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goat anti dscam antibody (R&D Systems)

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R&D Systems goat anti dscam antibody
Goat Anti Dscam Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+dscam/Human+DSCAM+Long+Isoform+Antibody/pm39532103-1010-44-48
Average 93 stars, based on 9 article reviews

goat anti dscam antibody - by Bioz Stars, 2026-10

93/100 stars

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Article Title: DSCAM regulates delamination of neurons in the developing midbrain.
Article Snippet: In fig. S2, the following three Dscam antibodies were used: rabbit anti-Dscam (1:100 to 1:5000; HPA019324; Atlas Antibodies, Stockholm, Sweden), rabbit antiDscam (1:100 to 1:5000; N-16, sc-79437; Santa Cruz Biotechnology), and goat anti-Dscam (1:100 to 1:5000; AF3666; R&D Systems).

Article Title: DSCAM regulates delamination of neurons in the developing midbrain
Article Snippet: In fig. S2, the following three Dscam antibodies were used: rabbit anti-Dscam (1:100 to 1:5000; HPA019324; Atlas Antibodies, Stockholm, Sweden), rabbit anti-Dscam (1:100 to 1:5000; N-16, sc-79437; Santa Cruz Biotechnology), and goat anti-Dscam (1:100 to 1:5000; AF3666; R&D Systems).

Expressing:

Article Title: Genetic Analysis of DSCAM's Role as a Netrin-1 Receptor in Vertebrates
Article Snippet: .. Using the described conditions, we could not see any difference in DSCAM expression in spinal cord sections of wild-type and DSCAM mutants using five different commercial antibodies: mouse anti-DSCAM (Millipore), rabbit anti-DSCAM (Novus), and goat anti-DSCAM (R&D Systems) used at a 1:100 dilution. .. This work was supported by grants from the Canadian Institutes of Health Research (Institutes of Genetics and Neuroscience, Mental Health and Addiction) to A.K., and by Genentech (P.H. and M.T.L.).

Produced:

Article Title: Neuronal DSCAM regulates the peri-synaptic localization of GLAST in Bergmann glia for functional synapse formation.
Article Snippet: The following primary antibodies were used: chick anti-GFP (1:500; ab13970; Abcam, Cambridge, UK), goat anti-Calbindin (1:500; AB_2571569; Frontier Institute, Hokkaido, Japan), guinea pig anti-vGluT2 (1:500; AB_2571621; Frontier Institute), goat anti-vGluT2 (1:500; AB_2571620; Frontier Institute), guinea pig anti-vGluT1 (1:500; AB5905; Millipore), guinea pig anti-VGAT (1;500; AB_2571624; Frontier Institute), rat anti-GFAP (1:500; 13-0300; Thermo Fisher Scientific, Waltham, MA, USA), goat anti-GLAST (1:500; AB_2571716; Frontier Institute), and rabbit anti-PKCγ (1:500; AB_2571824; Frontier Institute). .. For the detection of endogenous DSCAM in WT mice, the following primary antibodies were tested: rabbit anti-DSCAM (1:100–10000; LS-B5787-50; LifeSpan Biosystems, Minneapolis, MN, USA), mouse anti-DSCAM (1:100–10000; MAB2603; Millipore), rabbit anti-DSCAM(1:100–10000;NBP2-30716;NovusBiologicals, Centennial CO, USA), rabbit anti-DSCAM (1:100–10000; ORB156648; Biorbyt, Cambridge, UK), rabbit anti-DSCAM (1:100–10000; sc79437; Santa Cruz Biotechnology, Santa Cruz, CA, USA), rabbit anti-DSCAM (1:100–10000; HPA019324; Sigma-Aldrich, St. Louis, MO, USA), goat anti-DSCAM (1:100–10000; AF3666; R&D Systems, Minneapolis, MN, USA), and rabbit anti-DSCAM antibody produced in our laboratory (antigen: 1880-2008 amino acids). .. Specimenswere subsequently rinsedwith PBS and incubatedwith secondary antibodies of AffiPure F(ab’)2 Fragment conjugated with Alexa Fluor 488, 568, 594, or 647 (1:1,000; Jackson ImmunoResearch Laboratories, Baltimore Pile, PA, USA) orAlexa Fluor® (1:1,000; Abcam) andDAPI (5μg/mL; Invitrogen, Carlsbad, CA,USA) inblocking buffer in PBS at 25 °C for 2 h. To detect the DSCAM-ALFA in DscamALFA/ALFA mice, the cerebellar slices were incubated with pepsin solution (ab64201, Abcam) at 37 °C for 10min.

