ArticleExperimental eye research2011
Subunit-specific polyclonal antibody targeting human ρ1 GABA(C) receptor.
Article in Experimental eye research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Cysteine-terminated B-domain of Staphylococcus aureus protein A as a scaffold for targeting GABA(A) receptors.Analytical biochemistry · 2013Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The GABA(C) receptor, a postsynaptic membrane receptor expressed prominently in the retina, is a ligand-gated ion channel that consists of a combination of ρ subunits. We report characterization of a novel guinea pig polyclonal antibody, termed GABA(C) Ab N-14, directed against a 14-mer peptide (N-14) of the extracellular domain of the human ρ1 subunit. The antibody exhibits high sensitivity for N-14 by ELISA. In Western blots, GABA(C) Ab N-14 shows reactivity with the ρ1 subunit of preparations obtained from ρ1 GABA(C)-expressing neuroblastoma cells, Xenopus oocytes, and mammalian retina and brain. Flow cytometry reveals a rightward shift in mean fluorescence intensity of GABA(C)-expressing neuroblastoma cells probed with GABA(C) Ab N-14. Immunostaining of neuroblastoma cells and oocytes with GABA(C) Ab N-14 yields fluorescence only with GABA(C)-expressing cells. Antibody binding has no effect on GABA-elicited membrane current responses. Immunostaining of human retinal sections shows preferential staining within the inner plexiform layer. GABA(C) Ab N-14 appears well suited for investigative studies of GABA(C) ρ1 subunit in retina and other neural tissues.
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