Journal: Dentistry Journal

Article Title: Investigation of the Molecular Profile of Granular Cell Tumours and Schwannomas of the Oral Cavity

doi: 10.3390/dj10030038

Figure Lengend Snippet: Summary of the antibodies used for immunohistochemistry of GCTs and schwannomas.

Article Snippet: GAP43 , Bio-Techne Canada, Oakville On, NB300-143 , Rabbit polyclonal , Regenerating neural tissues/growth cones, GAP43 intracellular growth protein/membrane protein , 1/5000.

Techniques: Immunohistochemistry, Cell Surface Receptor Assay, Membrane, Plasmid Preparation

Journal: Scientific Reports

Article Title: Expression and regulation of FRMD6 in mouse DRG neurons and spinal cord after nerve injury

doi: 10.1038/s41598-020-58261-7

Figure Lengend Snippet: Primary antibodies.

Article Snippet: GAP43 , Rabbit , IHC (Coons) , 1 μg/ml , Atlas Antibodies AB/HPA015600.

Techniques:

Journal: The Journal of Cell Biology

Article Title: Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex

doi: 10.1083/jcb.200507061

Figure Lengend Snippet: Ral regulates GAP-43 phosphorylation. (A) COS cells were transfected with the indicated myc-tagged Ral constructs and cGAP-43. Levels of phospho-cGAP-43 in cell extracts were determined by immunoblotting with an anti–phospho-GAP-43 antibody. A representative blot is shown. Inactive Ral causes a significant decrease of cGAP-43 phosphorylation (top band, arrow). (B) Quantitative analysis of phosphorylated cGAP-43 in COS cells transfected with cGAP-43 and the indicated Ral constructs. Shown here are data from four independent experiments (means ± SEM; *, P < 0.01). (C) Cortical neurons were nucleofected with the indicated constructs and lysed after overnight expression. Levels of total and phosphoendogenous GAP-43 were then assessed by immunoblotting. The fourth, fifth, and sixth lanes were derived from the same blot. (D) Quantitative analysis of endogenous GAP-43 phosphorylation in cortical neurons after nucleofection with the indicated Ral mutant isoforms. Data were derived from four independent experiments (means ± SEM; **, P < 0.005).

Article Snippet: Antibodies used were mouse anti-RalA, rabbit anti-RalB (BD Biosciences), mouse anti–GAP-43 (Autogen Bioclear), rabbit anti–phospho(Ser41)-GAP-43 (Zymed Laboratories), rat anti–α-tubulin (Harlan), rat anti-HA (Roche), mouse anti-myc (clone 9E10), rabbit anti-myc (Research Diagnostics, Inc.), mouse anti–βIII tubulin (Sigma-Aldrich), and rabbit anti-p38 (Santa Cruz Biotechnology, Inc.).

Techniques: Transfection, Construct, Western Blot, Expressing, Derivative Assay, Mutagenesis

Journal: The Journal of Cell Biology

Article Title: Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex

doi: 10.1083/jcb.200507061

Figure Lengend Snippet: GAP-43 acts downstream of Ral. (A) Constitutively active Ral increases branching in neurons plated on laminin (top middle and right) compared with EGFP-F–expressing cells (top left). This effect is reduced by coexpression of cGAP-43(S42A) (middle and bottom). Shown here are cells stained with anti-myc antibody to detect mutant Ral and anti–cGAP-43. Bar, 100 μm. (B) Quantitative analysis of branching in cells injected with single Ral isoforms or with Ral and cGAP-43(S42A) (means ± SEM: GFP, 3.30 ± 0.18; RalA72L, 8.43 ± 0.97; RalA72L + cGAP-43(S42A), 3.55 ± 0.44; RalB23V, 8.88 ± 0.85; RalB23V + cGAP-43(S42A), 4.29 ± 0.41; *, P < 0.02; **, P < 0.0001).

Article Snippet: Antibodies used were mouse anti-RalA, rabbit anti-RalB (BD Biosciences), mouse anti–GAP-43 (Autogen Bioclear), rabbit anti–phospho(Ser41)-GAP-43 (Zymed Laboratories), rat anti–α-tubulin (Harlan), rat anti-HA (Roche), mouse anti-myc (clone 9E10), rabbit anti-myc (Research Diagnostics, Inc.), mouse anti–βIII tubulin (Sigma-Aldrich), and rabbit anti-p38 (Santa Cruz Biotechnology, Inc.).