Article Title: Neuronal DSCAM regulates the peri-synaptic localization of GLAST in Bergmann glia for functional synapse formation
Article Snippet: The following primary antibodies were used: chick anti-GFP (1:500; ab13970; Abcam, Cambridge, UK), goat anti-Calbindin (1:500; AB_2571569; Frontier Institute, Hokkaido, Japan), guinea pig anti-vGluT2 (1:500; AB_2571621; Frontier Institute), goat anti-vGluT2 (1:500; AB_2571620; Frontier Institute), guinea pig anti-vGluT1 (1:500; AB5905; Millipore), guinea pig anti-VGAT (1;500; AB_2571624; Frontier Institute), rat anti-GFAP (1:500; 13-0300; Thermo Fisher Scientific, Waltham, MA, USA), goat anti-GLAST (1:500; AB_2571716; Frontier Institute), and rabbit anti-PKCγ (1:500; AB_2571824; Frontier Institute). .. For the detection of endogenous DSCAM in WT mice, the following primary antibodies were tested: rabbit anti-DSCAM (1:100–10000; LS-B5787-50; LifeSpan Biosystems, Minneapolis, MN, USA), mouse anti-DSCAM (1:100–10000; MAB2603; Millipore), rabbit anti-DSCAM (1:100–10000; NBP2-30716; Novus Biologicals, Centennial CO, USA), rabbit anti-DSCAM (1:100–10000; ORB156648; Biorbyt, Cambridge, UK), rabbit anti-DSCAM (1:100–10000; sc79437; Santa Cruz Biotechnology, Santa Cruz, CA, USA), rabbit anti-DSCAM (1:100–10000; HPA019324; Sigma-Aldrich, St. Louis, MO, USA), goat anti-DSCAM (1:100–10000; AF3666; R&D Systems, Minneapolis, MN, USA), and rabbit anti-DSCAM antibody produced in our laboratory (antigen: 1880-2008 amino acids). .. Specimens were subsequently rinsed with PBS and incubated with secondary antibodies of AffiPure F(ab’) 2 Fragment conjugated with Alexa Fluor 488, 568, 594, or 647 (1:1,000; Jackson ImmunoResearch Laboratories, Baltimore Pile, PA, USA) or Alexa Fluor® (1:1,000; Abcam) and DAPI (5 μg/mL; Invitrogen, Carlsbad, CA, USA) in blocking buffer in PBS at 25 °C for 2 h. To detect the DSCAM-ALFA in Dscam ALFA/ALFA mice, the cerebellar slices were incubated with pepsin solution (ab64201, Abcam) at 37 °C for 10 min.

Incubation:

Article Title: DSCAM gene triplication causes excessive GABAergic synapses in the neocortex in Down syndrome mouse models
Article Snippet: .. The blots were incubated overnight at 4°C with goat anti-DSCAM (R&D Systems, AF3666; 1:500), anti-APP (Cell Signaling Technology, 2452; 1:1,000), or mouse anti-tubulin (12G10, 1:5,000, DSHB). .. After washing, blots were incubated for 2 hours with HRP-conjugated secondary antibodies (1:5,000) and developed by chemiluminescence (Pierce, 32106).

Membrane:

Article Title: DSCAM and DSCAML1 regulate the radial migration and callosal projection in developing cerebral cortex.
Article Snippet: DSCAM together with its closely related protein DSCAML1 functions in dendritic selfavoidance of a certain types of interneuron in mammalian retina.. However, the functions of these DSCAMs in developing mammalian cerebral cortex are not well understood.. Here we reduced the expression of DSCAM or DSCAML1 in mouse cortical neurons by RNA interference both in vitro and in vivo.

