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anti α synuclein antibody syn211 (Santa Cruz Biotechnology)

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Santa Cruz Biotechnology anti α synuclein antibody syn211
$Small α-syn PFF seeds were prepared as described previously. 100 or 200 nM monomer equivalent small α-syn PFF seeds were incubated with or without 400, 500, 1600 nM SVD-1a for 3 days at 37 °C in PBS pH 7.4. A and B Time-dependent DLS measurements with 200 nM small α-syn PFF seeds in the absence ( A ) and presence ( B ) of 500 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent conditions every 60 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as a radius plot where the signal amplitude of each particle size is represented by the data point diameter. C One-phase exponential decay fit of “200 nM PFF + 500 nM SVD-1a” shown in ( B ). Fit was performed for particles in the range of 1–100 nm with an amplitude > 0.2. Outliers were excluded from fitting using a Q value of 1%. Fitting results: Span = 23.38 nm, rate constant = 0.132 1/s; half-life = 5.2 h. Fitting was performed using the “One phase exponential decay” fitting function from GraphPad Prism 10 (GraphPad Software Inc., USA). SVD-1a does not precipitate small α-syn PFF seeds as demonstrated by protein quantification after centrifugation, shown in Supplementary Fig. . D For AFM analysis, small α-syn PFF seeds pretreated with or without 400 and 1600 nM SVD-1a were incubated and dried on a freshly cleaved mica surface, followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using the NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown are representative of the observed species and particle density identified on all surface sections. E Exemplary Western blot of small α-syn PFF samples incubated with SVD-1a. 200 nM small α-syn PFFs (monomer equivalent) were incubated with increasing concentrations of SVD-1a for 72 h at 37 °C. PFF and monomer samples that were incubated without SVD-1a served as controls. α-Syn was detected with the antibody <t>Syn211.</t> A prominent α-syn monomer band was present at the expected molecular weight. Below the monomer bands, no further bands were visible. In the upper part of the blot, above the marker range, PFFs were detected, using a longer exposure time due to a weaker signal (see Supplementary Fig. for the whole blot image with different exposure times). F Size-based fractionation by centrifugal concentration followed by ELISA quantification. 200 nM small α-syn PFF (monomer equivalent) were incubated with or without SVD-1a together with a 200 nM monomer control for 72 h at 37 °C. After incubation, the samples were fractioned using a 100 kDa MWCO centrifugal concentrator (Merck, Microcon DNA Fast Flow 100 MWCO). α-Syn content of flow through (red) and retentate (blue) was quantified using an α-syn specific ELISA (BioLegend, Human α-Synuclein (Colorimetric), 448607). Shown are the fractions of the retentate and flow through as a percentage of the total concentration identified for each sample. A linear regression line (blue or red dotted lines) was included for the SVD-1a-treated samples (left) to underline the concentration dependency of the SVD-1a treatment effect. The fractions identified for the α-syn monomer control sample are shown as a bar graph (right). Notably, the sample treated with 1000 nM SVD-1a shows the same distribution as the monomer control. Data are shown as mean values with ±SD ( n = 3).$
Anti α Synuclein Antibody Syn211, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 615 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Images

1) Product Images from "Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide"