Techniques: Expressing, Staining, Mutagenesis, Injection

Journal: The Journal of Cell Biology

Article Title: Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex

doi: 10.1083/jcb.200507061

Figure Lengend Snippet: GAP-43 acts downstream of Ral. (A) A phosphomimetic GAP-43 protein, cGAP-43(S42D), restores branching in neurons plated on laminin and expressing dominant-negative Ral. Shown here are neurons expressing EGFP-F (top left), RalA28N (top middle), or RalB28N (bottom left) and RalA28N or RalB28N and cGAP-43(S42D) (right). Cells are stained with an anti-myc antibody to detect mutant Ral and an anti–cGAP-43 antibody. Bar, 50 μm. (B) Quantitative analysis of branching in cells plated on laminin and injected with single Ral isoforms or with Ral and cGAP-43(S42D) (means ± SEM: GFP, 3.47 ± 0.37; RalA28N, 1.74 ± 0.52; RalA28N + cGAP-43(S42D), 2.42 ± 0.31; RalB28N, 1.56 ± 0.41; RalB28N + cGAP-43(S42D), 3.72 ± 0.35; *, P < 0.04; **, P < 0.001). (C) SCG neurons were plated on polyornithine, microinjected, and left to express the indicated proteins for 5 h before laminin addition. Expression of dominant-negative Ral decreases branching compared with EGFP-F–expressing cells (top, compare middle and right with left). Branching is restored in cells coexpressing cGAP-43(S42D) (middle and bottom rows). Bar, 100 μm. (D) Quantitative analysis of branching in neurons initially plated on polyornithine and injected with single Ral isoforms or with Ral and cGAP-43(S42A) before laminin addition (means ± SEM: GFP, 2.64 ± 0.35; RalA28N, 1.05 ± 0.32; RalA28N + cGAP-43(S42D), 1.82 ± 0.40; RalB28N, 1.74 ± 0.30; RalB28N + cGAP-43(S42D), 2.73 ± 0.45; **, P < 0.01).

Article Snippet: Antibodies used were mouse anti-RalA, rabbit anti-RalB (BD Biosciences), mouse anti–GAP-43 (Autogen Bioclear), rabbit anti–phospho(Ser41)-GAP-43 (Zymed Laboratories), rat anti–α-tubulin (Harlan), rat anti-HA (Roche), mouse anti-myc (clone 9E10), rabbit anti-myc (Research Diagnostics, Inc.), mouse anti–βIII tubulin (Sigma-Aldrich), and rabbit anti-p38 (Santa Cruz Biotechnology, Inc.).

Techniques: Expressing, Dominant Negative Mutation, Staining, Mutagenesis, Injection

Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

Article Title: Microglia‐Mediated Neuroimmune Response Regulates Cardiac Remodeling After Myocardial Infarction

doi: 10.1161/JAHA.122.029053

Figure Lengend Snippet: A , Representation examples of ECGs in each group (Sham, MI 3 days, MI 14 days). B , Analysis of QT interval and QTc in each group, n=6–7. C , Representative Western blotting bands and quantitative analysis for CX43 (connexin 43) in each group 14 days after MI, n=5. D , HRV parameters (LF, HF, and LF/HF) in each group, n=7. E , NE levels in the heart and serum were detected by ELISA kits 14 days after MI, n=6 in the heart and n=9–11 in the serum. F , Representative Western blotting bands and quantitative analysis for TH in each group 14 days after MI, n=5. G , Representative Western blotting bands and quantitative analysis for CHAT in each group 14 days after MI, n=5. H , Immunofluorescence of GAP43 in infarct border zone 14 days after MI, bar=50μm, n=5. I , Immunofluorescence of NPY in infarct border zone 14 days after MI, bar=50 μm, n=5. Data are presented as mean±SD and analyzed using 2‐way ANOVA followed by Tukey test. * P <0.05, # P <0.05. CHAT indicates choline acetyltransferase; CX43, connexin 43; DAPI, 4,6‐diamidino‐2‐phenylindole; DMSO, dimethyl sulfoxide; GAP43, growth‐associated protein 43; HF, high frequency; HRV, heart rate variability; icv., intracerebroventricular injection; LF, low frequency; NE, norepinephrine; NPY, neuropeptide Y; and TH, tyrosine hydroxylase.

Article Snippet: Primary antibodies used in cardiac tissue included Ly6G (Servicebio), CX43 (Servicebio), TH (tyrosine hydroxylase) (Servicebio), CHAT (Servicebio), GAP43 (growth associated protein 43) (Servicebio), and NPY (neuropeptide Y) (Boster).

Techniques: Western Blot, Enzyme-linked Immunosorbent Assay, Immunofluorescence, Injection