antibodies against p2x 1  (Alomone Labs)


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    antibodies against p2x 1  (Alomone Labs)


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    antibodies against p2x 1  (Alomone Labs)


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    antibodies against p2x 1  (Alomone Labs)


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    Alomone Labs antibodies against p2x 1
    The ATP analogs β,γ-ImATP and α,β-MeATP biphasically modulate the evoked release of glutamate from rat hippocampal nerve terminals through activation of P2 receptors. A, Time course of tritium release from rat hippocampal synaptosomes challenged with two periods of stimulation with 20 mm K+ for 30 s (S1 and S2), as indicated by the bars above the abscissa. This representative experiment shows that 60 μm β,γ-ImATP (filled symbols), applied through the superfusate in the test chambers 2 min before S2 (as indicated by the top bar), increases glutamate release in S2. B, The nonselective <t>P2X/P2Y</t> receptors agonist β,γ-ImATP caused a concentration-dependent biphasic effect on the evoked release of glutamate, inhibiting at the lower (10-30 μm) and facilitating at higher (60-100 μm) concentrations, whereas the P2X-prefering agonist α,β-MeATP only facilitated the evoked release of glutamate at all concentrations tested. *p < 0.05 compared with 0%. C, The facilitatory effects of both 60 μm β,γ-ImATP and 60 μm α,β-MeATP were not modified in the presence of 50 nm ZM241385 (a selective antagonist of adenosine A2A receptors) but were prevented by 20 μm PPADS (nonselective P2 receptor antagonist). D, The inhibitory effect of 30 μm β,γ-ImATP was not modified in the presence of 50 nm DPCPX (selective antagonist of adenosine A1 receptor) but were prevented by both 75 μm suramin and 20 μm PPADS. *p < 0.05 compared with the effects of ATP analogs. The results are mean ± SEM of four to six experiments.
    Antibodies Against P2x 1, 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 "Dual Presynaptic Control by ATP of Glutamate Release via Facilitatory P2X 1 , P2X 2/3 , and P2X 3 and Inhibitory P2Y 1 , P2Y 2 , and/or P2Y 4 Receptors in the Rat Hippocampus"

    Article Title: Dual Presynaptic Control by ATP of Glutamate Release via Facilitatory P2X 1 , P2X 2/3 , and P2X 3 and Inhibitory P2Y 1 , P2Y 2 , and/or P2Y 4 Receptors in the Rat Hippocampus

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0628-05.2005

    The ATP analogs β,γ-ImATP and α,β-MeATP biphasically modulate the evoked release of glutamate from rat hippocampal nerve terminals through activation of P2 receptors. A, Time course of tritium release from rat hippocampal synaptosomes challenged with two periods of stimulation with 20 mm K+ for 30 s (S1 and S2), as indicated by the bars above the abscissa. This representative experiment shows that 60 μm β,γ-ImATP (filled symbols), applied through the superfusate in the test chambers 2 min before S2 (as indicated by the top bar), increases glutamate release in S2. B, The nonselective P2X/P2Y receptors agonist β,γ-ImATP caused a concentration-dependent biphasic effect on the evoked release of glutamate, inhibiting at the lower (10-30 μm) and facilitating at higher (60-100 μm) concentrations, whereas the P2X-prefering agonist α,β-MeATP only facilitated the evoked release of glutamate at all concentrations tested. *p < 0.05 compared with 0%. C, The facilitatory effects of both 60 μm β,γ-ImATP and 60 μm α,β-MeATP were not modified in the presence of 50 nm ZM241385 (a selective antagonist of adenosine A2A receptors) but were prevented by 20 μm PPADS (nonselective P2 receptor antagonist). D, The inhibitory effect of 30 μm β,γ-ImATP was not modified in the presence of 50 nm DPCPX (selective antagonist of adenosine A1 receptor) but were prevented by both 75 μm suramin and 20 μm PPADS. *p < 0.05 compared with the effects of ATP analogs. The results are mean ± SEM of four to six experiments.
    Figure Legend Snippet: The ATP analogs β,γ-ImATP and α,β-MeATP biphasically modulate the evoked release of glutamate from rat hippocampal nerve terminals through activation of P2 receptors. A, Time course of tritium release from rat hippocampal synaptosomes challenged with two periods of stimulation with 20 mm K+ for 30 s (S1 and S2), as indicated by the bars above the abscissa. This representative experiment shows that 60 μm β,γ-ImATP (filled symbols), applied through the superfusate in the test chambers 2 min before S2 (as indicated by the top bar), increases glutamate release in S2. B, The nonselective P2X/P2Y receptors agonist β,γ-ImATP caused a concentration-dependent biphasic effect on the evoked release of glutamate, inhibiting at the lower (10-30 μm) and facilitating at higher (60-100 μm) concentrations, whereas the P2X-prefering agonist α,β-MeATP only facilitated the evoked release of glutamate at all concentrations tested. *p < 0.05 compared with 0%. C, The facilitatory effects of both 60 μm β,γ-ImATP and 60 μm α,β-MeATP were not modified in the presence of 50 nm ZM241385 (a selective antagonist of adenosine A2A receptors) but were prevented by 20 μm PPADS (nonselective P2 receptor antagonist). D, The inhibitory effect of 30 μm β,γ-ImATP was not modified in the presence of 50 nm DPCPX (selective antagonist of adenosine A1 receptor) but were prevented by both 75 μm suramin and 20 μm PPADS. *p < 0.05 compared with the effects of ATP analogs. The results are mean ± SEM of four to six experiments.