Article Title: Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide

Journal: NPJ Parkinson's Disease

doi: 10.1038/s41531-025-01132-7

$Small α-syn PFF seeds were prepared as described previously. 100 or 200 nM monomer equivalent small α-syn PFF seeds were incubated with or without 400, 500, 1600 nM SVD-1a for 3 days at 37 °C in PBS pH 7.4. A and B Time-dependent DLS measurements with 200 nM small α-syn PFF seeds in the absence ( A ) and presence ( B ) of 500 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent conditions every 60 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as a radius plot where the signal amplitude of each particle size is represented by the data point diameter. C One-phase exponential decay fit of “200 nM PFF + 500 nM SVD-1a” shown in ( B ). Fit was performed for particles in the range of 1–100 nm with an amplitude > 0.2. Outliers were excluded from fitting using a Q value of 1%. Fitting results: Span = 23.38 nm, rate constant = 0.132 1/s; half-life = 5.2 h. Fitting was performed using the “One phase exponential decay” fitting function from GraphPad Prism 10 (GraphPad Software Inc., USA). SVD-1a does not precipitate small α-syn PFF seeds as demonstrated by protein quantification after centrifugation, shown in Supplementary Fig. . D For AFM analysis, small α-syn PFF seeds pretreated with or without 400 and 1600 nM SVD-1a were incubated and dried on a freshly cleaved mica surface, followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using the NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown are representative of the observed species and particle density identified on all surface sections. E Exemplary Western blot of small α-syn PFF samples incubated with SVD-1a. 200 nM small α-syn PFFs (monomer equivalent) were incubated with increasing concentrations of SVD-1a for 72 h at 37 °C. PFF and monomer samples that were incubated without SVD-1a served as controls. α-Syn was detected with the antibody Syn211. A prominent α-syn monomer band was present at the expected molecular weight. Below the monomer bands, no further bands were visible. In the upper part of the blot, above the marker range, PFFs were detected, using a longer exposure time due to a weaker signal (see Supplementary Fig. for the whole blot image with different exposure times). F Size-based fractionation by centrifugal concentration followed by ELISA quantification. 200 nM small α-syn PFF (monomer equivalent) were incubated with or without SVD-1a together with a 200 nM monomer control for 72 h at 37 °C. After incubation, the samples were fractioned using a 100 kDa MWCO centrifugal concentrator (Merck, Microcon DNA Fast Flow 100 MWCO). α-Syn content of flow through (red) and retentate (blue) was quantified using an α-syn specific ELISA (BioLegend, Human α-Synuclein (Colorimetric), 448607). Shown are the fractions of the retentate and flow through as a percentage of the total concentration identified for each sample. A linear regression line (blue or red dotted lines) was included for the SVD-1a-treated samples (left) to underline the concentration dependency of the SVD-1a treatment effect. The fractions identified for the α-syn monomer control sample are shown as a bar graph (right). Notably, the sample treated with 1000 nM SVD-1a shows the same distribution as the monomer control. Data are shown as mean values with ±SD ( n = 3).$
Figure Legend Snippet: Small α-syn PFF seeds were prepared as described previously. 100 or 200 nM monomer equivalent small α-syn PFF seeds were incubated with or without 400, 500, 1600 nM SVD-1a for 3 days at 37 °C in PBS pH 7.4. A and B Time-dependent DLS measurements with 200 nM small α-syn PFF seeds in the absence ( A ) and presence ( B ) of 500 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent conditions every 60 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as a radius plot where the signal amplitude of each particle size is represented by the data point diameter. C One-phase exponential decay fit of “200 nM PFF + 500 nM SVD-1a” shown in ( B ). Fit was performed for particles in the range of 1–100 nm with an amplitude > 0.2. Outliers were excluded from fitting using a Q value of 1%. Fitting results: Span = 23.38 nm, rate constant = 0.132 1/s; half-life = 5.2 h. Fitting was performed using the “One phase exponential decay” fitting function from GraphPad Prism 10 (GraphPad Software Inc., USA). SVD-1a does not precipitate small α-syn PFF seeds as demonstrated by protein quantification after centrifugation, shown in Supplementary Fig. . D For AFM analysis, small α-syn PFF seeds pretreated with or without 400 and 1600 nM SVD-1a were incubated and dried on a freshly cleaved mica surface, followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using the NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown are representative of the observed species and particle density identified on all surface sections. E Exemplary Western blot of small α-syn PFF samples incubated with SVD-1a. 200 nM small α-syn PFFs (monomer equivalent) were incubated with increasing concentrations of SVD-1a for 72 h at 37 °C. PFF and monomer samples that were incubated without SVD-1a served as controls. α-Syn was detected with the antibody Syn211. A prominent α-syn monomer band was present at the expected molecular weight. Below the monomer bands, no further bands were visible. In the upper part of the blot, above the marker range, PFFs were detected, using a longer exposure time due to a weaker signal (see Supplementary Fig. for the whole blot image with different exposure times). F Size-based fractionation by centrifugal concentration followed by ELISA quantification. 200 nM small α-syn PFF (monomer equivalent) were incubated with or without SVD-1a together with a 200 nM monomer control for 72 h at 37 °C. After incubation, the samples were fractioned using a 100 kDa MWCO centrifugal concentrator (Merck, Microcon DNA Fast Flow 100 MWCO). α-Syn content of flow through (red) and retentate (blue) was quantified using an α-syn specific ELISA (BioLegend, Human α-Synuclein (Colorimetric), 448607). Shown are the fractions of the retentate and flow through as a percentage of the total concentration identified for each sample. A linear regression line (blue or red dotted lines) was included for the SVD-1a-treated samples (left) to underline the concentration dependency of the SVD-1a treatment effect. The fractions identified for the α-syn monomer control sample are shown as a bar graph (right). Notably, the sample treated with 1000 nM SVD-1a shows the same distribution as the monomer control. Data are shown as mean values with ±SD ( n = 3).

