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    qx 222  (Alomone Labs)


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    dimethylphenyl acetamide chloride qx 222  (Alomone Labs)


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    Alomone Labs dimethylphenyl acetamide chloride qx 222
    Aligned sequences of the M2 segments of mouse-muscle ACh receptor subunits. The numbering is that of the α subunit. The predicted membrane-spanning segments correspond to αM243 to αV261. The intracellular ( IN ) and extracellular ( EX ) ends are indicated. *Residues are aligned with residues in the ACh receptor from Torpedo electric tissue that were labeled by noncompetitive inhibitor derivatives. Mutations of the boxed-in residues affected channel block by <t>QX-222.</t> Cysteines substituted for the residues in bold italics are exposed in the channel in the presence of ACh (tested only in α and β). See text for references.
    Dimethylphenyl Acetamide Chloride Qx 222, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Delimiting the Binding Site for Quaternary Ammonium Lidocaine Derivatives in the Acetylcholine Receptor Channel"

    Article Title: Delimiting the Binding Site for Quaternary Ammonium Lidocaine Derivatives in the Acetylcholine Receptor Channel

    Journal: The Journal of General Physiology

    doi:

    Aligned sequences of the M2 segments of mouse-muscle ACh receptor subunits. The numbering is that of the α subunit. The predicted membrane-spanning segments correspond to αM243 to αV261. The intracellular ( IN ) and extracellular ( EX ) ends are indicated. *Residues are aligned with residues in the ACh receptor from Torpedo electric tissue that were labeled by noncompetitive inhibitor derivatives. Mutations of the boxed-in residues affected channel block by QX-222. Cysteines substituted for the residues in bold italics are exposed in the channel in the presence of ACh (tested only in α and β). See text for references.
    Figure Legend Snippet: Aligned sequences of the M2 segments of mouse-muscle ACh receptor subunits. The numbering is that of the α subunit. The predicted membrane-spanning segments correspond to αM243 to αV261. The intracellular ( IN ) and extracellular ( EX ) ends are indicated. *Residues are aligned with residues in the ACh receptor from Torpedo electric tissue that were labeled by noncompetitive inhibitor derivatives. Mutations of the boxed-in residues affected channel block by QX-222. Cysteines substituted for the residues in bold italics are exposed in the channel in the presence of ACh (tested only in α and β). See text for references.

    Techniques Used: Labeling, Blocking Assay

    Structures of QX-314 and QX-222.
    Figure Legend Snippet: Structures of QX-314 and QX-222.

    Techniques Used:

    The protection by QX-314 and QX-222 of Cys-substituted residues in M2 against reaction with MTSEA. For each mutant, the rate constant of the reaction in the presence of channel blocker and ACh ( k blocked ) and the rate constant of the reaction in the presence of ACh alone ( k open ) were determined as described in methods . The extent of protection is taken as 1 − ( k blocked / k open ). The means of two to four determinations and average errors or SEM are plotted. The lighter bars represent the protection by QX-314, and the darker bars represent the protection by QX-222. *ND.
    Figure Legend Snippet: The protection by QX-314 and QX-222 of Cys-substituted residues in M2 against reaction with MTSEA. For each mutant, the rate constant of the reaction in the presence of channel blocker and ACh ( k blocked ) and the rate constant of the reaction in the presence of ACh alone ( k open ) were determined as described in methods . The extent of protection is taken as 1 − ( k blocked / k open ). The means of two to four determinations and average errors or SEM are plotted. The lighter bars represent the protection by QX-314, and the darker bars represent the protection by QX-222. *ND.

