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syt  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc syt
    Densitometric analysis of PSD95, <t>SYT,</t> <t>and</t> <t>SYP</t> protein levels of CTRL and BPA‐treated cells. The level of ACTIN protein was used as a loading control for protein normalization in western blot analysis. For both CTRL and BPA‐treated samples, each lane represents an independent biological replicate of the experiment. Values are reported as mean ± SEM. * p ≤ 0.05, ** p ≤ 0.01. Uncropped gels are provided in the Figure .
    Syt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+syt/Synaptotagmin-1+Rabbit+mAb/pmc12499904-59-18-20
    Average 93 stars, based on 41 article reviews
    syt - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Bisphenol A Treatment Impairs Synaptic Function in Human Cholinergic Neurons"

    Article Title: Bisphenol A Treatment Impairs Synaptic Function in Human Cholinergic Neurons

    Journal: Journal of Biochemical and Molecular Toxicology

    doi: 10.1002/jbt.70558

    Densitometric analysis of PSD95, SYT, and SYP protein levels of CTRL and BPA‐treated cells. The level of ACTIN protein was used as a loading control for protein normalization in western blot analysis. For both CTRL and BPA‐treated samples, each lane represents an independent biological replicate of the experiment. Values are reported as mean ± SEM. * p ≤ 0.05, ** p ≤ 0.01. Uncropped gels are provided in the Figure .
    Figure Legend Snippet: Densitometric analysis of PSD95, SYT, and SYP protein levels of CTRL and BPA‐treated cells. The level of ACTIN protein was used as a loading control for protein normalization in western blot analysis. For both CTRL and BPA‐treated samples, each lane represents an independent biological replicate of the experiment. Values are reported as mean ± SEM. * p ≤ 0.05, ** p ≤ 0.01. Uncropped gels are provided in the Figure .

    Techniques Used: Control, Western Blot

    Related Articles

    other:

    Article Title: Bushen-Tiansui Formula Improves Cognitive Functions in an A β 1–42 Fibril-Infused Rat Model of Alzheimer's Disease
    Article Snippet: Equal amounts of protein (30-40 μ g) were loaded for blotting with anti-p-TrkB/TrkB (1 : 1000, #sc-8058/#sc-7268, Santa Cruz Biotechnology, CA, USA), anti-p-Akt/Akt (1 : 1000, #4060/#9272), anti-p-CREB/CREB (1 : 500, #9189/#9197), anti-Syt (1 : 1000, #14558), and anti-PSD-95 (1 : 1000, #2507) (Cell Signaling Technology, Denver, MA, USA), and anti-BDNF (1 : 500, #108319, Abcam, Cambridge, UK).



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    Developmental Studies Hybridoma Bank syt1 igg
    ( A ) Illustration of a fluorophore (indicated as a red star) excited by a 3D donut beam (or bottle-beam shape; in blue) in minimal photon flux (MINFLUX) super resolution microscopy. ( B ) 2D schematic of the localization of a fluorophore by a 3D excitation beam progressively narrowing the probing pattern (illustrated by small blue dots) to precisely localize the fluorescent molecule. ( C ) Representative images of maximum Z-projection of syt7 (orange, MINFLUX), <t>syt1</t> (blue, MINFLUX), and bassoon (tan, confocal) from a FOV. Scale bar, 2 µm. ( D ) Zoomed-in merged images (i – vi; syt7, syt1, and bassoon) from (C); overlap of syt7 and syt1 is represented in green. Scale bar, 0.2 µm. ( E,F ) Histogram of nearest neighbor distances (NND) of syt7 to syt1, and syt1 to syt7, respectively. Both graphs showed a peak around 22 nm, with the syt7 to syt1 peak being ∼2.5 times larger than the syt1 to syt7 NND peak. The broad peak, centered around ∼150 nm in both plots, occurs for any two random fluorescent molecules imaged by MINFLUX. The data were well-fitted with two Gaussian functions (dotted lines). ( G ) 3D representation of syt7 (orange circles) and syt1 (blue triangles) clusters distributed around the bassoon centroid (red cross). Darker shades of color indicate positive values along the X and Y axes, and larger symbols indicate positive values along the Z axis. ( H-J ) 2D scatter plot generated from the 3D graph in (G), showing syt7 clusters, syt1 clusters, and their overlap projected along the XY axes, respectively. Projections along the XZ, and YZ axes are shown in fig. S17A-C. Protein clusters were grouped using different shades. Center (0,0) indicates the bassoon centroid obtained from confocal imaging. Dotted ellipses indicate the average size of an active zone, with major and minor axes of ∼500 nm and ∼200 nm, respectively. N=15 FOVs, across six independent neuronal cultures.
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    Cell Signaling Technology Inc syt
    Densitometric analysis of PSD95, <t>SYT,</t> <t>and</t> <t>SYP</t> protein levels of CTRL and BPA‐treated cells. The level of ACTIN protein was used as a loading control for protein normalization in western blot analysis. For both CTRL and BPA‐treated samples, each lane represents an independent biological replicate of the experiment. Values are reported as mean ± SEM. * p ≤ 0.05, ** p ≤ 0.01. Uncropped gels are provided in the Figure .
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    Image Search Results