Techniques Used: Incubation, Software, Centrifugation, Gentle, Western Blot, Molecular Weight, Marker, Fractionation, Concentration Assay, Enzyme-linked Immunosorbent Assay, Control

Chromatin Immunoprecipitation:

Article Title: DAXX represents a new type of protein-folding enabler.
Article Snippet: Materials & experimental systems n/a Involved in the study Antibodies Eukaryotic cell lines Palaeontology Animals and other organisms Human research participants Clinical data Methods n/a Involved in the study ChIP-seq Flow cytometry MRI-based neuroimaging Antibodies Antibodies used Antibodies against the following proteins/epitopes were purchased from the indicated sources: GAPDH (sc-47724,Mouse, WB, IP, IF and IHC(P)), His (sc-8036, Mouse, IP, WB, IHC(P), ELISA, IF, FCM), GST (sc-138, Mouse, IP, WB, IHC(P), ELISA, IF, FCM), p53DO1 (sc-126, Mouse, WB, IP, IF, IHC(P) and FCM), Mdm2 (sc-965, Mouse, WB, IP, IF and IHC(P)), DAXX (sc-8043, Mouse IP,WB, IHC(P), ELISA, IF, FCM), α-synuclein syn211 (sc-12767, Mouse, IP, WB, IHC(P), ELISA, IF, and FCM) (Santa Cruz Biotechnology); Flag (#14793, Rabbit, WB, IP, IHC, ChIP, IF, FCM, ELISA) and DAXX (#4533S, Rabbit, WB, IP, IHC, ChIP, IF, FCM, ELISA) (Cell Signaling Technology); p53 (PAb1620, #OP33, Mouse, WB, IP, IF; PAb240, #OP29, Mouse, WB, IP), and Mdm2 (#OP46, Mouse, WB, IP) (Calbiochem); and HA (ab137838, Rabbit, WB, ICC/IF, IP) and Luciferase (ab21176, Rabbit, ICC/IF, WB) (Abcam); βAmyloid 1-42 (#805509) (BioLegend, Mouse, WB, IHC(P), ELISA).

Flow Cytometry:

Magnetic Resonance Imaging:

Western Blot:

Immunohistochemistry:

Enzyme-linked Immunosorbent Assay:

Immunocytochemistry:

Luciferase:

Binding Assay:

Electron Microscopy:

Sedimentation:

Dot Blot:

Incubation:

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fluorescent-labeled primary antibodies against total α-synuclein syn211 (Thermo Fisher)

Thermo Fisher fluorescent-labeled primary antibodies against total α-synuclein syn211

Comparison between levels of a-syn EVs in normal, AD, DLB, and PD patients. A) Levels of a-syn positive EVs in the four groups; B) Levels of CD32 a-syn EVs in the four groups C) Percentage of CD32 a-syn in the four groups; D) Receiving Operator Curve of identifying a-syn positive EVs compared to controls: sensitivity of 92.98% and a specificity of 78.95% at a cut-off of 20,700 <t>α-synuclein-EVs</t> per microliter of blood. *** indicates the first batch of samples where CD235a was used.

Fluorescent Labeled Primary Antibodies Against Total α Synuclein Syn211, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti α synuclein antibody syn211 (Santa Cruz Biotechnology)

Santa Cruz Biotechnology anti α synuclein antibody syn211
$Small α-syn PFF seeds were prepared as described previously. 100 or 200 nM monomer equivalent small α-syn PFF seeds were incubated with or without 400, 500, 1600 nM SVD-1a for 3 days at 37 °C in PBS pH 7.4. A and B Time-dependent DLS measurements with 200 nM small α-syn PFF seeds in the absence ( A ) and presence ( B ) of 500 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent conditions every 60 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as a radius plot where the signal amplitude of each particle size is represented by the data point diameter. C One-phase exponential decay fit of “200 nM PFF + 500 nM SVD-1a” shown in ( B ). Fit was performed for particles in the range of 1–100 nm with an amplitude > 0.2. Outliers were excluded from fitting using a Q value of 1%. Fitting results: Span = 23.38 nm, rate constant = 0.132 1/s; half-life = 5.2 h. Fitting was performed using the “One phase exponential decay” fitting function from GraphPad Prism 10 (GraphPad Software Inc., USA). SVD-1a does not precipitate small α-syn PFF seeds as demonstrated by protein quantification after centrifugation, shown in Supplementary Fig. . D For AFM analysis, small α-syn PFF seeds pretreated with or without 400 and 1600 nM SVD-1a were incubated and dried on a freshly cleaved mica surface, followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using the NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown are representative of the observed species and particle density identified on all surface sections. E Exemplary Western blot of small α-syn PFF samples incubated with SVD-1a. 200 nM small α-syn PFFs (monomer equivalent) were incubated with increasing concentrations of SVD-1a for 72 h at 37 °C. PFF and monomer samples that were incubated without SVD-1a served as controls. α-Syn was detected with the antibody <t>Syn211.</t> A prominent α-syn monomer band was present at the expected molecular weight. Below the monomer bands, no further bands were visible. In the upper part of the blot, above the marker range, PFFs were detected, using a longer exposure time due to a weaker signal (see Supplementary Fig. for the whole blot image with different exposure times). F Size-based fractionation by centrifugal concentration followed by ELISA quantification. 200 nM small α-syn PFF (monomer equivalent) were incubated with or without SVD-1a together with a 200 nM monomer control for 72 h at 37 °C. After incubation, the samples were fractioned using a 100 kDa MWCO centrifugal concentrator (Merck, Microcon DNA Fast Flow 100 MWCO). α-Syn content of flow through (red) and retentate (blue) was quantified using an α-syn specific ELISA (BioLegend, Human α-Synuclein (Colorimetric), 448607). Shown are the fractions of the retentate and flow through as a percentage of the total concentration identified for each sample. A linear regression line (blue or red dotted lines) was included for the SVD-1a-treated samples (left) to underline the concentration dependency of the SVD-1a treatment effect. The fractions identified for the α-syn monomer control sample are shown as a bar graph (right). Notably, the sample treated with 1000 nM SVD-1a shows the same distribution as the monomer control. Data are shown as mean values with ±SD ( n = 3).$
Anti α Synuclein Antibody Syn211, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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uk anti total asyn syn211 mab santa cruz biotechnology sc 12767 (Santa Cruz Biotechnology)

