Synaptotagmin, supplied by Synaptic Systems, used in various techniques. Bioz Stars score: 95/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Neuronal α‐amylase is important for neuronal activity and glycogenolysis and reduces in presence of amyloid beta pathology). Neuronal α‐amylase is important for neuronal activity and glycogenolysis and reduces in presence of amyloid beta pathology"
Article Title: Neuronal α‐amylase is important for neuronal activity and glycogenolysis and reduces in presence of amyloid beta pathology). Neuronal α‐amylase is important for neuronal activity and glycogenolysis and reduces in presence of amyloid beta pathology
Journal: Aging Cell
Figure Legend Snippet: Cellular localization of alpha (α)‐amylase in primary mouse neurons. Image in (a) shows immunofluorescent staining of α‐amylase with antibody directed against salivary α‐amylase (green) and neuronal marker microtubule‐associated protein 2 (MAP2) (magenta). The α‐amylase immunoreactivity is seen in the cell body (arrowhead) and along the dendrites (arrow). Confocal image in (b) shows a primary mouse neuronal process where α‐amylase staining (green) and phalloidin (magenta) are in close association. Confocal image in (c) shows immunofluorescent staining of primary mouse neuronal process where α‐amylase (green) and synaptotagmin (magenta) are in close association (arrow). Confocal image in (d) shows a close association between α‐amylase (green) and CAMKII (magenta) (arrow). Confocal image in (e) shows a primary mouse neuron stained against α‐amylase (green) and glycogen (magenta). The white squares indicate magnification of the area seen in (f and g). Arrows in (f‐g) indicate an close association between α‐amylase and glycogen. Scale bar in (a and e) indicates 5 μm, scale bar in (d and g) indicates 0.5 μm
Techniques Used: Staining, Marker
2) Product Images from "Aberrant Co-localization of Synaptic Proteins Promoted by Alzheimer’s Disease Amyloid-β Peptides: Protective Effect of Human Serum Albumin"
Article Title: Aberrant Co-localization of Synaptic Proteins Promoted by Alzheimer’s Disease Amyloid-β Peptides: Protective Effect of Human Serum Albumin
Journal: Journal of Alzheimer's Disease
Figure Legend Snippet: Effect of amyloid-beta peptides on PSD-95 and synaptotagmin localization. Neurons in primary culture (4 DIV) were incubated for 2 h in Hanks medium in the absence or the presence of 30 μM Aβ 25-35 , Aβ 40 , Aβ 42 , HSA, or HSA-Aβ complexes (C 25–35, C 40, C 42). After incubation, cells were fixed and immunocytochemistry against PSD-95 (in green) and against synaptotagmin (in red) was carried out. Images were taken using confocal microscopy. Orthogonal projections along the z-axis of the images are shown at the bottom and right. Scale bar: 20 μM
Techniques Used: Incubation, Immunocytochemistry, Confocal Microscopy
Figure Legend Snippet: Quantification of PSD-95, synaptotagmin fluorescence, and co-localization. Fluorescence (Integrated density) was measured in confocal photographs as those depicted in Fig. 8 using NIH Image J Software. Co-localization fluorescence is referred to concurrence points of green (PSD-95) and red (synaptotagmin) fluorescence. Results are expressed as percentages as compared to non-treated cells and are means±SEM ( n ≥24). One-way ANOVA and Dunnett Test were applied in order to compare different treatments vs. control. Distinct characters are used to indicate statistically different groups as compared to the control ( p
Techniques Used: Fluorescence, Software
3) Product Images from "Regulation of synaptic activity by snapin-mediated endolysosomal transport and sorting"
Article Title: Regulation of synaptic activity by snapin-mediated endolysosomal transport and sorting
Journal: The EMBO Journal
