Caspase-1 activation of human and mouse brain tissue were analyzed by Western blot of cleaved caspase-1. IL-1β was quantified by ELISA. Microglial ASC speck formation was detected by immunohistochemistry. All mice were on C57/Bl6 background, including WT, NLRP3−/−,27 (link), APP/PS15 (link), APP/PS1/NLRP3−/−, Caspase-1−/−,28 (link), APP/PS1/Caspase-1−/− and were analyzed for cognitive function using the Morris Water Maze, the object recognition test and open field behavioural testing. Synaptic plasticity was determined by measuring long term potentiation (LTP) in acutely isolated hippocampal slices. Spine density was assessed by analyzing mid apical dendritic sections of pyramidal CA1 neurons. Cerebral Aβ load was determined by thioflavin-S-histochemistry of serial sections. Sequential extraction of homogenized brains by radio-immunoprecipitation assay, sodium dodecyl sulfate buffer and formic acid was employed to determine Aβ levels. Aβ nitration was determined by ELISA and immunohistochemistry using a specific antibodies against 3NTyr10 (link)-Aβ25 (link). Western blot detection was used to analyze the protein levels of APP, CTFs, Aβ, BACE1, IDE and NOS2. Inflammasome activation was confirmed by detection of ASC speck formation in microglia isolated from adult mouse. Microglial Aβ phagocytosis was determined after peripheral injection of methoxy-XO4, isolation of microglia and subsequent FACS analysis. Confirmatory immunocytochemistry was performed using antibody IC16 and the lysosomal marker LAMP2. Plaque morphology and microglial Aβ uptake was analyzed by coimmunostaining with Iba-1, methoxy-XO4 and IC16. mRNA levels of IDE, NEP, M1 and M2 markers were determined either from sorted microglia or from brain tissue by qPCR.
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Thioflavin S
Thioflavin S
Thioflavin S is a fluorescent dye used to detect the presence of amyloid fibrils in tissues.
It binds to the cross-beta-sheet structure of amyloid proteins, emitting a bright green fluorescence upon binding.
Thioflavin S has been widely employed in the study of neurodegenerative disorders, such as Alzheimer's disease, where it helps visualize the accumulation of amyloid plaques.
This AI-driven platform, PubCompare.ai, can assist researchers in optimizing their Thioflavin S protocols by identifying the best methods from scientific literature, preprints, and patents, ensuring reproducibility and accelerating research progress.
Discover the power of AI-driven protocol comparison today and elevate your Thioflavin S research to new heights!
It binds to the cross-beta-sheet structure of amyloid proteins, emitting a bright green fluorescence upon binding.
Thioflavin S has been widely employed in the study of neurodegenerative disorders, such as Alzheimer's disease, where it helps visualize the accumulation of amyloid plaques.
This AI-driven platform, PubCompare.ai, can assist researchers in optimizing their Thioflavin S protocols by identifying the best methods from scientific literature, preprints, and patents, ensuring reproducibility and accelerating research progress.
Discover the power of AI-driven protocol comparison today and elevate your Thioflavin S research to new heights!
Most cited protocols related to «Thioflavin S»
Adult
Antibodies
BACE1 protein, human
Biological Assay
Brain
Buffers
Caspase 1
Cognition
Dendrites
Enzyme-Linked Immunosorbent Assay
formic acid
Histocytochemistry
Homo sapiens
Immunocytochemistry
Immunoglobulins
Immunohistochemistry
Immunoprecipitation
Inflammasomes
Interleukin-1 beta
isolation
LAMP2 protein, human
Long-Term Potentiation
Lysosomes
Mice, Laboratory
Microglia
Morris Water Maze Test
Neuronal Plasticity
Nitrates
Nitric Oxide Synthase Type II
Phagocytosis
Proteins
Pyramidal Cells
RNA, Messenger
Senile Plaques
Sulfate, Sodium Dodecyl
thioflavine
Tissues
Vertebral Column
Western Blotting
Ante-mortem clinical history for age at onset of cognitive symptoms, education, and Mini-Mental State Examination (MMSE) score (Folstein et al., 1975 (link)) was retrospectively abstracted from clinical reports for the Mayo Clinic Jacksonville series, with investigators blinded to Thal amyloid phase. Time elapsed from age of onset and last MMSE to death was calculated by subtracting the date of onset or MMSE test date, respectively. Time was converted to years by dividing by 365.25. The final MMSE score was recorded if MMSE test date was within 3 years of death.