Santa Cruz Biotechnology uk anti total asyn syn211 mab santa cruz biotechnology sc 12767
$Small α-syn PFF seeds were prepared as described previously. 100 or 200 nM monomer equivalent small α-syn PFF seeds were incubated with or without 400, 500, 1600 nM SVD-1a for 3 days at 37 °C in PBS pH 7.4. A and B Time-dependent DLS measurements with 200 nM small α-syn PFF seeds in the absence ( A ) and presence ( B ) of 500 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent conditions every 60 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as a radius plot where the signal amplitude of each particle size is represented by the data point diameter. C One-phase exponential decay fit of “200 nM PFF + 500 nM SVD-1a” shown in ( B ). Fit was performed for particles in the range of 1–100 nm with an amplitude > 0.2. Outliers were excluded from fitting using a Q value of 1%. Fitting results: Span = 23.38 nm, rate constant = 0.132 1/s; half-life = 5.2 h. Fitting was performed using the “One phase exponential decay” fitting function from GraphPad Prism 10 (GraphPad Software Inc., USA). SVD-1a does not precipitate small α-syn PFF seeds as demonstrated by protein quantification after centrifugation, shown in Supplementary Fig. . D For AFM analysis, small α-syn PFF seeds pretreated with or without 400 and 1600 nM SVD-1a were incubated and dried on a freshly cleaved mica surface, followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using the NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown are representative of the observed species and particle density identified on all surface sections. E Exemplary Western blot of small α-syn PFF samples incubated with SVD-1a. 200 nM small α-syn PFFs (monomer equivalent) were incubated with increasing concentrations of SVD-1a for 72 h at 37 °C. PFF and monomer samples that were incubated without SVD-1a served as controls. α-Syn was detected with the antibody <t>Syn211.</t> A prominent α-syn monomer band was present at the expected molecular weight. Below the monomer bands, no further bands were visible. In the upper part of the blot, above the marker range, PFFs were detected, using a longer exposure time due to a weaker signal (see Supplementary Fig. for the whole blot image with different exposure times). F Size-based fractionation by centrifugal concentration followed by ELISA quantification. 200 nM small α-syn PFF (monomer equivalent) were incubated with or without SVD-1a together with a 200 nM monomer control for 72 h at 37 °C. After incubation, the samples were fractioned using a 100 kDa MWCO centrifugal concentrator (Merck, Microcon DNA Fast Flow 100 MWCO). α-Syn content of flow through (red) and retentate (blue) was quantified using an α-syn specific ELISA (BioLegend, Human α-Synuclein (Colorimetric), 448607). Shown are the fractions of the retentate and flow through as a percentage of the total concentration identified for each sample. A linear regression line (blue or red dotted lines) was included for the SVD-1a-treated samples (left) to underline the concentration dependency of the SVD-1a treatment effect. The fractions identified for the α-syn monomer control sample are shown as a bar graph (right). Notably, the sample treated with 1000 nM SVD-1a shows the same distribution as the monomer control. Data are shown as mean values with ±SD ( n = 3).$
Uk Anti Total Asyn Syn211 Mab Santa Cruz Biotechnology Sc 12767, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse monoclonal anti α synuclein syn211 antibody (Santa Cruz Biotechnology)

