induced by 0.6 μg/mL tunicamycin on N283Q mutant Ca V 2.1 channels containing β 3 and α 2 δ 1 subunits. The zero current level is indicated by dotted lines. Average Ca 2+ current density-voltage relationships ( F ) and normalized I-V curves ( G ) for N283Q mutant Ca V 2.1 channels expressed in DMSO-treated cells (filled cyan triangles, n = 10) and in cells treated with 0.6 μg/mL tunicamycin (filled green circles, n = 8). Peak Ca 2+ current density through N283Q Ca V 2.1 channels after vehicle (DMSO) and tunicamycin treatments were −23.3 ± 5.6 pA/pF ( n = 10) and −11.6 ± 3.6 pA/pF ( n = 8), respectively ( p = 0.06, Student’s t -test). ( H ) Reduction in V 1/2 for activation of Ca V 2.1 channels composed by N283Q mutant α 1A , β 3 and α 2 δ 1 subunits (estimated from normalized I-V curves shown in ( G ) as indicated in Materials and Methods) produced by 0.6 μg/mL tunicamycin ( n = 8). ** p < 0.01 versus the control condition (vehicle, n = 10; Student’s t -test).
    Ca V 2.1 N283q Mutant Channel, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ca v 2.1 n283q mutant channel/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    ca v 2.1 n283q mutant channel - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

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    N283Q glycosylation site mutation reduces Ca 2+ current density through Ca V 2.1 channels heterologously expressed in HEK293 cells, without altering their voltage-dependent activation. ( A ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the decrease in Ca 2+ current density through Ca V 2.1 channels containing the mutation at the α 1A glycosylation site N283, which exhibit voltage dependence of activation similar to that of WT channels. Dotted lines mark the zero current level. Average Ca 2+ current density-voltage relationships ( B ) and normalized I-V curves ( C ) for WT (open circles, n = 13) and N283Q (filled dark cyan triangles, n = 19) Ca V 2.1 channels. N283Q reduces maximal Ca 2+ current density (obtained by membrane depolarization to +15 mV) from −69.4 ± 12.9 pA/pF ( n = 13) to −19.5 ± 3.2 pA/pF ( n = 19) ( p < 0.001, Mann-Whitney U -test). ( D ) N283Q mutation has no significant effect on the V 1/2 for Ca V 2.1 channel activation (estimated from normalized I-V curves shown in C as indicated in Materials and Methods, p = 0.798, Student’s t -test). ( E ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the shift of activation to lower depolarization induced by 0.6 μg/mL tunicamycin on N283Q mutant Ca V 2.1 channels containing β 3 and α 2 δ 1 subunits. The zero current level is indicated by dotted lines. Average Ca 2+ current density-voltage relationships ( F ) and normalized I-V curves ( G ) for N283Q mutant Ca V 2.1 channels expressed in DMSO-treated cells (filled cyan triangles, n = 10) and in cells treated with 0.6 μg/mL tunicamycin (filled green circles, n = 8). Peak Ca 2+ current density through N283Q Ca V 2.1 channels after vehicle (DMSO) and tunicamycin treatments were −23.3 ± 5.6 pA/pF ( n = 10) and −11.6 ± 3.6 pA/pF ( n = 8), respectively ( p = 0.06, Student’s t -test). ( H ) Reduction in V 1/2 for activation of Ca V 2.1 channels composed by N283Q mutant α 1A , β 3 and α 2 δ 1 subunits (estimated from normalized I-V curves shown in ( G ) as indicated in Materials and Methods) produced by 0.6 μg/mL tunicamycin ( n = 8). ** p < 0.01 versus the control condition (vehicle, n = 10; Student’s t -test).