    ( A ) Illustration of a fluorophore (indicated as a red star) excited by a 3D donut beam (or bottle-beam shape; in blue) in minimal photon flux (MINFLUX) super resolution microscopy. ( B ) 2D schematic of the localization of a fluorophore by a 3D excitation beam progressively narrowing the probing pattern (illustrated by small blue dots) to precisely localize the fluorescent molecule. ( C ) Representative images of maximum Z-projection of syt7 (orange, MINFLUX), syt1 (blue, MINFLUX), and bassoon (tan, confocal) from a FOV. Scale bar, 2 µm. ( D ) Zoomed-in merged images (i – vi; syt7, syt1, and bassoon) from (C); overlap of syt7 and syt1 is represented in green. Scale bar, 0.2 µm. ( E,F ) Histogram of nearest neighbor distances (NND) of syt7 to syt1, and syt1 to syt7, respectively. Both graphs showed a peak around 22 nm, with the syt7 to syt1 peak being ∼2.5 times larger than the syt1 to syt7 NND peak. The broad peak, centered around ∼150 nm in both plots, occurs for any two random fluorescent molecules imaged by MINFLUX. The data were well-fitted with two Gaussian functions (dotted lines). ( G ) 3D representation of syt7 (orange circles) and syt1 (blue triangles) clusters distributed around the bassoon centroid (red cross). Darker shades of color indicate positive values along the X and Y axes, and larger symbols indicate positive values along the Z axis. ( H-J ) 2D scatter plot generated from the 3D graph in (G), showing syt7 clusters, syt1 clusters, and their overlap projected along the XY axes, respectively. Projections along the XZ, and YZ axes are shown in fig. S17A-C. Protein clusters were grouped using different shades. Center (0,0) indicates the bassoon centroid obtained from confocal imaging. Dotted ellipses indicate the average size of an active zone, with major and minor axes of ∼500 nm and ∼200 nm, respectively. N=15 FOVs, across six independent neuronal cultures.

    Journal: bioRxiv

    Article Title: Alternative splicing of synaptotagmin 7 regulates oligomerization and short-term synaptic plasticity

    doi: 10.1101/2025.10.27.684894

    Figure Lengend Snippet: ( A ) Illustration of a fluorophore (indicated as a red star) excited by a 3D donut beam (or bottle-beam shape; in blue) in minimal photon flux (MINFLUX) super resolution microscopy. ( B ) 2D schematic of the localization of a fluorophore by a 3D excitation beam progressively narrowing the probing pattern (illustrated by small blue dots) to precisely localize the fluorescent molecule. ( C ) Representative images of maximum Z-projection of syt7 (orange, MINFLUX), syt1 (blue, MINFLUX), and bassoon (tan, confocal) from a FOV. Scale bar, 2 µm. ( D ) Zoomed-in merged images (i – vi; syt7, syt1, and bassoon) from (C); overlap of syt7 and syt1 is represented in green. Scale bar, 0.2 µm. ( E,F ) Histogram of nearest neighbor distances (NND) of syt7 to syt1, and syt1 to syt7, respectively. Both graphs showed a peak around 22 nm, with the syt7 to syt1 peak being ∼2.5 times larger than the syt1 to syt7 NND peak. The broad peak, centered around ∼150 nm in both plots, occurs for any two random fluorescent molecules imaged by MINFLUX. The data were well-fitted with two Gaussian functions (dotted lines). ( G ) 3D representation of syt7 (orange circles) and syt1 (blue triangles) clusters distributed around the bassoon centroid (red cross). Darker shades of color indicate positive values along the X and Y axes, and larger symbols indicate positive values along the Z axis. ( H-J ) 2D scatter plot generated from the 3D graph in (G), showing syt7 clusters, syt1 clusters, and their overlap projected along the XY axes, respectively. Projections along the XZ, and YZ axes are shown in fig. S17A-C. Protein clusters were grouped using different shades. Center (0,0) indicates the bassoon centroid obtained from confocal imaging. Dotted ellipses indicate the average size of an active zone, with major and minor axes of ∼500 nm and ∼200 nm, respectively. N=15 FOVs, across six independent neuronal cultures.

    Article Snippet: We also note that the syt1 IgG (DSHB, mAB48) has been extensively characterized and does not yield significant background signals using syt1 KO neurons ( , ; ).

    Techniques: Super-Resolution Microscopy, Generated, Imaging

    Densitometric analysis of PSD95, SYT, and SYP protein levels of CTRL and BPA‐treated cells. The level of ACTIN protein was used as a loading control for protein normalization in western blot analysis. For both CTRL and BPA‐treated samples, each lane represents an independent biological replicate of the experiment. Values are reported as mean ± SEM. * p ≤ 0.05, ** p ≤ 0.01. Uncropped gels are provided in the Figure .

    Journal: Journal of Biochemical and Molecular Toxicology

    Article Title: Bisphenol A Treatment Impairs Synaptic Function in Human Cholinergic Neurons

    doi: 10.1002/jbt.70558

    Figure Lengend Snippet: Densitometric analysis of PSD95, SYT, and SYP protein levels of CTRL and BPA‐treated cells. The level of ACTIN protein was used as a loading control for protein normalization in western blot analysis. For both CTRL and BPA‐treated samples, each lane represents an independent biological replicate of the experiment. Values are reported as mean ± SEM. * p ≤ 0.05, ** p ≤ 0.01. Uncropped gels are provided in the Figure .

    Article Snippet: Following blocking, the membranes were incubated overnight, at 4°C with primary antibodies against SYP (AB9272; Merk‐Millipore; dilution 1:80,000), SYT (#14558; Cell Signaling Technology; dilution 1:1000), PSD‐95 (#2507; Cell Signaling Technology; dilution 1:1000), PARP‐1 (AB‐83632; Immunological Science; dilution 1:1000), and CASP‐3 (sc‐271028; Santa Cruz; dilution 1:1000).

    Techniques: Control, Western Blot