galanin  (Alomone Labs)


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    Structured Review

    Alomone Labs galanin
    NPY (green) and <t>galanin</t> (magenta) immunoreactivity do not co-localize in fibers, although their distribution is largely coextensive Photomicrographs of NPY and galanin staining from a rostral (r3) and intermediate (i4) nTS level.
    Galanin, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/galanin/product/Alomone Labs
    Average 93 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    galanin - by Bioz Stars, 2022-11
    93/100 stars

    Images

    1) Product Images from "Immunocytochemical Organization and Sour Taste Activation in the Rostral Nuc. Solitary Tract of Mice"

    Article Title: Immunocytochemical Organization and Sour Taste Activation in the Rostral Nuc. Solitary Tract of Mice

    Journal: The Journal of comparative neurology

    doi: 10.1002/cne.24059

    NPY (green) and galanin (magenta) immunoreactivity do not co-localize in fibers, although their distribution is largely coextensive Photomicrographs of NPY and galanin staining from a rostral (r3) and intermediate (i4) nTS level.
    Figure Legend Snippet: NPY (green) and galanin (magenta) immunoreactivity do not co-localize in fibers, although their distribution is largely coextensive Photomicrographs of NPY and galanin staining from a rostral (r3) and intermediate (i4) nTS level.

    Techniques Used: Staining

    2) Product Images from "Immunocytochemical Organization and Sour Taste Activation in the Rostral Nuc. Solitary Tract of Mice"

    Article Title: Immunocytochemical Organization and Sour Taste Activation in the Rostral Nuc. Solitary Tract of Mice

    Journal: The Journal of comparative neurology

    doi: 10.1002/cne.24059

    NPY (green) and galanin (magenta) immunoreactivity do not co-localize in fibers, although their distribution is largely coextensive Photomicrographs of NPY and galanin staining from a rostral (r3) and intermediate (i4) nTS level.
    Figure Legend Snippet: NPY (green) and galanin (magenta) immunoreactivity do not co-localize in fibers, although their distribution is largely coextensive Photomicrographs of NPY and galanin staining from a rostral (r3) and intermediate (i4) nTS level.

    Techniques Used: Staining

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    Alomone Labs anti p2x2 receptor antibody
    Human genetic variations of the <t>P2X2</t> <t>receptor.</t> (a) P2X2 domains including extracellular domain, transmembrane domain (TMD), intracellular domain (ICD), interface positions and ATP potency effect positions annotated from literature (Chataigneau et al., 2013 ). (b) Distribution of all human genetic variations found among ~76,000 individuals. Depicted structure displays a human P2X2 homology model based on the human ATP‐bound open‐state P2X3 structure (PDB ID: 5SVK) (Mansoor et al., 2016 ). (c) Density of missense variants (relative distribution by domain length). Note that extracellular domain (ECD) includes both ATP and interface positions. (d) Distribution of variant densities across 100,000 sampling simulations highlighting that the interface domain displays more genetic variants in the human population than expected from a random distribution of missense variants. (e) Evolutionary orthologue conservation by domain. (f) Predicted deleteriousness (combined annotation‐dependent depletion (CADD) scores) by domain
    Anti P2x2 Receptor Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p2x2 receptor antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti p2x2 receptor antibody - by Bioz Stars, 2022-11
    94/100 stars
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    Human genetic variations of the P2X2 receptor. (a) P2X2 domains including extracellular domain, transmembrane domain (TMD), intracellular domain (ICD), interface positions and ATP potency effect positions annotated from literature (Chataigneau et al., 2013 ). (b) Distribution of all human genetic variations found among ~76,000 individuals. Depicted structure displays a human P2X2 homology model based on the human ATP‐bound open‐state P2X3 structure (PDB ID: 5SVK) (Mansoor et al., 2016 ). (c) Density of missense variants (relative distribution by domain length). Note that extracellular domain (ECD) includes both ATP and interface positions. (d) Distribution of variant densities across 100,000 sampling simulations highlighting that the interface domain displays more genetic variants in the human population than expected from a random distribution of missense variants. (e) Evolutionary orthologue conservation by domain. (f) Predicted deleteriousness (combined annotation‐dependent depletion (CADD) scores) by domain