Upon neuropathologic examination, Mayo Clinic Jacksonville brains were received for evaluation with the left hemibrain formalin-fixed and the right frozen at −80°. Brain weight represents the fixed specimen that was calculated based upon doubling the weight of the available (usually left) hemibrain. A standardized dissection and sampling method was used as described previously (Terry et al., 1987 (link)). Tissue samples were processed and embedded in paraffin blocks. Mayo Clinic Rochester brains were sampled and examined according to the CERAD protocol (Mirra et al., 1991 (link)). Comparable cortical and subcortical slides were sent to Mayo Clinic Jacksonville for staining and assessment. Senile plaques and NFT were assessed and severity of amyloid angiopathy scored with thioflavin-S fluorescent microscopy, as previously described (Murray et al., 2011 (link)). The thioflavin-S staining protocol we used for these studies is sensitive to all senile plaque types (e.g. diffuse, cored, and neuritic) (Dickson et al., 1992 (link)), which were each included with a truncated maximum of 50 plaques per 3 mm2 using a ×10 objective (Supplementary Fig. 1 ). At the time of diagnosis Mayo Clinic Jacksonville brains were assigned a Braak NFT stage using thioflavin-S (Braak and Braak, 1991 (link)), with retrospective assessment on Mayo Clinic Rochester brains performed subsequent to thioflavin-S staining. Thal amyloid phase was assigned for Mayo Clinic Jacksonville brains by retrospectively assessing senile plaque quantification of neocortex (i.e. mid-frontal, inferior parietal or superior temporal cortex) and hippocampus using thioflavin-S staining results as supported in the latest NIA-AA recommendations (Hyman et al., 2012 (link); Montine et al., 2012 (link)). Neuropathologic reports were abstracted for non-database material on basal ganglia and cerebellum to complete Thal amyloid phase evaluation (Thal et al., 2002 (link)). We do not currently evaluate senile plaques in the superior colliculus or substantia nigra, but the CA4 of the hippocampus performs as well if not better (Thal et al., 2002 (link)). The maximum Thal amyloid phase was assigned if senile plaques were found in: Phase 1: neocortex; Phase 2: CA1/subiculum of the hippocampus; Phase 3: basal ganglia; Phase 4: CA4 of the hippocampus; and Phase 5: cerebellar molecular layer. Supplementary Fig. 1 illustrates regional assessment of senile plaques on thioflavin-S microscopy for Thal amyloid phase. TAR DNA binding protein 43 (TARDBP, previously known as TDP-43) positivity (Amador-Ortiz et al., 2007 (link)) and Lewy body disease type (Uchikado et al., 2006 (link)) was assessed using immunohistochemical methods, as previously described. The presence of significant vascular disease was based on Jellinger and Attems (2003) (link) incidence study. Global cerebral amyloid angiopathy was assessed using a semiquantitative severity measure of 0 = none; 1 = mild; 2 = moderate; 3 = severe from the most severely affected region.
PET imaging was performed in Mayo Clinic Rochester using the 11C amyloid tracer PiB with four 5-min dynamic frames acquired 40–60 min after injection, as previously described (Jack et al., 2008 (link); Kantarci et al., 2012a (link)). Standard corrections, co-registrations, and normalization to internal references were applied (Jack et al., 2008 (link); Kantarci et al., 2012a (link)). Briefly, PiB-PET images were co-registered to the T1-weighted MRI scan of the subject with a custom modified anatomical labelling atlas. Atlas labels in the custom template space were warped to the native T1 MRI space of the subject, as previously described (Kantarci et al., 2012a (link)). PiB-PET cortical regions of interest were partial volume corrected and included both grey matter and white matter without segmentation. PiB-PET uptake was normalized to cerebellar grey/white matter uptake to obtain SUV ratios for brain regions. The meta-region of interest used to measure cortical retention of PiB included an average of the bilateral prefrontal, orbitofrontal, temporal, parietal, anterior cingulate, posterior cingulate, and precuneus regions (Jack et al., 2008 (link)). Using our pipeline we defined the threshold for PiB-positivity at the cut-off point that corresponded to a 90% sensitivity of clinically diagnosed Alzheimer’s disease subjects with an abnormal PET scan (Jack et al., 2014 (link)), which corresponds to a PiB-PET SUV ratio ≥ 1.4.
For APOE genotyping, DNA was obtained from frozen brain tissue using standard protocols. Each sample was genotyped for APOE-ε2, -ε3, and -ε4 with TaqMan® chemistry (Applied Biosystems).