Image Search Results

FIGURE 1 Search for DSCAML1 gene mutations in human neurodevelopmental disorders. (a) Location of human DSCAML1 mutations. The mutations shown above in the schematic of human DSCAML1 are from patients with ASD, ID/DD or schizophrenia. The red characters represent the inherited mutations from patients with ASD not found in ExAc and genomAD. The orange characters indicate the de novo mutations of ASD patients not found in ExAc and genomAD. The light blue characters are the de novo mutations from patients with intellectual disability/ developmental disorder (ID/DD). The purple characters are the mutations from patients with schizophrenia. The black characters indicate the inherited mutations from patients with ASD found in ExAc and genomAD. (b) Wild-type and the three mutations of DSCAML1 analyzed in this study. In the wild-type DSCAML1, the amino acid sequence at the C-terminal is shown, and the terminal three amino acids colored in blue is the PDZ-binding motif. In the C729R mutant DSCAML1, the cysteine, which is indispensable for the disulfide bond in the seventh Ig domain, is replaced with arginine. In the R1685* mutant, most intracellular domain is lost. In the K2108Nfs*37 mutant, the C-terminal 6 amino acids of DSCAML1, including PDZ-binding motif, are lost. Instead, 37 amino acids represented in red color are added

Journal: Genes to cells : devoted to molecular & cellular mechanisms

Article Title: Potential involvement of DSCAML1 mutations in neurodevelopmental disorders.

doi: 10.1111/gtc.12831

Figure Lengend Snippet: FIGURE 1 Search for DSCAML1 gene mutations in human neurodevelopmental disorders. (a) Location of human DSCAML1 mutations. The mutations shown above in the schematic of human DSCAML1 are from patients with ASD, ID/DD or schizophrenia. The red characters represent the inherited mutations from patients with ASD not found in ExAc and genomAD. The orange characters indicate the de novo mutations of ASD patients not found in ExAc and genomAD. The light blue characters are the de novo mutations from patients with intellectual disability/ developmental disorder (ID/DD). The purple characters are the mutations from patients with schizophrenia. The black characters indicate the inherited mutations from patients with ASD found in ExAc and genomAD. (b) Wild-type and the three mutations of DSCAML1 analyzed in this study. In the wild-type DSCAML1, the amino acid sequence at the C-terminal is shown, and the terminal three amino acids colored in blue is the PDZ-binding motif. In the C729R mutant DSCAML1, the cysteine, which is indispensable for the disulfide bond in the seventh Ig domain, is replaced with arginine. In the R1685* mutant, most intracellular domain is lost. In the K2108Nfs*37 mutant, the C-terminal 6 amino acids of DSCAML1, including PDZ-binding motif, are lost. Instead, 37 amino acids represented in red color are added

Article Snippet: Membranes were blocked with 0.5 % nonfat milk in Trisbuffered saline for 30 min and immunoblotted with rabbit anti- DSCAML1 (C- terminal recognition; Atlas Antibody, HPA035230, 1:500), goat anti- DSCAML1 (N- terminal recognition; R&D system, AF3315, 1:100) or mouse anti- β- actin (MBL, 177– 3, 1:1,000) antibodies.

Techniques: Sequencing, Binding Assay, Mutagenesis

FIGURE 2 Expression and localization of DSCAML1 mutant proteins. (a,b) Expression of DSCAML1 mutant proteins. The expression of DSCAML1WT and DSCAML1 mutant proteins was examined by immunoblotting with C-terminal (A) and N-terminal (b) recognizing antibodies. Red arrows represent DSCAML1 faint bands for DSCAML1K2108Nfs*37. (c–h) Localization of DSCAML1 mutant proteins. Immunostaining was performed using anti- N-terminal DSCAML1 antibody (magenta) and phalloidin (green). Extracellular or total DSCAML1 protein was stained without or with a detergent pretreatment, respectively. The orange arrowheads indicate DSCAML1 on the cell–cell contact sites. The scale bar shows 10 µm

