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Image Search Results
Journal: The FASEB Journal
Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform
doi: 10.1096/fj.201900577rrrr
Figure Lengend Snippet: FIGURE 9 Interaction of CHL1 and DRD2 on TH- and DARP32-positive neurons in striatal sections. Proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies was combined with immunostaining using rabbit anti-DARPP32 (A) or anti-TH (B) antibodies to analyze tissue sections from 12- to 18-week-old CHL1+/+ mice. Nuclei are stained with DAPI (blue). Representative images are shown. Close- ups of two regions (without DAPI staining) are indicated by boxes and arrowheads indicate red spots indicating close molecular interaction of CHL1 with DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals
Article Snippet: The polyclonal rabbit antibodies against TH phosphorylated at Ser40 (pSer-TH) (Bio-Rad/AbD Serotec Cat# AHP912, RRID:AB_567401) and against DARPP32 phosphorylated at
Techniques: Proximity Ligation Assay, Immunostaining, Staining
Journal: The FASEB Journal
Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform
doi: 10.1096/fj.201900577rrrr
Figure Lengend Snippet: FIGURE 10 Interaction of CHL1 and DRD2 on TH- and DARP32-positive cells in cultures of ventral midbrain and striatum. Cultures of ventral midbrain (A) or striatum (B) were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies combined with immunofluorescent staining using rabbit anti-TH or anti-DARPP32 antibodies. Nuclei are stained with DAPI (blue). Representative images of different cells are shown. Red spots indicate close molecular interaction between CHL1 and DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals
Article Snippet: The polyclonal rabbit antibodies against TH phosphorylated at Ser40 (pSer-TH) (Bio-Rad/AbD Serotec Cat# AHP912, RRID:AB_567401) and against DARPP32 phosphorylated at
Techniques: Proximity Ligation Assay, Staining
Journal: The FASEB Journal
Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform
doi: 10.1096/fj.201900577rrrr
Figure Lengend Snippet: FIGURE 11 Reduced DRD2 and pSer40-TH levels in the dorsal striatum and reduced pThr34-DARPP32 levels in the ventral striatum in the absence of CHL1. The dorsal and ventral parts of the striatum were isolated from 10- to 13-week-old CHL1+/+ and CHL1−/− mice and subjected to Western blot analysis with anti-DRD2 and anti-GAPDH antibodies (A), anti-pSer40-TH and anti-TH antibodies (B) or anti-pThr34-DARPP32 and anti-DARPP32 (C) antibodies. Protein levels were determined by densitometry and DRD2 levels relative to GAPDH levels (A), pSer40-TH levels relative to total TH levels (B) and pThr34-DARPP32 levels relative to total DARPP32 levels (C) were calculated. A-C, Representative Western blots (left panels) are shown and mean values + standard error of the mean from eight CHL1−/− and 11 CHL1+/+ mice (right panels) are shown for the relative levels of DRD2 (A), pSer40-TH (B) and pThr34-DARPP32 (C) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; *P < .05, **P < .01). A, Lanes not adjacent to each other but derived from the same blot are separated by a vertical line
Article Snippet: The polyclonal rabbit antibodies against TH phosphorylated at Ser40 (pSer-TH) (Bio-Rad/AbD Serotec Cat# AHP912, RRID:AB_567401) and against DARPP32 phosphorylated at
Techniques: Isolation, Western Blot, Comparison, Derivative Assay
Journal: eLife
Article Title: Dopamine neuron morphology and output are differentially controlled by mTORC1 and mTORC2
doi: 10.7554/eLife.75398
Figure Lengend Snippet:
Article Snippet: The following primary antibodies were used: mouse anti-Tyrosine Hydroxylase (1:2000, Immunostar: 22941);
Techniques: BIA-KA, Recombinant, Software, Modification