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Syntaxin n type ca2
N Type Ca2, supplied by Syntaxin, used in various techniques. Bioz Stars score: 89/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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n type ca2 - by Bioz Stars, 2020-11
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In Vivo:

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. Peptides containing the synprint site of N-type Ca2+ channels reversibly inhibit synaptic transmission in cultured sympathetic neurons, suggesting that synprint peptides compete with N-type Ca2+ channels for binding to syntaxin and/or SNAP-25 in vivo ( ). .. These results implicate direct interactions of N-type Ca2+ channels with syntaxin and SNAP-25 in the docking and exocytosis of synaptic vesicles.

In Vitro:

Article Title: SNAREs and regulated vesicle exocytosis
Article Snippet: .. Such notion is supported by the observed in vitro interaction between syntaxin and N-type Ca2+ channels ( ). .. Catterall and colleagues now demonstrate that injection of peptides into presynaptic neurons, which cause dissociation of Ca2+ channel-SNARE complex in vitro , reversibly attenuates synchronous transmitter release ( ).

Cell Culture:

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. Peptides containing the synprint site of N-type Ca2+ channels reversibly inhibit synaptic transmission in cultured sympathetic neurons, suggesting that synprint peptides compete with N-type Ca2+ channels for binding to syntaxin and/or SNAP-25 in vivo ( ). .. These results implicate direct interactions of N-type Ca2+ channels with syntaxin and SNAP-25 in the docking and exocytosis of synaptic vesicles.

Concentration Assay:

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. In contrast, the blocking efficiency of the synprint peptide was maximal at low Ca2+ (10–20 μM), which is in the same range of Ca2+ concentration for maximal binding of N-type Ca2+ channels to syntaxin , and was reduced at higher concentration. .. The synprint peptide (0.5 μM) reduced synaptotagmin binding to syntaxin by approximately 50% at low Ca2+ or at 1 mM Ca2+ , but inhibited binding by approximately 90% at 10 μM and 80% at 20 μM, respectively.

other:

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: These solid-phase immunoassay results provide independent support for the specificity of interaction of these three SNARE proteins with the synprint site of N-type Ca2+ channels.

Blocking Assay:

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. In contrast, the blocking efficiency of the synprint peptide was maximal at low Ca2+ (10–20 μM), which is in the same range of Ca2+ concentration for maximal binding of N-type Ca2+ channels to syntaxin , and was reduced at higher concentration. .. The synprint peptide (0.5 μM) reduced synaptotagmin binding to syntaxin by approximately 50% at low Ca2+ or at 1 mM Ca2+ , but inhibited binding by approximately 90% at 10 μM and 80% at 20 μM, respectively.

Transmission Assay:

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. Peptides containing the synprint site of N-type Ca2+ channels reversibly inhibit synaptic transmission in cultured sympathetic neurons, suggesting that synprint peptides compete with N-type Ca2+ channels for binding to syntaxin and/or SNAP-25 in vivo ( ). .. These results implicate direct interactions of N-type Ca2+ channels with syntaxin and SNAP-25 in the docking and exocytosis of synaptic vesicles.

Binding Assay:

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. The Ca2+ -dependent displacement of synaptotagmin by the synprint peptide observed in these experiments supports the conclusion that the binding of N-type Ca2+ channels to syntaxin is physiologically significant and implies that synaptotagmin competes with the Ca2+ channel for binding to a common site on syntaxin. .. Thus, one of the roles of the synprint site on the Ca2+ channel may be to bind syntaxin after vesicle docking to prevent the core complex from gaining access to synaptotagmin.

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. In contrast, the blocking efficiency of the synprint peptide was maximal at low Ca2+ (10–20 μM), which is in the same range of Ca2+ concentration for maximal binding of N-type Ca2+ channels to syntaxin , and was reduced at higher concentration. .. The synprint peptide (0.5 μM) reduced synaptotagmin binding to syntaxin by approximately 50% at low Ca2+ or at 1 mM Ca2+ , but inhibited binding by approximately 90% at 10 μM and 80% at 20 μM, respectively.

Article Title: Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I
Article Snippet: .. Peptides containing the synprint site of N-type Ca2+ channels reversibly inhibit synaptic transmission in cultured sympathetic neurons, suggesting that synprint peptides compete with N-type Ca2+ channels for binding to syntaxin and/or SNAP-25 in vivo ( ). .. These results implicate direct interactions of N-type Ca2+ channels with syntaxin and SNAP-25 in the docking and exocytosis of synaptic vesicles.