Journal: Genes to cells : devoted to molecular & cellular mechanisms

Article Title: Potential involvement of DSCAML1 mutations in neurodevelopmental disorders.

doi: 10.1111/gtc.12831

Figure Lengend Snippet: FIGURE 2 Expression and localization of DSCAML1 mutant proteins. (a,b) Expression of DSCAML1 mutant proteins. The expression of DSCAML1WT and DSCAML1 mutant proteins was examined by immunoblotting with C-terminal (A) and N-terminal (b) recognizing antibodies. Red arrows represent DSCAML1 faint bands for DSCAML1K2108Nfs*37. (c–h) Localization of DSCAML1 mutant proteins. Immunostaining was performed using anti- N-terminal DSCAML1 antibody (magenta) and phalloidin (green). Extracellular or total DSCAML1 protein was stained without or with a detergent pretreatment, respectively. The orange arrowheads indicate DSCAML1 on the cell–cell contact sites. The scale bar shows 10 µm

Techniques: Expressing, Mutagenesis, Western Blot, Immunostaining, Staining

FIGURE 3 Glycosylation and degradation of DSCAML1 mutant proteins. (a) Glycosylation modification of DSCAML1WT and DSCAML1C729R. Extracellular DSCAML1 was immunoprecipitated with control IgG or the N-terminal DSCAML1 antibody and then was digested with either Endo H or PNGase F. (b) Effect of proteasome inhibitor on the expression of DSCAML1 mutant proteins. DSCAML1WT or DSCAML1 mutant clones were incubated with or without MG-132 for 24 hr. Then, immunoblotting was performed using indicated antibodies

Journal: Genes to cells : devoted to molecular & cellular mechanisms

Article Title: Potential involvement of DSCAML1 mutations in neurodevelopmental disorders.

doi: 10.1111/gtc.12831

Figure Lengend Snippet: FIGURE 3 Glycosylation and degradation of DSCAML1 mutant proteins. (a) Glycosylation modification of DSCAML1WT and DSCAML1C729R. Extracellular DSCAML1 was immunoprecipitated with control IgG or the N-terminal DSCAML1 antibody and then was digested with either Endo H or PNGase F. (b) Effect of proteasome inhibitor on the expression of DSCAML1 mutant proteins. DSCAML1WT or DSCAML1 mutant clones were incubated with or without MG-132 for 24 hr. Then, immunoblotting was performed using indicated antibodies

Techniques: Glycoproteomics, Mutagenesis, Modification, Immunoprecipitation, Control, Expressing, Clone Assay, Incubation, Western Blot

FIGURE 4 Adhesive function of DSCAML1 mutant proteins. The binding ability between mutant DSCAML1 and DSCAML1WT, or only between mutant DSCAML1 was evaluated. mCherry-labeled DSCAML1WT clone and each EGFP- labeled clone (Control, DSCAML1WT, DSCAML1C729R, DSCAML1R1685*, DSCAML1K2108Nfs*37) were mixed in the microtubes, respectively. Enlarged representative images were shown below the large panel. Scale bar: 100 µm. (a–e). Aggregates composed of at least two mCherry-positive cells and EGFP-positive cells (f) and aggregates composed of at least four EGFP-positive cells (g) were counted. The results are shown as box-and-whisker plots. Statistical analyses were performed between control and DSCAML1 (WT or mutant) clones (Brunner–Munzel test). The data of p-values are presented above

Journal: Genes to cells : devoted to molecular & cellular mechanisms

Article Title: Potential involvement of DSCAML1 mutations in neurodevelopmental disorders.

doi: 10.1111/gtc.12831

Figure Lengend Snippet: FIGURE 4 Adhesive function of DSCAML1 mutant proteins. The binding ability between mutant DSCAML1 and DSCAML1WT, or only between mutant DSCAML1 was evaluated. mCherry-labeled DSCAML1WT clone and each EGFP- labeled clone (Control, DSCAML1WT, DSCAML1C729R, DSCAML1R1685*, DSCAML1K2108Nfs*37) were mixed in the microtubes, respectively. Enlarged representative images were shown below the large panel. Scale bar: 100 µm. (a–e). Aggregates composed of at least two mCherry-positive cells and EGFP-positive cells (f) and aggregates composed of at least four EGFP-positive cells (g) were counted. The results are shown as box-and-whisker plots. Statistical analyses were performed between control and DSCAML1 (WT or mutant) clones (Brunner–Munzel test). The data of p-values are presented above