    Techniques Used: Mutagenesis

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    Alomone Labs dimethylphenyl acetamide chloride qx 222
    Aligned sequences of the M2 segments of mouse-muscle ACh receptor subunits. The numbering is that of the α subunit. The predicted membrane-spanning segments correspond to αM243 to αV261. The intracellular ( IN ) and extracellular ( EX ) ends are indicated. *Residues are aligned with residues in the ACh receptor from Torpedo electric tissue that were labeled by noncompetitive inhibitor derivatives. Mutations of the boxed-in residues affected channel block by <t>QX-222.</t> Cysteines substituted for the residues in bold italics are exposed in the channel in the presence of ACh (tested only in α and β). See text for references.
    Dimethylphenyl Acetamide Chloride Qx 222, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Aligned sequences of the M2 segments of mouse-muscle ACh receptor subunits. The numbering is that of the α subunit. The predicted membrane-spanning segments correspond to αM243 to αV261. The intracellular ( IN ) and extracellular ( EX ) ends are indicated. *Residues are aligned with residues in the ACh receptor from Torpedo electric tissue that were labeled by noncompetitive inhibitor derivatives. Mutations of the boxed-in residues affected channel block by QX-222. Cysteines substituted for the residues in bold italics are exposed in the channel in the presence of ACh (tested only in α and β). See text for references.

    Journal: The Journal of General Physiology

    Article Title: Delimiting the Binding Site for Quaternary Ammonium Lidocaine Derivatives in the Acetylcholine Receptor Channel

    doi:

    Figure Lengend Snippet: Aligned sequences of the M2 segments of mouse-muscle ACh receptor subunits. The numbering is that of the α subunit. The predicted membrane-spanning segments correspond to αM243 to αV261. The intracellular ( IN ) and extracellular ( EX ) ends are indicated. *Residues are aligned with residues in the ACh receptor from Torpedo electric tissue that were labeled by noncompetitive inhibitor derivatives. Mutations of the boxed-in residues affected channel block by QX-222. Cysteines substituted for the residues in bold italics are exposed in the channel in the presence of ACh (tested only in α and β). See text for references.

    Article Snippet: The quaternary lidocaine derivative 2-(triethylammonio)- N -(2,6-dimethylphenyl)acetamide bromide (QX-314) was from Alomone Laboratories (Jerusalem, Israel) and from Astra (Westborough, MA), and 2-(trimethylammonio)- N -(2,6-dimethylphenyl)acetamide chloride (QX-222) was from Astra.

    Techniques: Labeling, Blocking Assay

    Structures of QX-314 and QX-222.

    Journal: The Journal of General Physiology

    Article Title: Delimiting the Binding Site for Quaternary Ammonium Lidocaine Derivatives in the Acetylcholine Receptor Channel

    doi:

    Figure Lengend Snippet: Structures of QX-314 and QX-222.

    Article Snippet: The quaternary lidocaine derivative 2-(triethylammonio)- N -(2,6-dimethylphenyl)acetamide bromide (QX-314) was from Alomone Laboratories (Jerusalem, Israel) and from Astra (Westborough, MA), and 2-(trimethylammonio)- N -(2,6-dimethylphenyl)acetamide chloride (QX-222) was from Astra.

    Techniques:

    The protection by QX-314 and QX-222 of Cys-substituted residues in M2 against reaction with MTSEA. For each mutant, the rate constant of the reaction in the presence of channel blocker and ACh ( k blocked ) and the rate constant of the reaction in the presence of ACh alone ( k open ) were determined as described in methods . The extent of protection is taken as 1 − ( k blocked / k open ). The means of two to four determinations and average errors or SEM are plotted. The lighter bars represent the protection by QX-314, and the darker bars represent the protection by QX-222. *ND.

    Journal: The Journal of General Physiology

    Article Title: Delimiting the Binding Site for Quaternary Ammonium Lidocaine Derivatives in the Acetylcholine Receptor Channel

    doi:

    Figure Lengend Snippet: The protection by QX-314 and QX-222 of Cys-substituted residues in M2 against reaction with MTSEA. For each mutant, the rate constant of the reaction in the presence of channel blocker and ACh ( k blocked ) and the rate constant of the reaction in the presence of ACh alone ( k open ) were determined as described in methods . The extent of protection is taken as 1 − ( k blocked / k open ). The means of two to four determinations and average errors or SEM are plotted. The lighter bars represent the protection by QX-314, and the darker bars represent the protection by QX-222. *ND.

    Article Snippet: The quaternary lidocaine derivative 2-(triethylammonio)- N -(2,6-dimethylphenyl)acetamide bromide (QX-314) was from Alomone Laboratories (Jerusalem, Israel) and from Astra (Westborough, MA), and 2-(trimethylammonio)- N -(2,6-dimethylphenyl)acetamide chloride (QX-222) was from Astra.

    Techniques: Mutagenesis