Santa Cruz Biotechnology mouse monoclonal anti α synuclein syn211 antibody
$Small α-syn PFF seeds were prepared as described previously. 100 or 200 nM monomer equivalent small α-syn PFF seeds were incubated with or without 400, 500, 1600 nM SVD-1a for 3 days at 37 °C in PBS pH 7.4. A and B Time-dependent DLS measurements with 200 nM small α-syn PFF seeds in the absence ( A ) and presence ( B ) of 500 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent conditions every 60 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as a radius plot where the signal amplitude of each particle size is represented by the data point diameter. C One-phase exponential decay fit of “200 nM PFF + 500 nM SVD-1a” shown in ( B ). Fit was performed for particles in the range of 1–100 nm with an amplitude > 0.2. Outliers were excluded from fitting using a Q value of 1%. Fitting results: Span = 23.38 nm, rate constant = 0.132 1/s; half-life = 5.2 h. Fitting was performed using the “One phase exponential decay” fitting function from GraphPad Prism 10 (GraphPad Software Inc., USA). SVD-1a does not precipitate small α-syn PFF seeds as demonstrated by protein quantification after centrifugation, shown in Supplementary Fig. . D For AFM analysis, small α-syn PFF seeds pretreated with or without 400 and 1600 nM SVD-1a were incubated and dried on a freshly cleaved mica surface, followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using the NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown are representative of the observed species and particle density identified on all surface sections. E Exemplary Western blot of small α-syn PFF samples incubated with SVD-1a. 200 nM small α-syn PFFs (monomer equivalent) were incubated with increasing concentrations of SVD-1a for 72 h at 37 °C. PFF and monomer samples that were incubated without SVD-1a served as controls. α-Syn was detected with the antibody <t>Syn211.</t> A prominent α-syn monomer band was present at the expected molecular weight. Below the monomer bands, no further bands were visible. In the upper part of the blot, above the marker range, PFFs were detected, using a longer exposure time due to a weaker signal (see Supplementary Fig. for the whole blot image with different exposure times). F Size-based fractionation by centrifugal concentration followed by ELISA quantification. 200 nM small α-syn PFF (monomer equivalent) were incubated with or without SVD-1a together with a 200 nM monomer control for 72 h at 37 °C. After incubation, the samples were fractioned using a 100 kDa MWCO centrifugal concentrator (Merck, Microcon DNA Fast Flow 100 MWCO). α-Syn content of flow through (red) and retentate (blue) was quantified using an α-syn specific ELISA (BioLegend, Human α-Synuclein (Colorimetric), 448607). Shown are the fractions of the retentate and flow through as a percentage of the total concentration identified for each sample. A linear regression line (blue or red dotted lines) was included for the SVD-1a-treated samples (left) to underline the concentration dependency of the SVD-1a treatment effect. The fractions identified for the α-syn monomer control sample are shown as a bar graph (right). Notably, the sample treated with 1000 nM SVD-1a shows the same distribution as the monomer control. Data are shown as mean values with ±SD ( n = 3).$
Mouse Monoclonal Anti α Synuclein Syn211 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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monoclonal anti-human mouse α-synuclein syn211 (Thermo Fisher)

Thermo Fisher monoclonal anti-human mouse α-synuclein syn211

<t>A30P-aSyn-O-induced</t> synaptic loss in primary dopaminergic neurons is mediated by calcineurin. Primary mouse midbrain dopaminergic neurons were treated with 5 µM of aSyn monomers <t>or</t> <t>oligomers</t> in the absence or in the presence of 2 µM of CsA for 24 h. Cells were immuno-stained with anti-MAP2 and anti-synapsin 1 antibodies ( A ). The number of synapses in each condition was evaluated by counting synaptic puncta ( B ). All experiments were performed at least three times and graphs are represented as mean and SD. Scale bar = 50 μm

Monoclonal Anti Human Mouse α Synuclein Syn211, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-α-synuclein syn211 (Millipore)

Millipore anti-α-synuclein syn211

Anti α Synuclein Syn211, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/%CE%B1+synuclein+syn211/antibody+syn211/pm36261424-274-18-22
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anti-human α-synuclein (syn211 (Millipore)

Millipore anti-human α-synuclein (syn211

Anti Human α Synuclein (Syn211, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results

Journal: PLoS ONE

Article Title: Poly (ADP-Ribose) and α–synuclein extracellular vesicles in patients with Parkinson disease: A possible biomarker of disease severity

doi: 10.1371/journal.pone.0264446

Figure Lengend Snippet: Comparison between levels of a-syn EVs in normal, AD, DLB, and PD patients. A) Levels of a-syn positive EVs in the four groups; B) Levels of CD32 a-syn EVs in the four groups C) Percentage of CD32 a-syn in the four groups; D) Receiving Operator Curve of identifying a-syn positive EVs compared to controls: sensitivity of 92.98% and a specificity of 78.95% at a cut-off of 20,700 α-synuclein-EVs per microliter of blood. *** indicates the first batch of samples where CD235a was used.