Techniques: Adhesive, Mutagenesis, Binding Assay, Labeling, Control, Whisker Assay, Clone Assay

FIGURE 5 Localization of DSCAML1 mutant proteins on the cell membrane of primary hippocampal neurons. Rat primary hippocampal cultures were prepared and co- electroporated with control, DSCAML1WT or DSCAML1 mutants plus mRFP at DIV0, respectively. The cultured neurons were fixed at DIV21. The cultured cells were first immunostained with N-terminal DSCAML1 antibody (a–e), followed by cell membrane permeabilization, then with mRFP antibody. A magnified image of the white dotted box region is shown below. Scale bars of the above or below images are 10 µm or 5 µm, respectively

Journal: Genes to cells : devoted to molecular & cellular mechanisms

Article Title: Potential involvement of DSCAML1 mutations in neurodevelopmental disorders.

doi: 10.1111/gtc.12831

Figure Lengend Snippet: FIGURE 5 Localization of DSCAML1 mutant proteins on the cell membrane of primary hippocampal neurons. Rat primary hippocampal cultures were prepared and co- electroporated with control, DSCAML1WT or DSCAML1 mutants plus mRFP at DIV0, respectively. The cultured neurons were fixed at DIV21. The cultured cells were first immunostained with N-terminal DSCAML1 antibody (a–e), followed by cell membrane permeabilization, then with mRFP antibody. A magnified image of the white dotted box region is shown below. Scale bars of the above or below images are 10 µm or 5 µm, respectively

Techniques: Mutagenesis, Membrane, Control, Cell Culture

FIGURE 6 Effect of DSCAML1 mutants on mature spine development. Effect of DSCAML1 mutants on matured spine formation in primary hippocampal neurons. The cultured cells are immunostained with anti-RFP and anti-PSD95 antibodies. Red indicates mRFP signal, and white indicates PSD95 signal. The magnified image of the white dotted box region above is shown below. Scale bars of the above or below images are 10 µm or 5 µm, respectively (a–e). Box- and-whisker plots for number of PSD95- positive mature spines. All experiments were performed in triplicate (N = 3). In each experiment, 7 cells were chosen. Three segments of dendrites with 20 µm length in each neuron were randomly obtained. The statistical analyses were performed by Brown–Forsythe test with Bonferroni correction (α = 0.05) (f). The stacked bar graphs showing numbers of categorized spines in transfected neurons. Asterisks show significant difference compared with control (p < 0.001) (Brunner–Munzel test) (g)

Journal: Genes to cells : devoted to molecular & cellular mechanisms

Article Title: Potential involvement of DSCAML1 mutations in neurodevelopmental disorders.

doi: 10.1111/gtc.12831

Figure Lengend Snippet: FIGURE 6 Effect of DSCAML1 mutants on mature spine development. Effect of DSCAML1 mutants on matured spine formation in primary hippocampal neurons. The cultured cells are immunostained with anti-RFP and anti-PSD95 antibodies. Red indicates mRFP signal, and white indicates PSD95 signal. The magnified image of the white dotted box region above is shown below. Scale bars of the above or below images are 10 µm or 5 µm, respectively (a–e). Box- and-whisker plots for number of PSD95- positive mature spines. All experiments were performed in triplicate (N = 3). In each experiment, 7 cells were chosen. Three segments of dendrites with 20 µm length in each neuron were randomly obtained. The statistical analyses were performed by Brown–Forsythe test with Bonferroni correction (α = 0.05) (f). The stacked bar graphs showing numbers of categorized spines in transfected neurons. Asterisks show significant difference compared with control (p < 0.001) (Brunner–Munzel test) (g)

Techniques: Cell Culture, Whisker Assay, Transfection, Control

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goat anti dscam antibody (R&D Systems)

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