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gaba a receptor β3 subunit  (Janssen)

 
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    Janssen gaba a receptor β3 subunit
    Gaba A Receptor β3 Subunit, supplied by Janssen, 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/product/gaba+(a)+receptor+%CE%B23+subunit/gaba+a+rs/pmc04221816-399-12-8
    Average 90 stars, based on 1 article reviews
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    Expressing:

    Article Title: Contrasting actions of group I metabotropic glutamate receptors in distinct mouse striatal neurones
    Article Snippet: .. [ PMC free article ] [ PubMed ] Janssen MJ, Yasuda RP, Vicini S. GABA A receptor β3 subunit expression regulates tonic current in developing striatopallidal medium spiny neurons. ..



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    The transmembrane domain of a α1β3γ2L structural homology model based on GluCl (pdb 4COF) is depicted 25. Subunit peptide backbones are shown as ribbons <t>(α1</t> = yellow; β3 = blue; γ2L = green), with sidechains of interest (see Table 1) shown in space-filling mode and labeled. Amino acid sidechains on β3-M3 and α1-M1 that are directly photolabeled by analogs of one or more study anesthetics are colored orange-red. Anesthetic contact sidechains that have previously been identified using substituted cysteine modification-protection are colored purple. Other β3-M2 and β3-M3 sidechains that line the β+–α– cleft and three sidechains predicted to face the β3 intra-subunit helix bundle pocket (Y284, G287, and E298), are colored gray. The location of α1Q242 (pink) is also shown. Inserts display the molecular space-filling structures of propofol, etomidate, and alphaxalone, approximately scaled to the receptor model. Hydrogens have been hidden for clarity.
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    Janssen gaba(a) receptor β3 subunit
    The transmembrane domain of a α1β3γ2L structural homology model based on GluCl (pdb 4COF) is depicted 25. Subunit peptide backbones are shown as ribbons <t>(α1</t> = yellow; β3 = blue; γ2L = green), with sidechains of interest (see Table 1) shown in space-filling mode and labeled. Amino acid sidechains on β3-M3 and α1-M1 that are directly photolabeled by analogs of one or more study anesthetics are colored orange-red. Anesthetic contact sidechains that have previously been identified using substituted cysteine modification-protection are colored purple. Other β3-M2 and β3-M3 sidechains that line the β+–α– cleft and three sidechains predicted to face the β3 intra-subunit helix bundle pocket (Y284, G287, and E298), are colored gray. The location of α1Q242 (pink) is also shown. Inserts display the molecular space-filling structures of propofol, etomidate, and alphaxalone, approximately scaled to the receptor model. Hydrogens have been hidden for clarity.
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    Non-R-mAb antibodies used in this study. Table lists Abs used in this study outside of the R-mAbs whose generation is described here. For each Ab the name, immunogen used in Ab generation, source and RRID number in the Antibody Registry, form and concentration/dilution used, and specific use in this paper is detailed.

    Journal: eLife

    Article Title: A toolbox of IgG subclass-switched recombinant monoclonal antibodies for enhanced multiplex immunolabeling of brain

    doi: 10.7554/eLife.43322

    Figure Lengend Snippet: Non-R-mAb antibodies used in this study. Table lists Abs used in this study outside of the R-mAbs whose generation is described here. For each Ab the name, immunogen used in Ab generation, source and RRID number in the Antibody Registry, form and concentration/dilution used, and specific use in this paper is detailed.

    Article Snippet: N87/25 , Fusion protein aa 370–433 of mouse GABA-A-receptor β3 subunit , Mouse IgG1 mAb, NeuroMab RRID: AB_10673389 , Tissue culture supernatant, 1:5 , 4.

    Techniques: Concentration Assay, Affinity Purification, Recombinant

    The transmembrane domain of a α1β3γ2L structural homology model based on GluCl (pdb 4COF) is depicted 25. Subunit peptide backbones are shown as ribbons (α1 = yellow; β3 = blue; γ2L = green), with sidechains of interest (see Table 1) shown in space-filling mode and labeled. Amino acid sidechains on β3-M3 and α1-M1 that are directly photolabeled by analogs of one or more study anesthetics are colored orange-red. Anesthetic contact sidechains that have previously been identified using substituted cysteine modification-protection are colored purple. Other β3-M2 and β3-M3 sidechains that line the β+–α– cleft and three sidechains predicted to face the β3 intra-subunit helix bundle pocket (Y284, G287, and E298), are colored gray. The location of α1Q242 (pink) is also shown. Inserts display the molecular space-filling structures of propofol, etomidate, and alphaxalone, approximately scaled to the receptor model. Hydrogens have been hidden for clarity.

    Journal: Anesthesiology

    Article Title: Alphaxalone Binds in Inner Transmembrane β + –α − Interfaces of α1β3γ2 γ-Aminobutyric Acid Type A Receptors

    doi: 10.1097/ALN.0000000000001978

    Figure Lengend Snippet: The transmembrane domain of a α1β3γ2L structural homology model based on GluCl (pdb 4COF) is depicted 25. Subunit peptide backbones are shown as ribbons (α1 = yellow; β3 = blue; γ2L = green), with sidechains of interest (see Table 1) shown in space-filling mode and labeled. Amino acid sidechains on β3-M3 and α1-M1 that are directly photolabeled by analogs of one or more study anesthetics are colored orange-red. Anesthetic contact sidechains that have previously been identified using substituted cysteine modification-protection are colored purple. Other β3-M2 and β3-M3 sidechains that line the β+–α– cleft and three sidechains predicted to face the β3 intra-subunit helix bundle pocket (Y284, G287, and E298), are colored gray. The location of α1Q242 (pink) is also shown. Inserts display the molecular space-filling structures of propofol, etomidate, and alphaxalone, approximately scaled to the receptor model. Hydrogens have been hidden for clarity.

    Article Snippet: Complementary DNAs encoding human α1, β3, and γ2L GABA A receptor subunits in pCDNA3.1 expression vectors (Thermo Fisher Scientific, Waltham, MA, USA) were used.

    Techniques: Labeling, Modification