Article Snippet: Plasmas were diluted 1/10 th in PBS, and 10 microliters of diluted plasma were incubated with fluorescent-labeled primary antibodies against total α-synuclein (syn211, Thermo Fisher) and CD235a (clone HI264, Biolegend).

Techniques: Comparison

A) Levels of total a-syn EVs in PD and correlation with UPDRS scores; B) UPDRS scores and median levels of CD325a-syn EVs in PD; C) Levels of total a-syn EVs in PD and correlation with UPDRS scores; D) UPDRS scores and median levels of a-syn EVs in PD; E) Levels of total a-syn EVs in PD and correlation with UPDRS scores in replication cohort; F) UPDRS scores and median levels of a-syn EVs in PD in replication cohort.

Journal: PLoS ONE

Article Title: Poly (ADP-Ribose) and α–synuclein extracellular vesicles in patients with Parkinson disease: A possible biomarker of disease severity

doi: 10.1371/journal.pone.0264446

Figure Lengend Snippet: A) Levels of total a-syn EVs in PD and correlation with UPDRS scores; B) UPDRS scores and median levels of CD325a-syn EVs in PD; C) Levels of total a-syn EVs in PD and correlation with UPDRS scores; D) UPDRS scores and median levels of a-syn EVs in PD; E) Levels of total a-syn EVs in PD and correlation with UPDRS scores in replication cohort; F) UPDRS scores and median levels of a-syn EVs in PD in replication cohort.

Techniques:

A) Levels of total a-syn EVs in PD and correlation with PAR activity in PD. B) UPDRS scores and PAR activity in PD; C) Levels of total a-syn EVs in PD and correlation with PAR activity in PD in replication cohort; D) UPDRS scores and PAR activity in PD in replication cohort.

Journal: PLoS ONE

Article Title: Poly (ADP-Ribose) and α–synuclein extracellular vesicles in patients with Parkinson disease: A possible biomarker of disease severity

doi: 10.1371/journal.pone.0264446

Figure Lengend Snippet: A) Levels of total a-syn EVs in PD and correlation with PAR activity in PD. B) UPDRS scores and PAR activity in PD; C) Levels of total a-syn EVs in PD and correlation with PAR activity in PD in replication cohort; D) UPDRS scores and PAR activity in PD in replication cohort.

Techniques: Activity Assay

Journal: NPJ Parkinson's Disease

Article Title: Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide

doi: 10.1038/s41531-025-01132-7

Figure Lengend Snippet: Small α-syn PFF seeds were prepared as described previously. 100 or 200 nM monomer equivalent small α-syn PFF seeds were incubated with or without 400, 500, 1600 nM SVD-1a for 3 days at 37 °C in PBS pH 7.4. A and B Time-dependent DLS measurements with 200 nM small α-syn PFF seeds in the absence ( A ) and presence ( B ) of 500 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent conditions every 60 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as a radius plot where the signal amplitude of each particle size is represented by the data point diameter. C One-phase exponential decay fit of “200 nM PFF + 500 nM SVD-1a” shown in ( B ). Fit was performed for particles in the range of 1–100 nm with an amplitude > 0.2. Outliers were excluded from fitting using a Q value of 1%. Fitting results: Span = 23.38 nm, rate constant = 0.132 1/s; half-life = 5.2 h. Fitting was performed using the “One phase exponential decay” fitting function from GraphPad Prism 10 (GraphPad Software Inc., USA). SVD-1a does not precipitate small α-syn PFF seeds as demonstrated by protein quantification after centrifugation, shown in Supplementary Fig. . D For AFM analysis, small α-syn PFF seeds pretreated with or without 400 and 1600 nM SVD-1a were incubated and dried on a freshly cleaved mica surface, followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using the NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown are representative of the observed species and particle density identified on all surface sections. E Exemplary Western blot of small α-syn PFF samples incubated with SVD-1a. 200 nM small α-syn PFFs (monomer equivalent) were incubated with increasing concentrations of SVD-1a for 72 h at 37 °C. PFF and monomer samples that were incubated without SVD-1a served as controls. α-Syn was detected with the antibody Syn211. A prominent α-syn monomer band was present at the expected molecular weight. Below the monomer bands, no further bands were visible. In the upper part of the blot, above the marker range, PFFs were detected, using a longer exposure time due to a weaker signal (see Supplementary Fig. for the whole blot image with different exposure times). F Size-based fractionation by centrifugal concentration followed by ELISA quantification. 200 nM small α-syn PFF (monomer equivalent) were incubated with or without SVD-1a together with a 200 nM monomer control for 72 h at 37 °C. After incubation, the samples were fractioned using a 100 kDa MWCO centrifugal concentrator (Merck, Microcon DNA Fast Flow 100 MWCO). α-Syn content of flow through (red) and retentate (blue) was quantified using an α-syn specific ELISA (BioLegend, Human α-Synuclein (Colorimetric), 448607). Shown are the fractions of the retentate and flow through as a percentage of the total concentration identified for each sample. A linear regression line (blue or red dotted lines) was included for the SVD-1a-treated samples (left) to underline the concentration dependency of the SVD-1a treatment effect. The fractions identified for the α-syn monomer control sample are shown as a bar graph (right). Notably, the sample treated with 1000 nM SVD-1a shows the same distribution as the monomer control. Data are shown as mean values with ±SD ( n = 3).

