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mouse monoclonal anti drd2 (Santa Cruz Biotechnology)

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Santa Cruz Biotechnology mouse monoclonal anti drd2
Mouse Monoclonal Anti Drd2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 206 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti-drd2+monoclonal+antibody/D2DR+Antibody/pmc12893853-52-50-56
Average 94 stars, based on 206 article reviews

mouse monoclonal anti drd2 - by Bioz Stars, 2026-10

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Article Title: Combined Exposure to Metals in Drinking Water Alters the Dopamine System in Mouse Striatum.
Article Snippet: For immunoblotting, the following primary antibodies were used: mouse anti-TH monoclonal antibody (1:150,000 dilution; Chemicon, Temecula, CA, USA), rat anti-DAT monoclonal antibody (1:500 dilution; Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse anti-VMAT2 monoclonal antibody (1:1000 dilution; Santa Cruz Biotechnology), mouse anti-DRD1 monoclonal antibody (1:500 dilution; Santa Cruz Biotechnology), and mouse anti-DRD2 monoclonal antibody (1:1000 dilution; Santa Cruz Biotechnology).

Article Title: Abnormal motor function and the expression of striatal dopamine D2 receptors in manganese-treated mice.
Article Snippet: For immunoblotting, the following primary antibodies were used: mouse anti-TH monoclonal antibody (1 : 4000 dilution, Chemicon), mouse anti-DRD2 monoclonal antibody (1 : 100 dilution, Santa Cruz Biotechnology), and rabbit anti-DRD3 polyclonal antibody (1 : 100 dilution, Santa Cruz Biotechnology).

Article Title: Effect of lavender oil on motor function and dopamine receptor expression in the olfactory bulb of mice.
Article Snippet: Aim of the study: Although treatment with the essential oil of lavender induces neuroemotional changes, there is a lack of data regarding its specific effects on neurotransduction, especially dopaminergic neurotransduction.. We investigated the relationship between altered motor activity and changes in the expression of dopamine receptors (DR), particularly the receptor subtypes D2 and D3, in lavender oiltreated mice.. Materials and methods: After the administration of lavender oil (intraperitoneal injections of 10–1000 mg/kg lavender oil once per day for 5 days), motor coordination and dopamine receptor expression were examined in the olfactory bulb and the striatum of the mouse brain. lfactory bulb triatum otor activity opamine receptor Results: After 5 days, mice treated with 1000 mg/kg lavender oil showed significantly increased rotarod activity when compared to controls.

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FIGURE 1 Association of CHL1 and DRD2. Brain extracts from CHL1+/+ (A-C) or CHL1−/− (C) mice (input) were subjected to immunoprecipitation (IP) with anti-CHL1 (A, C), anti-NCAM (A), anti-DRD2 (B), or non-immune control antibodies (A, B) and to Western blot analysis (WB) with anti-DRD2 (A, C) or anti-CHL1 (B) antibodies. D, CHL1-Fc and NCAM-Fc were incubated with a brain extract from CHL1+/+ mice (input) followed by pull-down (PD) with Protein A beads and by Western blot analysis (WB) with anti-DRD2 antibody. A-D, Representative Western blots from three independent experiments are shown. Lanes not adjacent to each other but derived from the same blot are separated by a vertical line. Aliquots of brain extracts not subjected to immunoprecipitation or pull-down experiments are designated as input

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 1 Association of CHL1 and DRD2. Brain extracts from CHL1+/+ (A-C) or CHL1−/− (C) mice (input) were subjected to immunoprecipitation (IP) with anti-CHL1 (A, C), anti-NCAM (A), anti-DRD2 (B), or non-immune control antibodies (A, B) and to Western blot analysis (WB) with anti-DRD2 (A, C) or anti-CHL1 (B) antibodies. D, CHL1-Fc and NCAM-Fc were incubated with a brain extract from CHL1+/+ mice (input) followed by pull-down (PD) with Protein A beads and by Western blot analysis (WB) with anti-DRD2 antibody. A-D, Representative Western blots from three independent experiments are shown. Lanes not adjacent to each other but derived from the same blot are separated by a vertical line. Aliquots of brain extracts not subjected to immunoprecipitation or pull-down experiments are designated as input

Article Snippet: The mouse monoclonal antibody against DRD2 (Santa Cruz Biotechnology Cat# sc-5303, RRID:AB_668816), the rabbit polyclonal antibody against GAPDH (Santa Cruz Biotechnology Cat# sc-25778, RRID:AB_10167668), and Protein A/G agarose beads were from Santa Cruz Biotechnology (Heidelberg, Germany).