    Techniques Used: Activation Assay, Concentration Assay, Modification

    The facilitatory effect of ATP analogs is mediated by P2X receptors, whereas the inhibitory effect is mediated by P2Y receptors. A, The facilitatory effect of 60 μm β,γ-ImATP was reverted in the presence of NF023 (10 μm; a selective P2X1, P2X2/3, and P2X3 receptor antagonist) and not modified by either RB2 (10 μm; a P2Y receptor antagonist) or MRS2179 (10 μm; a selective P2Y1 receptor antagonist). B, The inhibitory effect of 10 μmβ, γ-ImATP was not modified by NF023 but was prevented by RB2 and attenuated by MRS2179. *p < 0.05 compared with the first bar from left in A and B. The results are mean ± SEM of four to six experiments.
    Figure Legend Snippet: The facilitatory effect of ATP analogs is mediated by P2X receptors, whereas the inhibitory effect is mediated by P2Y receptors. A, The facilitatory effect of 60 μm β,γ-ImATP was reverted in the presence of NF023 (10 μm; a selective P2X1, P2X2/3, and P2X3 receptor antagonist) and not modified by either RB2 (10 μm; a P2Y receptor antagonist) or MRS2179 (10 μm; a selective P2Y1 receptor antagonist). B, The inhibitory effect of 10 μmβ, γ-ImATP was not modified by NF023 but was prevented by RB2 and attenuated by MRS2179. *p < 0.05 compared with the first bar from left in A and B. The results are mean ± SEM of four to six experiments.

    Techniques Used: Modification

    β,γ-ImATP modulates the evoked [Ca2+]i transients in a biphasic manner through inhibitory P2Y and facilitatory P2X receptors in rat hippocampal nerve terminals. A, Representative experiment of the increase and decrease of the K+ (20 mm)-evoked [Ca2+]i caused by β, γ-ImATP at 60 and 30 μm, respectively. All experiments were performed in the presence of 50 nm ZM241385 and 50 nm DPCPX to exclude P1 receptor-mediated effects. B, The facilitatory effect of 60 μm β,γ-ImATP was prevented by PPADS (20 μm; a nonselective P2 receptor antagonist) and by NF023 (10 μm; a selective antagonist of P2X1, P2X2/3, and P2X3 receptors) and not modified by RB2 (10 μm; a preferring antagonist of P2Y receptors). C, The inhibitory effect of 30 μm β,γ-ImATP was not modified by NF023 but was prevented by PPADS and attenuated by RB2. The percentage variations of [Ca2+]i are relative to control values (B, C). *p < 0.05 compared with 0%. **p < 0.05 compared with first bar from left in B and C. The results are mean ± SEM of four to six experiments.
    Figure Legend Snippet: β,γ-ImATP modulates the evoked [Ca2+]i transients in a biphasic manner through inhibitory P2Y and facilitatory P2X receptors in rat hippocampal nerve terminals. A, Representative experiment of the increase and decrease of the K+ (20 mm)-evoked [Ca2+]i caused by β, γ-ImATP at 60 and 30 μm, respectively. All experiments were performed in the presence of 50 nm ZM241385 and 50 nm DPCPX to exclude P1 receptor-mediated effects. B, The facilitatory effect of 60 μm β,γ-ImATP was prevented by PPADS (20 μm; a nonselective P2 receptor antagonist) and by NF023 (10 μm; a selective antagonist of P2X1, P2X2/3, and P2X3 receptors) and not modified by RB2 (10 μm; a preferring antagonist of P2Y receptors). C, The inhibitory effect of 30 μm β,γ-ImATP was not modified by NF023 but was prevented by PPADS and attenuated by RB2. The percentage variations of [Ca2+]i are relative to control values (B, C). *p < 0.05 compared with 0%. **p < 0.05 compared with first bar from left in B and C. The results are mean ± SEM of four to six experiments.