Article Snippet: Anti-α-synuclein antibody Syn211 (RRID:AB_628318, Santa Cruz Biotechnology, Dallas, TX, USA) was used as primary antibody at a concentration of 1 μg/ml in TBS-T for 1 h at RT.

Techniques: Incubation, Software, Centrifugation, Gentle, Western Blot, Molecular Weight, Marker, Fractionation, Concentration Assay, Enzyme-linked Immunosorbent Assay, Control

A30P-aSyn-O-induced synaptic loss in primary dopaminergic neurons is mediated by calcineurin. Primary mouse midbrain dopaminergic neurons were treated with 5 µM of aSyn monomers or oligomers in the absence or in the presence of 2 µM of CsA for 24 h. Cells were immuno-stained with anti-MAP2 and anti-synapsin 1 antibodies ( A ). The number of synapses in each condition was evaluated by counting synaptic puncta ( B ). All experiments were performed at least three times and graphs are represented as mean and SD. Scale bar = 50 μm

Journal: Molecular Medicine

Article Title: The alpha-synuclein oligomers activate nuclear factor of activated T-cell (NFAT) modulating synaptic homeostasis and apoptosis

doi: 10.1186/s10020-023-00704-8

Figure Lengend Snippet: A30P-aSyn-O-induced synaptic loss in primary dopaminergic neurons is mediated by calcineurin. Primary mouse midbrain dopaminergic neurons were treated with 5 µM of aSyn monomers or oligomers in the absence or in the presence of 2 µM of CsA for 24 h. Cells were immuno-stained with anti-MAP2 and anti-synapsin 1 antibodies ( A ). The number of synapses in each condition was evaluated by counting synaptic puncta ( B ). All experiments were performed at least three times and graphs are represented as mean and SD. Scale bar = 50 μm

Article Snippet: After this period, the membrane was incubated with primary antibody against aSyn (Monoclonal anti-human mouse α-synuclein Syn211 Invitrogen™), against A11 oligomers (Polyclonal Rabbit Anti-amyloid oligomer A11 AB9234 Millipore™) and against amyloid fibers OC (Polyclonal Rabbit Anti-amyloid fibers OC AB2286 Millipore™) all at 1:1000 dilution for 18 h at 4 °C.

Techniques: Staining

A30P-aSyn-O-induced toxicity in differentiated N2a dopaminergic cells is dependent on NFAT activation. Differentiated N2a were treated with different concentrations of A30P-aSyn monomers (M), oligomers (O), and fibrils (F) in the absence or in the presence of 2 µM of CsA and cellular damage was evaluated by LDH release ( A ). The specific NFAT inhibitor VIVIT was able to prevent the cellular damaged caused by A30P-aSyn-O evaluated by LDH ( B ), crystal violet ( C ) or propidium iodide staining ( D ). All experiments were performed at least three times and graphs are represented as mean and SD where *p > 0.05, **p > 0.01 and ***p > 0.001

Journal: Molecular Medicine

Article Title: The alpha-synuclein oligomers activate nuclear factor of activated T-cell (NFAT) modulating synaptic homeostasis and apoptosis

doi: 10.1186/s10020-023-00704-8

Figure Lengend Snippet: A30P-aSyn-O-induced toxicity in differentiated N2a dopaminergic cells is dependent on NFAT activation. Differentiated N2a were treated with different concentrations of A30P-aSyn monomers (M), oligomers (O), and fibrils (F) in the absence or in the presence of 2 µM of CsA and cellular damage was evaluated by LDH release ( A ). The specific NFAT inhibitor VIVIT was able to prevent the cellular damaged caused by A30P-aSyn-O evaluated by LDH ( B ), crystal violet ( C ) or propidium iodide staining ( D ). All experiments were performed at least three times and graphs are represented as mean and SD where *p > 0.05, **p > 0.01 and ***p > 0.001