    Journal: British Journal of Pharmacology

    Article Title: P2X2 receptor subunit interfaces are missense variant hotspots, where mutations tend to increase apparent ATP affinity). P2X2 receptor subunit interfaces are missense variant hotspots, where mutations tend to increase apparent ATP affinity

    doi: 10.1111/bph.15830

    Figure Lengend Snippet: Human genetic variations of the P2X2 receptor. (a) P2X2 domains including extracellular domain, transmembrane domain (TMD), intracellular domain (ICD), interface positions and ATP potency effect positions annotated from literature (Chataigneau et al., 2013 ). (b) Distribution of all human genetic variations found among ~76,000 individuals. Depicted structure displays a human P2X2 homology model based on the human ATP‐bound open‐state P2X3 structure (PDB ID: 5SVK) (Mansoor et al., 2016 ). (c) Density of missense variants (relative distribution by domain length). Note that extracellular domain (ECD) includes both ATP and interface positions. (d) Distribution of variant densities across 100,000 sampling simulations highlighting that the interface domain displays more genetic variants in the human population than expected from a random distribution of missense variants. (e) Evolutionary orthologue conservation by domain. (f) Predicted deleteriousness (combined annotation‐dependent depletion (CADD) scores) by domain

    Article Snippet: Membranes were incubated in LI‐COR blocking buffer for 1 h, followed by incubation in LI‐COR blocking buffer containing rabbit polyclonal anti‐P2X2 (#APR‐003, RRID:AB_2040054 , Alomone Labs; 1:2000) and mouse anti‐ Na+ /K+ ‐ATPase (05‐369; EMD Merck Millipore) at 4°C overnight.

    Techniques: Variant Assay, Sampling

    Characterization of double mutants disrupting different subunit interface. (a) Homology model of rP2X2 receptor (R) with residues corresponding to the positions mutated shown as spheres. (b) Example recordings of D78N, L276A and D78N/L276A and western blot of surface fraction or total lysate extracted from oocytes expressing the indicated constructs (or uninjected oocytes). Scale bar: X, 10 s; Y, nA or μA. Note that the uncropped blot is provided as Figure S2 . (c, d) Normalized ATP‐elicited concentration–response data for WT (empty symbols) indicated single‐mutant (single‐colour symbols) and double‐mutant (split‐colour symbols) P2X2 receptors in response to application of increasing concentrations of ATP. Data are shown as mean ± SD ( n = 5–33)

    Journal: British Journal of Pharmacology

    Article Title: P2X2 receptor subunit interfaces are missense variant hotspots, where mutations tend to increase apparent ATP affinity). P2X2 receptor subunit interfaces are missense variant hotspots, where mutations tend to increase apparent ATP affinity

    doi: 10.1111/bph.15830

    Figure Lengend Snippet: Characterization of double mutants disrupting different subunit interface. (a) Homology model of rP2X2 receptor (R) with residues corresponding to the positions mutated shown as spheres. (b) Example recordings of D78N, L276A and D78N/L276A and western blot of surface fraction or total lysate extracted from oocytes expressing the indicated constructs (or uninjected oocytes). Scale bar: X, 10 s; Y, nA or μA. Note that the uncropped blot is provided as Figure S2 . (c, d) Normalized ATP‐elicited concentration–response data for WT (empty symbols) indicated single‐mutant (single‐colour symbols) and double‐mutant (split‐colour symbols) P2X2 receptors in response to application of increasing concentrations of ATP. Data are shown as mean ± SD ( n = 5–33)

    Article Snippet: Membranes were incubated in LI‐COR blocking buffer for 1 h, followed by incubation in LI‐COR blocking buffer containing rabbit polyclonal anti‐P2X2 (#APR‐003, RRID:AB_2040054 , Alomone Labs; 1:2000) and mouse anti‐ Na+ /K+ ‐ATPase (05‐369; EMD Merck Millipore) at 4°C overnight.

    Techniques: Western Blot, Expressing, Construct, Concentration Assay, Mutagenesis

    Human genetic variations of the P2X2 receptor. (A) P2X2 domains including ECD, TMD, ICD, Interface positions, and ATP potency effect positions annotated from literature ( Chataigneau et al., 2013 ). (B) Distribution of all human genetic variations found among ∼140,000 individuals. Depicted structure displays a human P2X2 homology model based on the human ATP-bound open state P2X3 structure [PDBid: 5SVK] ( Mansoor et al., 2016 ). (C) Density of missense variants (relative distribution by domain length). Note that ECD includes both ATP and Interface positions. (D) Distribution of variant densities across 100,000 sampling simulations highlighting that the interface domain displays more genetic variants in the human population than expected from a random distribution of missense variants. (E) Evolutionary ortholog conservation by domain. (F) Predicted deleteriousness (CADD scores) by domain.

    Journal: bioRxiv

    Article Title: P2X2 receptor subunit interfaces are missense variant hotspots where mutations tend to increase apparent ATP affinity

    doi: 10.1101/2021.03.26.436616

    Figure Lengend Snippet: Human genetic variations of the P2X2 receptor. (A) P2X2 domains including ECD, TMD, ICD, Interface positions, and ATP potency effect positions annotated from literature ( Chataigneau et al., 2013 ). (B) Distribution of all human genetic variations found among ∼140,000 individuals. Depicted structure displays a human P2X2 homology model based on the human ATP-bound open state P2X3 structure [PDBid: 5SVK] ( Mansoor et al., 2016 ). (C) Density of missense variants (relative distribution by domain length). Note that ECD includes both ATP and Interface positions. (D) Distribution of variant densities across 100,000 sampling simulations highlighting that the interface domain displays more genetic variants in the human population than expected from a random distribution of missense variants. (E) Evolutionary ortholog conservation by domain. (F) Predicted deleteriousness (CADD scores) by domain.