Techniques: Immunoprecipitation, Control, Western Blot, Incubation, Derivative Assay

FIGURE 2 Binding of CHL1-Fc to the first extracellular loop of DRD2. Synthetic peptides comprising the first (A), second (B), or third (C) extracellular DRD2 loop or the DRD2 N-terminus (D) were coated as substrate and incubated with increasing concentrations of CHL1-Fc or NCAM-Fc. Binding was determined by ELISA using horseradish peroxidase-conjugated anti-Fc antibodies. Mean values ± standard error of the mean from three independent experiments carried out in triplicates are shown

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 2 Binding of CHL1-Fc to the first extracellular loop of DRD2. Synthetic peptides comprising the first (A), second (B), or third (C) extracellular DRD2 loop or the DRD2 N-terminus (D) were coated as substrate and incubated with increasing concentrations of CHL1-Fc or NCAM-Fc. Binding was determined by ELISA using horseradish peroxidase-conjugated anti-Fc antibodies. Mean values ± standard error of the mean from three independent experiments carried out in triplicates are shown

Techniques: Binding Assay, Incubation, Enzyme-linked Immunosorbent Assay

FIGURE 3 Binding of CHL1-Fc to DRD2 at the cell surface of transfected HEK293 cells. Live HEK293 cell expressing DRD2-S or DRD2-L were incubated with CHL1-Fc. After fixation, cells were incubated with goat anti-CHL1 antibody and mouse anti-DRD2 antibody against the extracellular N-terminus. After washing, cells were stained with Cy2-conjugated anti-mouse (green) and Cy3- conjugated anti-goat (red) antibodies. Areas indicated by white dashed lines and arrows show areas with CHL1-immunopositive signals, which partially overlap with intense DRD2-immunopositive staining. Arrowheads indicate nuclei of CHL1- and DRD2-immunonegative untransfected cells. The experiment was performed two times. Scale bar: 10 µm

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 3 Binding of CHL1-Fc to DRD2 at the cell surface of transfected HEK293 cells. Live HEK293 cell expressing DRD2-S or DRD2-L were incubated with CHL1-Fc. After fixation, cells were incubated with goat anti-CHL1 antibody and mouse anti-DRD2 antibody against the extracellular N-terminus. After washing, cells were stained with Cy2-conjugated anti-mouse (green) and Cy3- conjugated anti-goat (red) antibodies. Areas indicated by white dashed lines and arrows show areas with CHL1-immunopositive signals, which partially overlap with intense DRD2-immunopositive staining. Arrowheads indicate nuclei of CHL1- and DRD2-immunonegative untransfected cells. The experiment was performed two times. Scale bar: 10 µm

Techniques: Binding Assay, Transfection, Expressing, Incubation, Staining

FIGURE 4 Interaction of CHL1 with DRD2-S and DRD2-L in transfected HEK293 cells. HEK293 cells were transfected with pCAG- DRD2-S, pCAG-DRD2-L, pCAG-DRD2-S/CHL1, or pCAG-DRD2-L/CHL1 to express DRD2-S or DRD2-L alone or together with CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Transfected cells were subjected to proximity ligation assay with anti-CHL1 and anti-DRD2 antibodies. A, Representative images at low (left and middle panel) and high magnification (right panels) from two independent experiments performed in duplicates are shown and red spots indicate close interaction of CHL1 with DRD2-S and DRD2-L. Scale bars: 10 µm. B, Red spots were counted in HEK293 cells co-expressing DRD2-S or DRD2-L and CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Numbers of red spots per cell from two independent experiments performed in duplicates are shown (*P < .001; two-tailed Student's t test). C, Representative images taken with and without phase contrast are shown. Red spots are located predominantly at the cell surface (arrows) and indicate the close interaction between CHL1 and DRD2-S at the cell surface

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 4 Interaction of CHL1 with DRD2-S and DRD2-L in transfected HEK293 cells. HEK293 cells were transfected with pCAG- DRD2-S, pCAG-DRD2-L, pCAG-DRD2-S/CHL1, or pCAG-DRD2-L/CHL1 to express DRD2-S or DRD2-L alone or together with CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Transfected cells were subjected to proximity ligation assay with anti-CHL1 and anti-DRD2 antibodies. A, Representative images at low (left and middle panel) and high magnification (right panels) from two independent experiments performed in duplicates are shown and red spots indicate close interaction of CHL1 with DRD2-S and DRD2-L. Scale bars: 10 µm. B, Red spots were counted in HEK293 cells co-expressing DRD2-S or DRD2-L and CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Numbers of red spots per cell from two independent experiments performed in duplicates are shown (*P < .001; two-tailed Student's t test). C, Representative images taken with and without phase contrast are shown. Red spots are located predominantly at the cell surface (arrows) and indicate the close interaction between CHL1 and DRD2-S at the cell surface