Upon neuropathologic examination, Mayo Clinic Jacksonville brains were received for evaluation with the left hemibrain formalin-fixed and the right frozen at −80°. Brain weight represents the fixed specimen that was calculated based upon doubling the weight of the available (usually left) hemibrain. A standardized dissection and sampling method was used as described previously (Terry et al., 1987 (link)). Tissue samples were processed and embedded in paraffin blocks. Mayo Clinic Rochester brains were sampled and examined according to the CERAD protocol (Mirra et al., 1991 (link)). Comparable cortical and subcortical slides were sent to Mayo Clinic Jacksonville for staining and assessment. Senile plaques and NFT were assessed and severity of amyloid angiopathy scored with thioflavin-S fluorescent microscopy, as previously described (Murray et al., 2011 (link)). The thioflavin-S staining protocol we used for these studies is sensitive to all senile plaque types (e.g. diffuse, cored, and neuritic) (Dickson et al., 1992 (link)), which were each included with a truncated maximum of 50 plaques per 3 mm2 using a ×10 objective (
PET imaging was performed in Mayo Clinic Rochester using the 11C amyloid tracer PiB with four 5-min dynamic frames acquired 40–60 min after injection, as previously described (Jack et al., 2008 (link); Kantarci et al., 2012a (link)). Standard corrections, co-registrations, and normalization to internal references were applied (Jack et al., 2008 (link); Kantarci et al., 2012a (link)). Briefly, PiB-PET images were co-registered to the T1-weighted MRI scan of the subject with a custom modified anatomical labelling atlas. Atlas labels in the custom template space were warped to the native T1 MRI space of the subject, as previously described (Kantarci et al., 2012a (link)). PiB-PET cortical regions of interest were partial volume corrected and included both grey matter and white matter without segmentation. PiB-PET uptake was normalized to cerebellar grey/white matter uptake to obtain SUV ratios for brain regions. The meta-region of interest used to measure cortical retention of PiB included an average of the bilateral prefrontal, orbitofrontal, temporal, parietal, anterior cingulate, posterior cingulate, and precuneus regions (Jack et al., 2008 (link)). Using our pipeline we defined the threshold for PiB-positivity at the cut-off point that corresponded to a 90% sensitivity of clinically diagnosed Alzheimer’s disease subjects with an abnormal PET scan (Jack et al., 2014 (link)), which corresponds to a PiB-PET SUV ratio ≥ 1.4.
For APOE genotyping, DNA was obtained from frozen brain tissue using standard protocols. Each sample was genotyped for APOE-ε2, -ε3, and -ε4 with TaqMan® chemistry (Applied Biosystems).
Alleles
Amygdaloid Body
Antemortem Diagnosis
Apolipoproteins E
Biological Assay
Blindness
Brain
Cerebrovascular Disorders
Cognition
Cognitive Impairments, Mild
Congenital Abnormality
Cortex, Cerebral
Dementia
Diagnosis
Formalin
Freezing
Genome
Immunoglobulins
Immunohistochemistry
Lewy Body Disease
MAPT protein, human
Microscopy
Mini Mental State Examination
Neuritis
Paraffin Embedding
Parietal Lobule
protein TDP-43, human
Protoplasm
Seahorses
Senile Plaques
Subiculum
Superior Temporal Gyrus
thioflavin S
Visual Cortex
Most recents protocols related to «Thioflavin S»
Thioflavin S staining was done directly on tissue sections used for MALDI-MSI on ITO coated slides after MALDI-MSI. Slides were first dipped in methanol and to remove DAN matrix and allowed to dry. Tissue was then fixed in 3% formaldehyde in PBS for 15 minutes. 1% Thioflavin S was made in 50 mL H2O and filtered prior to application. Tissue was first washed three times in 50% ethanol for three minutes each time. A three min H2O wash was then performed. 1% filtered thioflavin S was then applied to the samples for 10 minutes in the dark. All steps here on out were performed in the dark to preserve fluorescence. The tissue was then dehydrated using three, five-minute washes in 70% ethanol and three, three-minute washes in 50% ethanol. The tissue was then washed in dH2O for 15 minutes then allowed to air-dry for 15 minutes prior to coverslipping with Fluoroshield with DAPI.
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thioflavin S staining was performed to analyse tau tangles in the brains of tauopathy model mice upon MARK4 protein ablation. Briefly, after washing, slices were mounted on a glass slide and allowed to completely dry on a heat plate at 42°C, followed by incubation with 0.5 mM thioflavin S (Merck, T1892) in 50% ethanol for 7 min.35 (link),36 (link) The number of thioflavin S-positive puncta was quantified using default thresholding segmentation and measure-particle functions in ImageJ (U. S. National Institute of Health, Bethesda, Maryland, USA).
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Each tissue section was incubated in 500 μM of thioflavin-S (Sigma-Aldrich) solution, dissolved in 50% ethanol, for 7 min at room temperature, as described elsewhere [33 (link)]. Hoechst-33342 (10μg/mL, Sigma-Aldrich) was used to observe the nuclear morphology. Images were captured and analyzed in AXIO Observer inverted microscope (Carl Zeiss). The number and area of plaques detected by thioflavin-S were quantified using ImageJ software.