Techniques: Activation Assay, Staining

Synapsin 1 levels are decreased in the presence of A30P-aSyn oligomers in an NFAT-dependent pathway. Mouse primary hippocampal neurons ( A ) or differentiated N2a cells ( C ) were treated with A30P-aSyn-O (10 µM) in the absence or in the presence of VIVIT (10 µM) for 18 h. Genes responsive to NFAT pathway modulation found in the panel ( Syn1 , Tubb4 , Kalrn , Bcl-2A1A and Bim ) were validated by real time PCR. CA-NFAT-ER N2a cells were treated with 150 of OHT (Tamoxifen) and were analyzed after 24 h by real-time-PCR for the same genes ( E ). Western blot analyses were made for the same cells and treatments to assess expression level of Syn1 protein ( B , D , F ; left). β-Actin was used as loading control. Graphical representation of band intensities of Syn1 normalized to β-actin ( B , D , F ; right). Mouse primary hippocampal neurons were treated with 10 µM of A30P-aSyn-O in the absence or presence of 2 µM of CsA or 10 µM of VIVIT for 24 h. Cells were immunostained with anti-MAP2 and anti-synapsin-1 antibodies ( G ). All experiments were performed at least three times and graphs are represented as mean and SD where *p > 0.05, **p > 0.01 and ***p > 0.001. Scale bar = 10 μm

Journal: Molecular Medicine

Article Title: The alpha-synuclein oligomers activate nuclear factor of activated T-cell (NFAT) modulating synaptic homeostasis and apoptosis

doi: 10.1186/s10020-023-00704-8

Figure Lengend Snippet: Synapsin 1 levels are decreased in the presence of A30P-aSyn oligomers in an NFAT-dependent pathway. Mouse primary hippocampal neurons ( A ) or differentiated N2a cells ( C ) were treated with A30P-aSyn-O (10 µM) in the absence or in the presence of VIVIT (10 µM) for 18 h. Genes responsive to NFAT pathway modulation found in the panel ( Syn1 , Tubb4 , Kalrn , Bcl-2A1A and Bim ) were validated by real time PCR. CA-NFAT-ER N2a cells were treated with 150 of OHT (Tamoxifen) and were analyzed after 24 h by real-time-PCR for the same genes ( E ). Western blot analyses were made for the same cells and treatments to assess expression level of Syn1 protein ( B , D , F ; left). β-Actin was used as loading control. Graphical representation of band intensities of Syn1 normalized to β-actin ( B , D , F ; right). Mouse primary hippocampal neurons were treated with 10 µM of A30P-aSyn-O in the absence or presence of 2 µM of CsA or 10 µM of VIVIT for 24 h. Cells were immunostained with anti-MAP2 and anti-synapsin-1 antibodies ( G ). All experiments were performed at least three times and graphs are represented as mean and SD where *p > 0.05, **p > 0.01 and ***p > 0.001. Scale bar = 10 μm

Techniques: Real-time Polymerase Chain Reaction, Western Blot, Expressing

Schematic representation of the participation of NFAT on synapse degeneration in synucleinopathies. A specific population of aSyn-O present in the extracellular milieu could be inserted in the plasma membrane leading to leakage of calcium to the interior of the neurons. Upon calcium binding, activation of calcineurin takes place. This phosphatase dephosphorylates the hyperphosphorylated, inactive NFAT leading to its activation and translocation to the nucleus. There, NFAT binds to its cognate promoter sequences including the one that regulates the expression of the gene of synapsin 1 ( Syn1 ). NFAT downregulates the expression of this gene decreasing the amount synapsin 1, a protein that is involved in vesicle trafficking facilitating neurotransmitter release. This cascade of events leads to synapse degeneration one of the events observed in PD and other synucleionopathies

Journal: Molecular Medicine

Article Title: The alpha-synuclein oligomers activate nuclear factor of activated T-cell (NFAT) modulating synaptic homeostasis and apoptosis

doi: 10.1186/s10020-023-00704-8

Figure Lengend Snippet: Schematic representation of the participation of NFAT on synapse degeneration in synucleinopathies. A specific population of aSyn-O present in the extracellular milieu could be inserted in the plasma membrane leading to leakage of calcium to the interior of the neurons. Upon calcium binding, activation of calcineurin takes place. This phosphatase dephosphorylates the hyperphosphorylated, inactive NFAT leading to its activation and translocation to the nucleus. There, NFAT binds to its cognate promoter sequences including the one that regulates the expression of the gene of synapsin 1 ( Syn1 ). NFAT downregulates the expression of this gene decreasing the amount synapsin 1, a protein that is involved in vesicle trafficking facilitating neurotransmitter release. This cascade of events leads to synapse degeneration one of the events observed in PD and other synucleionopathies

Techniques: Binding Assay, Activation Assay, Translocation Assay, Expressing

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