    Article Snippet: Membranes were incubated in LI-COR blocking buffer for 1 hr, followed by incubation in LI-COR blocking buffer containing rabbit polyclonal anti-P2X2 (#APR-003, Alomone labs; 1:2000) and mouse anti-Na+ /K+ -ATPase (05-369; EMD Merck Millipore) at 4 °C overnight.

    Techniques: Variant Assay, Sampling

    Photomicrograph of the rostral solitary nucleus stained for P2X2 which effectively demarcates the central subdivision. Approximate borders of the nucleus are demarcated with arrows. Incoming fibers of the solitary tract (st) were also labeled with P2X2. Many cells with I A were located in the central subdivision (black symbols). Despite the failure to identify cells in the central subdivision without I A in this sample (white symbols), such cells were recorded in our previous study ( 12 ). An asterisk designates damage to the tissue where a stimulating electrode was positioned adjacent to the solitary tract. IV, 4th ventricle.

    Journal: bioRxiv

    Article Title: GABA and IA Independently Regulate rNST Responses to Afferent Input

    doi: 10.1101/2021.09.14.460273

    Figure Lengend Snippet: Photomicrograph of the rostral solitary nucleus stained for P2X2 which effectively demarcates the central subdivision. Approximate borders of the nucleus are demarcated with arrows. Incoming fibers of the solitary tract (st) were also labeled with P2X2. Many cells with I A were located in the central subdivision (black symbols). Despite the failure to identify cells in the central subdivision without I A in this sample (white symbols), such cells were recorded in our previous study ( 12 ). An asterisk designates damage to the tissue where a stimulating electrode was positioned adjacent to the solitary tract. IV, 4th ventricle.

    Article Snippet: PBS rinses separated the following steps: Slices were treated with 1% sodium borohydride (20 min), then incubated in blocking serum (60 min, 0.3% Triton, 1% Bovine Serum Albumin, 5% Donkey Serum) prior to primary antibody incubation with a polyclonal rabbit P2X2 antibody (1:10000, Alomone Labs, Catalog#: APR-003, Lot#: AN-1502), followed by a fluorescently tagged anti-rabbit secondary antibody (Alexa Fluor 546, Catalog #: A10040, Lot#: 1833519).

    Techniques: Staining, Labeling

    Overview of P2XR structure and residues at subunit interface. (A) Homology model of rP2X2R based on the X-ray crystal structure of the ATP-bound zebrafish P2X4R. One of the three subunits is color-coded: the two TM helices forming the fluke in green; lower and upper body in light and dark blue, respectively; the head domain in purple; the dorsal fin in orange and the flippers in yellow and red. The ATP molecules are shown in light grey spheres. The side chains at the subunit interface mutated in this study are highlighted with red spheres. (B) Table of side chains predicted to interact across the inter-subunit interface. The side chains mutated to disrupt a given interaction are shown in black font, the others in grey font. 1 : Residue involved in disulfide bond, therefore not considered here. Note that due to sequence differences between P2X2 and P2X4 not all residues/interactions are conserved.

    Journal: bioRxiv

    Article Title: Disrupting inter-subunit interactions favors channel opening in P2X2 receptors

    doi: 10.1101/2021.03.26.436616

    Figure Lengend Snippet: Overview of P2XR structure and residues at subunit interface. (A) Homology model of rP2X2R based on the X-ray crystal structure of the ATP-bound zebrafish P2X4R. One of the three subunits is color-coded: the two TM helices forming the fluke in green; lower and upper body in light and dark blue, respectively; the head domain in purple; the dorsal fin in orange and the flippers in yellow and red. The ATP molecules are shown in light grey spheres. The side chains at the subunit interface mutated in this study are highlighted with red spheres. (B) Table of side chains predicted to interact across the inter-subunit interface. The side chains mutated to disrupt a given interaction are shown in black font, the others in grey font. 1 : Residue involved in disulfide bond, therefore not considered here. Note that due to sequence differences between P2X2 and P2X4 not all residues/interactions are conserved.

    Article Snippet: Membranes were incubated with rabbit polyclonal anti-P2X2 (#APR-003, Alomone labs; 1:2000) and mouse anti-Na+ /K+-ATPase (05-369; EMD Merck Millipore) at 4 °C overnight.

    Techniques: Sequencing