    Techniques Used: Modification

    RT-PCR identification of the P2 receptors expressed in single pyramidal neurons of the rat hippocampus. Individual cell bodies of CA1 and CA3 pyramidal neurons were removed under visual microscopic guidance from a Nissl-stained 10-μm-thick hippocampal slice, using a laser dissection slot (7.5 μm). Every sample of mRNA extracted from the cytoplasmic contents harvested from single hippocampal pyramidal neurons was subjected to reverse transcription protocol and amplified using a TPEA. They were then screened by PCR analysis, and the PCR products were resolved on 2-3% agarose gels and visualized by ethidium bromide staining. A, No PCR product was observed in the cDNA samples corresponding to an intronic marker (lane A), which indicates that all post-TPEA samples were DNA free. As positive controls, genomic DNA was always tested in parallel (lane B). B, Every single cDNA sample obtained from the laser-dissected single neurons that matched the PCR criteria for obtaining a single glutamatergic neuron [i.e., positive for a house-keeping gene (ribosomal protein L11) and a glutamatergic marker (NMDA receptor 1 subunit) and negative for both a GABAergic (GAD) and astrocytic (GFAP) markers] was screened by gene-specific PCR analysis for P2X subunits and P2Y receptors (B, bottom gels). In every assay, positive controls were performed using whole-brain cDNA instead (B, top gels). All the primers used are detailed in Table 1. Rib. Prot. L11, Ribosomal protein L11.
    Figure Legend Snippet: RT-PCR identification of the P2 receptors expressed in single pyramidal neurons of the rat hippocampus. Individual cell bodies of CA1 and CA3 pyramidal neurons were removed under visual microscopic guidance from a Nissl-stained 10-μm-thick hippocampal slice, using a laser dissection slot (7.5 μm). Every sample of mRNA extracted from the cytoplasmic contents harvested from single hippocampal pyramidal neurons was subjected to reverse transcription protocol and amplified using a TPEA. They were then screened by PCR analysis, and the PCR products were resolved on 2-3% agarose gels and visualized by ethidium bromide staining. A, No PCR product was observed in the cDNA samples corresponding to an intronic marker (lane A), which indicates that all post-TPEA samples were DNA free. As positive controls, genomic DNA was always tested in parallel (lane B). B, Every single cDNA sample obtained from the laser-dissected single neurons that matched the PCR criteria for obtaining a single glutamatergic neuron [i.e., positive for a house-keeping gene (ribosomal protein L11) and a glutamatergic marker (NMDA receptor 1 subunit) and negative for both a GABAergic (GAD) and astrocytic (GFAP) markers] was screened by gene-specific PCR analysis for P2X subunits and P2Y receptors (B, bottom gels). In every assay, positive controls were performed using whole-brain cDNA instead (B, top gels). All the primers used are detailed in Table 1. Rib. Prot. L11, Ribosomal protein L11.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Staining, Dissection, Amplification, Marker