Techniques: Transfection, Proximity Ligation Assay, Expressing, Two Tailed Test

FIGURE 5 Quinpirole reduces the cell surface level of DRD2-S in the absence of CHL1. A-C, HEK293 expressing DRD2-S (A) or DRD2-L (B) alone or co-expressing DRD2-S and CHL1 (DRD2-S/CHL1) (A, C) or DRD2-L and CHL1 (DRD2-L/CHL1) (B, C) were incubated with (+quin) or without (−quin) quinpirole followed by cell surface biotinylation, isolation of biotinylated proteins and Western blot analysis (WB) of the biotinylated proteins (surface) and the cell lysates (total) with anti-DRD2 (A, B) and anti-CHL1 (C) antibodies. The anti-GAPDH antibody was used to control loading (A, B). Total levels indicate the levels of CHL1 and DRD2 in cell lysates before isolation of biotinylated proteins, and cell surface levels represent biotinylated DRD2 after isolation of biotinylated proteins. A-C, Shown are representative blots from three independent experiments. D, E, Cell surface levels of DRD2-S and DRD2-L and total DRD2-S and DRD2-L levels in the cell lysates were determined, cell surface levels were normalized to total levels and the ratio of relative cell surface level after quinpirole treatment (+quin) and relative cell surface level after treatment without quinpirole (−quin) was calculated. Means + standard deviation from three independent experiments are shown for the ratios of the cell surface levels with quinpirole treatment relative to the cell surface levels without quinpirole treatment (D) and for the cell surface levels without quinpirole treatment relative to the total levels without quinpirole treatment (E) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; **P < .01; ns: not significant)

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 5 Quinpirole reduces the cell surface level of DRD2-S in the absence of CHL1. A-C, HEK293 expressing DRD2-S (A) or DRD2-L (B) alone or co-expressing DRD2-S and CHL1 (DRD2-S/CHL1) (A, C) or DRD2-L and CHL1 (DRD2-L/CHL1) (B, C) were incubated with (+quin) or without (−quin) quinpirole followed by cell surface biotinylation, isolation of biotinylated proteins and Western blot analysis (WB) of the biotinylated proteins (surface) and the cell lysates (total) with anti-DRD2 (A, B) and anti-CHL1 (C) antibodies. The anti-GAPDH antibody was used to control loading (A, B). Total levels indicate the levels of CHL1 and DRD2 in cell lysates before isolation of biotinylated proteins, and cell surface levels represent biotinylated DRD2 after isolation of biotinylated proteins. A-C, Shown are representative blots from three independent experiments. D, E, Cell surface levels of DRD2-S and DRD2-L and total DRD2-S and DRD2-L levels in the cell lysates were determined, cell surface levels were normalized to total levels and the ratio of relative cell surface level after quinpirole treatment (+quin) and relative cell surface level after treatment without quinpirole (−quin) was calculated. Means + standard deviation from three independent experiments are shown for the ratios of the cell surface levels with quinpirole treatment relative to the cell surface levels without quinpirole treatment (D) and for the cell surface levels without quinpirole treatment relative to the total levels without quinpirole treatment (E) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; **P < .01; ns: not significant)

Techniques: Expressing, Incubation, Isolation, Western Blot, Control, Standard Deviation, Comparison