    Journal: International Journal of Molecular Sciences

    Article Title: Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy

    doi: 10.3390/ijms19020619

    Figure Lengend Snippet: N283Q glycosylation site mutation reduces Ca 2+ current density through Ca V 2.1 channels heterologously expressed in HEK293 cells, without altering their voltage-dependent activation. ( A ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the decrease in Ca 2+ current density through Ca V 2.1 channels containing the mutation at the α 1A glycosylation site N283, which exhibit voltage dependence of activation similar to that of WT channels. Dotted lines mark the zero current level. Average Ca 2+ current density-voltage relationships ( B ) and normalized I-V curves ( C ) for WT (open circles, n = 13) and N283Q (filled dark cyan triangles, n = 19) Ca V 2.1 channels. N283Q reduces maximal Ca 2+ current density (obtained by membrane depolarization to +15 mV) from −69.4 ± 12.9 pA/pF ( n = 13) to −19.5 ± 3.2 pA/pF ( n = 19) ( p < 0.001, Mann-Whitney U -test). ( D ) N283Q mutation has no significant effect on the V 1/2 for Ca V 2.1 channel activation (estimated from normalized I-V curves shown in C as indicated in Materials and Methods, p = 0.798, Student’s t -test). ( E ) Current traces elicited by 20 ms depolarizing pulses from −80 mV to the indicated voltages (inset) illustrating the shift of activation to lower depolarization induced by 0.6 μg/mL tunicamycin on N283Q mutant Ca V 2.1 channels containing β 3 and α 2 δ 1 subunits. The zero current level is indicated by dotted lines. Average Ca 2+ current density-voltage relationships ( F ) and normalized I-V curves ( G ) for N283Q mutant Ca V 2.1 channels expressed in DMSO-treated cells (filled cyan triangles, n = 10) and in cells treated with 0.6 μg/mL tunicamycin (filled green circles, n = 8). Peak Ca 2+ current density through N283Q Ca V 2.1 channels after vehicle (DMSO) and tunicamycin treatments were −23.3 ± 5.6 pA/pF ( n = 10) and −11.6 ± 3.6 pA/pF ( n = 8), respectively ( p = 0.06, Student’s t -test). ( H ) Reduction in V 1/2 for activation of Ca V 2.1 channels composed by N283Q mutant α 1A , β 3 and α 2 δ 1 subunits (estimated from normalized I-V curves shown in ( G ) as indicated in Materials and Methods) produced by 0.6 μg/mL tunicamycin ( n = 8). ** p < 0.01 versus the control condition (vehicle, n = 10; Student’s t -test).

    Article Snippet: Ca V 2.1 N283Q mutant channel was generated by site-directed mutagenesis of the human α 1A cDNA (GenScript Corporation, Piscatway, NJ, USA).

    Techniques: Glycoproteomics, Mutagenesis, Activation Assay, Membrane, MANN-WHITNEY, Produced, Control

    N283Q glycosylation site mutation lessens Ca V 2.1 channel inactivation. Ca 2+ current traces (normalized to the corresponding peak amplitude) illustrating differential inactivation of WT (black traces) and N283Q (cyan traces) Ca V 2.1 channels, in response to a 3 s depolarizing pulse to +20 mV ( A ) or 0 mV ( D ). Dotted lines indicate the zero current level. ( B , E ) Average Ca 2+ current inactivation (in %) at the end of these 3s depolarizing pulses obtained from HEK293 cells expressing either WT or N283Q Ca V 2.1 channels. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test). ( C , F ) Average τ inactivation values of Ca 2+ currents through WT (open bars) and N283Q (cyan bars) Ca V 2.1 channels expressed in HEK293 cells, elicited by a 3 s depolarizing pulse to +20 mV or 0 mV, as indicated. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test).

    Journal: International Journal of Molecular Sciences

    Article Title: Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy

    doi: 10.3390/ijms19020619

    Figure Lengend Snippet: N283Q glycosylation site mutation lessens Ca V 2.1 channel inactivation. Ca 2+ current traces (normalized to the corresponding peak amplitude) illustrating differential inactivation of WT (black traces) and N283Q (cyan traces) Ca V 2.1 channels, in response to a 3 s depolarizing pulse to +20 mV ( A ) or 0 mV ( D ). Dotted lines indicate the zero current level. ( B , E ) Average Ca 2+ current inactivation (in %) at the end of these 3s depolarizing pulses obtained from HEK293 cells expressing either WT or N283Q Ca V 2.1 channels. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test). ( C , F ) Average τ inactivation values of Ca 2+ currents through WT (open bars) and N283Q (cyan bars) Ca V 2.1 channels expressed in HEK293 cells, elicited by a 3 s depolarizing pulse to +20 mV or 0 mV, as indicated. Data are expressed as the mean ± SEM of the number of experiments shown in brackets (*** p < 0.001 and ** p < 0.01 versus WT, Mann-Whitney U -test).

    Article Snippet: Ca V 2.1 N283Q mutant channel was generated by site-directed mutagenesis of the human α 1A cDNA (GenScript Corporation, Piscatway, NJ, USA).

    Techniques: Glycoproteomics, Mutagenesis, Expressing, MANN-WHITNEY