Figure Legend Snippet: Snapin-deficient neurons display enlarged presynaptic terminals retaining various degradative organelles A, B Representative electron micrographs (A) and quantitative analysis (B) showing aberrant accumulation of degradative organelles within enlarged presynaptic terminals of snapin − / − cortical neurons at DIV14. Colored arrowheads indicate various types of degradative organelles: red, AVs; blue, endosomal vacuoles; and green, MVBs/LEs. All these organelles were not readily observed at WT presynaptic terminals. C, D Representative images (C) and quantitative analysis (D) showing enhanced intensity of synaptophysin in snapin − / − neurons. Cortical neurons at DIV14 were co-immunostained with antibodies against SV protein synaptophysin (green) and dendritic marker MAP2 (red). E Sequential immunoblots of synaptosomal fractions (Syn), cytosolic fractions (Cytosol), and total brain lysates (Total) showing elevated endolysosomal marker LAMP-1 and autophagy marker LC3-II (red boxes) in synapse-enriched preparations from snapin cKO mice at P40. Snapin is relatively enriched in synaptosomal fractions in WT mouse brains and is almost absent in synaptosomes from snapin cKO animals (green box). Note that synaptic protein levels (i.e., synaptotagmin) are not necessarily increased in synaptosomal preparations from adult snapin cKO mice, while EM and immunocytochemistry revealed increased SVs levels in snapin − / − presynaptic terminals in in vitro culture conditions. A possible explanation for this discrepancy is that oversized and dysfunctional terminals might be eliminated by microglia in adult snapin cKO animals to optimize network activity and survival. Data information: Data were analyzed from the total number of electron micrographs (B) or neurons (D) indicated in parentheses (n) above bar graphs (B) or within bars (D) taken from three pairs of mice for each genotype and expressed as means ± s.e.m. with Student’s t -test (B) and Mann–Whitney U -test (D). P- values: *0.01–0.05; ***0.0001 to 0.001; ****
Techniques Used: Marker, Western Blot, Mouse Assay, Immunocytochemistry, In Vitro, Activity Assay, MANN-WHITNEY
4) Product Images from "Selected SALM (Synaptic Adhesion-Like Molecule) Family Proteins Regulate Synapse Formation"
Article Title: Selected SALM (Synaptic Adhesion-Like Molecule) Family Proteins Regulate Synapse Formation
Journal: The Journal of Neuroscience
Figure Legend Snippet: SALM3 and SALM5 induce the uptake of synaptotagmin lumenal domain antibodies in contacting axons of cocultured neurons. A–D , HEK293T cells were transfected with SALM2-Ecto, SALM3-Ecto, SALM5-Ecto, or EGFP-f (control), were cocultured with rat hippocampal neurons (DIV 9–12), followed by the incubation of the live neurons with synaptotagmin I (SynTag) lumenal domain antibodies to tag functional presynaptic nerve terminals and double staining for SynTag ( A1 , B1 , C1 , and D1 ) and EGFP ( A2 )/HA (for SALMs-Ecto; B2 , C2 , and D2 ). Scale bar, 15 μm. E , Quantification of the results from A–D . Mean ± SEM (EGFP-f, 5.5 ± 1.0, n = 17; SALM2-Ecto, 3.8 ± 0.1, n = 20; SALM3-Ecto, 25.5 ± 3.1, n = 26; SALM5-Ecto, 25.0 ± 2.6, n = 28; *** p
Techniques Used: Transfection, Incubation, Functional Assay, Double Staining
5) Product Images from "Regulated delivery of AMPA receptor subunits to the presynaptic membrane"
Article Title: Regulated delivery of AMPA receptor subunits to the presynaptic membrane
Journal: The EMBO Journal
Figure Legend Snippet: Fig. 7. Distribution of AMPA receptor subunits in subcellular fractions from synaptosomes. ( A ) The AMPA receptor subunits GluR2/3 and GluR1, the GluR2/3 binding partner GRIP, the NMDA receptor subunit NR1, the plasma membrane marker Na + /K + ATPase and the synaptic vesicle protein synaptophysin are all clearly detectable in the crude synaptosome fraction (P2). The crude synaptic vesicle fraction (LP2) obtained upon hypo-osmotic lysis of synaptosomes and differential centrifugation, contains GluR2/3, synaptophysin, GluR1 and GRIP. GluR2/3 and, at a much lesser extent, GluR1 and GRIP, are present, together with synaptophysin, in a synaptic vesicle fraction purified by continuous sucrose density gradient (SG-V). ( B ) Western blot analysis of a vesicular fraction immunoisolated from the SG-V fraction, using magnetic beads coated with antibodies directed against synaptotagmin. Note that synaptophysin (syp), synaptobrevin/VAMP2 (syb) and GluR2/3 are co-enriched in the immunoisolated fraction. ( C ) Western blot analysis of a highly purified synaptic vesicle fraction prepared via CPG-V reveals the presence of GluR2 and GluR1, together with synapsin I (syn I), in synaptic vesicles. Note the lack of GRIP immunoreactivity in the purified synaptic vesicles.
Techniques Used: Binding Assay, Marker, Lysis, Centrifugation, Purification, Western Blot, Magnetic Beads