FIGURE 6 Quinpirole-induced internalization of DRD2-S is reduced in the presence of CHL1. A, B, HEK293 expressing DRD2-S or co- expressing DRD2-S and CHL1 (DRD2-S/CHL1) were incubated with anti-DRD2 antibody against the extracellular N-terminus. After removal of unbound antibodies, cells were stimulated without (−quin) or with (+quin) quinpirole, fixed and incubated with Cy-3-conjugated secondary antibody. After removal of unbound secondary antibodies, cells were permeabilized and incubated with Cy-2-conjugated secondary antibody and analyzed by confocal microscopy. Cy-3-conjugated secondary antibodies (red) indicate non-internalized DRD2-bound anti-DRD2 antibodies at the cell surface and Cy-2-conjugated secondary antibodies (green) label internalized DRD2-bound anti-DRD2 antibodies. A, Representative images of HEK293 expressing DRD2-S after quinpirole treatment show surface DRD2 (red) and internalized DRD2 (green). Scale bar: 10 µm. B, Integrated densities of internalized and cell surface receptor-bound antibodies were determined and integrated densities of internalized receptor-bound antibodies were normalized to the total integrated densities (sum of integrated densities of internalized and cell surface receptor-bound antibodies). Box plots for the relative levels of internalized DRD2 are shown (**P < .01, ***P < .001; One-way ANOVA with post-hoc Student Newman- Keul's test). The experiment was performed two times in duplicates

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 6 Quinpirole-induced internalization of DRD2-S is reduced in the presence of CHL1. A, B, HEK293 expressing DRD2-S or co- expressing DRD2-S and CHL1 (DRD2-S/CHL1) were incubated with anti-DRD2 antibody against the extracellular N-terminus. After removal of unbound antibodies, cells were stimulated without (−quin) or with (+quin) quinpirole, fixed and incubated with Cy-3-conjugated secondary antibody. After removal of unbound secondary antibodies, cells were permeabilized and incubated with Cy-2-conjugated secondary antibody and analyzed by confocal microscopy. Cy-3-conjugated secondary antibodies (red) indicate non-internalized DRD2-bound anti-DRD2 antibodies at the cell surface and Cy-2-conjugated secondary antibodies (green) label internalized DRD2-bound anti-DRD2 antibodies. A, Representative images of HEK293 expressing DRD2-S after quinpirole treatment show surface DRD2 (red) and internalized DRD2 (green). Scale bar: 10 µm. B, Integrated densities of internalized and cell surface receptor-bound antibodies were determined and integrated densities of internalized receptor-bound antibodies were normalized to the total integrated densities (sum of integrated densities of internalized and cell surface receptor-bound antibodies). Box plots for the relative levels of internalized DRD2 are shown (**P < .01, ***P < .001; One-way ANOVA with post-hoc Student Newman- Keul's test). The experiment was performed two times in duplicates

Techniques: Expressing, Incubation, Confocal Microscopy, Cell Surface Receptor Assay

FIGURE 7 Co-immunostaining of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ (A, C) and CHL1−/− (B) mice were subjected to immunostaining using goat anti-CHL1 and mouse anti-DRD2 antibodies and Cy-3-conjugated anti- mouse and Cy-2-conjugated anti-goat secondary antibodies. Nuclei are stained with DAPI. Representative image of immunofluorescence staining for DAPI (blue), CHL1 (green), and DRD2 (red) are shown and yellow signals show co- localizations. C, Close-ups of two regions indicated by boxes in (A). A-C, Scale bars: 20 µm. Three independent experiments were performed with different sets of animals

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 7 Co-immunostaining of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ (A, C) and CHL1−/− (B) mice were subjected to immunostaining using goat anti-CHL1 and mouse anti-DRD2 antibodies and Cy-3-conjugated anti- mouse and Cy-2-conjugated anti-goat secondary antibodies. Nuclei are stained with DAPI. Representative image of immunofluorescence staining for DAPI (blue), CHL1 (green), and DRD2 (red) are shown and yellow signals show co- localizations. C, Close-ups of two regions indicated by boxes in (A). A-C, Scale bars: 20 µm. Three independent experiments were performed with different sets of animals

Techniques: Immunostaining, Staining, Immunofluorescence

FIGURE 8 Co-localization of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ and CHL1−/− mice were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies. Nuclei are stained with DAPI (blue). Representative images are shown at low (left and middle panel) and high (right panel) magnifications. Red spots indicate close molecular interaction of CHL1 with DRD2 in CHL1+/+ mice. CHL1−/− mice served as controls. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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 8 Co-localization of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ and CHL1−/− mice were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies. Nuclei are stained with DAPI (blue). Representative images are shown at low (left and middle panel) and high (right panel) magnifications. Red spots indicate close molecular interaction of CHL1 with DRD2 in CHL1+/+ mice. CHL1−/− mice served as controls. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Techniques: Proximity Ligation Assay, Staining

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

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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

Techniques: Proximity Ligation Assay, Immunostaining, Staining

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

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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

Techniques: Proximity Ligation Assay, Staining

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

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

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

Techniques: Isolation, Western Blot, Comparison, Derivative Assay

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