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  • 88
    Syntaxin n type ca2 channel gating
    Stimulus-induced secretion consists of CIVDS and CDS components in the somata of DRG neurons. ( A ) Depolarization- and UV-flash-induced C m signals in a DRG neuron dialyzed with 5 mM NP-EGTA and 0.2 mM fura-6F. In <t>Ca2+-free</t> extracellular solution ( left panel ), a step depolarization (200 ms) evoked CIVDS ( C m0 ). When extracellular Ca 2+ was added ( right panel ), UV flashes ( arrows ) evoked a substantial increase of C m ( C m (UV)), which was caused by the Ca 2+ increase in the absence of membrane depolarization. Series conductance ( G s) and membrane current ( I m ), and Ca 2+ trace ([Ca 2+ ]i) are also shown. ( B ) Depolarization-induced C m signals. In Ca 2+ -free extracellular solution ( left panel ), a step depolarization (200 ms) evoked a C m increase (CIVDS) followed by a rapid reversal as in A . C m1 refers to the entire course. Subsequently, extracellular Ca 2+ (2.5 mM) was puffed ( right panel ), and the same stimulus evoked a biphasic response ( C m2 ). The first Cm increase was followed by a small but rapid reversal and then a slow but substantial increase. C m2 − C m1 ( dashed line ) indicated the CDS component.
    N Type Ca2 Channel Gating, supplied by Syntaxin, used in various techniques. Bioz Stars score: 88/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n type ca2 channel gating/product/Syntaxin
    Average 88 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    n type ca2 channel gating - by Bioz Stars, 2020-11
    88/100 stars
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    89
    Syntaxin p q type ca2
    Stimulus-induced secretion consists of CIVDS and CDS components in the somata of DRG neurons. ( A ) Depolarization- and UV-flash-induced C m signals in a DRG neuron dialyzed with 5 mM NP-EGTA and 0.2 mM fura-6F. In <t>Ca2+-free</t> extracellular solution ( left panel ), a step depolarization (200 ms) evoked CIVDS ( C m0 ). When extracellular Ca 2+ was added ( right panel ), UV flashes ( arrows ) evoked a substantial increase of C m ( C m (UV)), which was caused by the Ca 2+ increase in the absence of membrane depolarization. Series conductance ( G s) and membrane current ( I m ), and Ca 2+ trace ([Ca 2+ ]i) are also shown. ( B ) Depolarization-induced C m signals. In Ca 2+ -free extracellular solution ( left panel ), a step depolarization (200 ms) evoked a C m increase (CIVDS) followed by a rapid reversal as in A . C m1 refers to the entire course. Subsequently, extracellular Ca 2+ (2.5 mM) was puffed ( right panel ), and the same stimulus evoked a biphasic response ( C m2 ). The first Cm increase was followed by a small but rapid reversal and then a slow but substantial increase. C m2 − C m1 ( dashed line ) indicated the CDS component.
    P Q Type Ca2, supplied by Syntaxin, used in various techniques. Bioz Stars score: 89/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p q type ca2/product/Syntaxin
    Average 89 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    p q type ca2 - by Bioz Stars, 2020-11
    89/100 stars
      Buy from Supplier

    Image Search Results


    Stimulus-induced secretion consists of CIVDS and CDS components in the somata of DRG neurons. ( A ) Depolarization- and UV-flash-induced C m signals in a DRG neuron dialyzed with 5 mM NP-EGTA and 0.2 mM fura-6F. In Ca2+-free extracellular solution ( left panel ), a step depolarization (200 ms) evoked CIVDS ( C m0 ). When extracellular Ca 2+ was added ( right panel ), UV flashes ( arrows ) evoked a substantial increase of C m ( C m (UV)), which was caused by the Ca 2+ increase in the absence of membrane depolarization. Series conductance ( G s) and membrane current ( I m ), and Ca 2+ trace ([Ca 2+ ]i) are also shown. ( B ) Depolarization-induced C m signals. In Ca 2+ -free extracellular solution ( left panel ), a step depolarization (200 ms) evoked a C m increase (CIVDS) followed by a rapid reversal as in A . C m1 refers to the entire course. Subsequently, extracellular Ca 2+ (2.5 mM) was puffed ( right panel ), and the same stimulus evoked a biphasic response ( C m2 ). The first Cm increase was followed by a small but rapid reversal and then a slow but substantial increase. C m2 − C m1 ( dashed line ) indicated the CDS component.

    Journal: Biophysical Journal

    Article Title: Action Potential Modulates Ca2+-Dependent and Ca2+-Independent Secretion in a Sensory Neuron

    doi: 10.1016/j.bpj.2008.11.037

    Figure Lengend Snippet: Stimulus-induced secretion consists of CIVDS and CDS components in the somata of DRG neurons. ( A ) Depolarization- and UV-flash-induced C m signals in a DRG neuron dialyzed with 5 mM NP-EGTA and 0.2 mM fura-6F. In Ca2+-free extracellular solution ( left panel ), a step depolarization (200 ms) evoked CIVDS ( C m0 ). When extracellular Ca 2+ was added ( right panel ), UV flashes ( arrows ) evoked a substantial increase of C m ( C m (UV)), which was caused by the Ca 2+ increase in the absence of membrane depolarization. Series conductance ( G s) and membrane current ( I m ), and Ca 2+ trace ([Ca 2+ ]i) are also shown. ( B ) Depolarization-induced C m signals. In Ca 2+ -free extracellular solution ( left panel ), a step depolarization (200 ms) evoked a C m increase (CIVDS) followed by a rapid reversal as in A . C m1 refers to the entire course. Subsequently, extracellular Ca 2+ (2.5 mM) was puffed ( right panel ), and the same stimulus evoked a biphasic response ( C m2 ). The first Cm increase was followed by a small but rapid reversal and then a slow but substantial increase. C m2 − C m1 ( dashed line ) indicated the CDS component.

    Article Snippet: Molecular determinants of the functional interaction between syntaxin and N-type Ca2+ channel gating.

    Techniques: Mass Spectrometry