    Subsynaptic distribution of P2X and P2Y receptors in the hippocampus. A, Selective antibodies for each P2X and P2Y receptors were tested by Western blot analysis in a fraction enriched in the presynaptic active zone, in the postsynaptic density, in nerve terminals outside the active zone, and in the initial synaptosomal fraction from which fractionation began. These fractions were over 90% pure, as illustrated by the ability to recover the immunoreactivity for SNAP25 in the presynaptic active zone fraction, PSD95 in the postsynaptic density fraction, and synaptophysin (a protein located in synaptic vesicles) in the extrasynaptic fraction. B, C, Western blots in these fractions evaluating the subsynaptic distribution of the immunoreactivity of the antibodies selective for each P2X subunit and for each P2Y receptor tested (20-120 μg of protein of each fraction were applied to SDS-PAGE gels). To gauge the selectivity of the antibodies used, their immunoreactivity were tested in membranes of HEK cells transiently transfected with cDNAs encoding for each P2X subunit (B) and of 1321N1 human astrocytoma cell line stably transfected with each P2Y receptor (C). For P2Y12 receptor, rat platelet membranes were used as a positive control. Each blot is representative of at least three blots from different groups of animals with similar results. For each fractionation procedure, Western blot analysis for the markers of each fraction was performed as illustrated in A to assess the efficiency of each fractionation. Pre, Presynaptic active zone; Post, postsynaptic density; Extra, outside the active zone; Syn, synaptosomal.
    Figure Legend Snippet: Subsynaptic distribution of P2X and P2Y receptors in the hippocampus. A, Selective antibodies for each P2X and P2Y receptors were tested by Western blot analysis in a fraction enriched in the presynaptic active zone, in the postsynaptic density, in nerve terminals outside the active zone, and in the initial synaptosomal fraction from which fractionation began. These fractions were over 90% pure, as illustrated by the ability to recover the immunoreactivity for SNAP25 in the presynaptic active zone fraction, PSD95 in the postsynaptic density fraction, and synaptophysin (a protein located in synaptic vesicles) in the extrasynaptic fraction. B, C, Western blots in these fractions evaluating the subsynaptic distribution of the immunoreactivity of the antibodies selective for each P2X subunit and for each P2Y receptor tested (20-120 μg of protein of each fraction were applied to SDS-PAGE gels). To gauge the selectivity of the antibodies used, their immunoreactivity were tested in membranes of HEK cells transiently transfected with cDNAs encoding for each P2X subunit (B) and of 1321N1 human astrocytoma cell line stably transfected with each P2Y receptor (C). For P2Y12 receptor, rat platelet membranes were used as a positive control. Each blot is representative of at least three blots from different groups of animals with similar results. For each fractionation procedure, Western blot analysis for the markers of each fraction was performed as illustrated in A to assess the efficiency of each fractionation. Pre, Presynaptic active zone; Post, postsynaptic density; Extra, outside the active zone; Syn, synaptosomal.

    Techniques Used: Western Blot, Fractionation, SDS Page, Transfection, Stable Transfection, Positive Control

    Relative subsynaptic distribution of P2X 1-7 subunits and P2Y 1,2,4,6,11,12 receptors in the presynaptic, postsynaptic, and extrasynaptic fractions
    Figure Legend Snippet: Relative subsynaptic distribution of P2X 1-7 subunits and P2Y 1,2,4,6,11,12 receptors in the presynaptic, postsynaptic, and extrasynaptic fractions

    Techniques Used:

    Identification of P2X and P2Y receptors present in rat hippocampal glutamatergic nerve terminals by double immunocytochemical analysis of rat hippocampal single nerve terminals. In A, as an example, the immunocytochemical identification of P2X3 receptors subunit (left) in glutamatergic nerve terminals identified as immunopositive for vesicular glutamate transporters type 1 and type 2 (middle) that comprised 38.6 ± 1.3% (n = 3) of the total synaptosomal population is shown. After merging both images (right), the percentage of rat hippocampal glutamatergic nerve terminals endowed with each P2X subunit and each P2Y receptor was quantified, which is presented in B. The data are mean ± SEM of three or four experiments, and in each experiment, using different synaptosomal preparation from different animals, four different fields acquired from two different coverslips were analyzed.
    Figure Legend Snippet: Identification of P2X and P2Y receptors present in rat hippocampal glutamatergic nerve terminals by double immunocytochemical analysis of rat hippocampal single nerve terminals. In A, as an example, the immunocytochemical identification of P2X3 receptors subunit (left) in glutamatergic nerve terminals identified as immunopositive for vesicular glutamate transporters type 1 and type 2 (middle) that comprised 38.6 ± 1.3% (n = 3) of the total synaptosomal population is shown. After merging both images (right), the percentage of rat hippocampal glutamatergic nerve terminals endowed with each P2X subunit and each P2Y receptor was quantified, which is presented in B. The data are mean ± SEM of three or four experiments, and in each experiment, using different synaptosomal preparation from different animals, four different fields acquired from two different coverslips were analyzed.

    Techniques Used:

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