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Thioflavin-S staining was conducted 3 days after surgery on the sham group, I/R injury group, and I/R + pinacidil groups (0.1 and 0.5 mg/kg/day) to measure the benefits of pinacidil on no-reflow area according to previous study [29 (link)]. Similarly, Thioflavin-S staining was also performed on the sham and I/R groups that were transfected with or without AAV9-CRT. 2% thioflavin-S (MCE, USA) was dissolved in normal saline and injected into a different set of mice via the tail vein. After ten cardiac cycles, mouse hearts were immediately harvested, quickly washed with cold PBS, and fixed in 4% PFA overnight. The heart was cut into 1 mm slices, exposed to ultraviolet light, and photographed by a stereomicroscope (Leica, Germany). The no-reflow degree was calculated by the ratio of the dark area to the LV area.
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Tissue sections prepared on microscope slides were deparaffinized, rehydrated, and immersed in a solution of 0.002% (w/v) thioflavin S (Sigma-Aldrich, St. Louis, MO, USA) and 50% ethanol. Following sequential rinsing with 50% ethanol and PBS, nuclei were counterstained with 4′,6-diamidino-2-phenylindole dihydrochloride (DAPI). The sections were mounted using a commercially available mounting medium (Dako Denmark A/S, Glostrup, Denmark). The thioflavin S–labeled Aβ plaques and DAPI-stained nuclei were observed under a fluorescence microscope (Eclipse 80i, Nikon, Tokyo, Japan) at 100× magnification.
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Top products related to «Thioflavin S»
Sourced in United States, Germany, United Kingdom, Sao Tome and Principe, Canada
Thioflavin S is a fluorescent dye used in research as a labeling agent. It has the ability to selectively bind to and stain specific structures, such as amyloid fibrils. Thioflavin S exhibits an increased fluorescence upon binding, which makes it a useful tool for the detection and quantification of these structures in various applications.
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Thioflavin T is a fluorescent dye used in the detection and quantification of amyloid fibrils. It exhibits enhanced fluorescence upon binding to these protein aggregates. The dye is commonly utilized in various research applications, including the study of protein misfolding and amyloidosis.
Sourced in Germany, United States
Thioflavin S solution is a laboratory reagent used for the detection and visualization of amyloid fibrils. It is a fluorescent dye that binds specifically to beta-sheet structures in proteins, resulting in a characteristic yellowish-green fluorescence when exposed to ultraviolet light.
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The FLUOstar Omega is a multimode microplate reader designed for a variety of fluorescence, luminescence, and absorbance-based applications. It offers high-performance detection capabilities and supports a wide range of microplate formats.
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Thioflavin S (ThioS) is a fluorescent dye used in laboratory settings. It is primarily used to detect and visualize the presence of amyloid fibrils, which are insoluble protein aggregates associated with various neurodegenerative diseases. Thioflavin S binds to the beta-sheet structure of amyloid fibrils, causing them to fluoresce when exposed to specific wavelengths of light.
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Thio-S is a laboratory equipment product manufactured by Merck Group. It is a device used for the detection and analysis of sulfur-containing compounds. The core function of Thio-S is to provide accurate and reliable measurements of sulfur content in various samples, enabling researchers and analysts to better understand the composition and properties of their materials.
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Thioflavin S (ThS) is a fluorescent dye used in laboratory settings. It is a core component for the detection and quantification of amyloid fibrils.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
Sourced in Germany, United States
T1892 is a piece of laboratory equipment designed for use in scientific research and analysis. It serves as a tool for performing various tasks and measurements within a controlled laboratory environment.
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The BX51 microscope is an optical microscope designed for a variety of laboratory applications. It features a modular design and offers various illumination and observation methods to accommodate different sample types and research needs.
More about "Thioflavin S"
Thioflavin S, also known as ThioS or Thio-S, is a fluorescent dye widely used in the study of neurodegenerative disorders, such as Alzheimer's disease.
This dye binds to the cross-beta-sheet structure of amyloid proteins, emitting a bright green fluorescence upon binding.
This property makes Thioflavin S a valuable tool for visualizing the accumulation of amyloid plaques in tissues.
The FLUOstar Omega is a commonly used instrument for detecting and quantifying the fluorescence of Thioflavin S-bound amyloid fibrils.
Additionally, Thioflavin T, a related dye, is also employed in similar applications.
Bovine serum albumin (BSA) is sometimes used in conjunction with Thioflavin S to enhance the specificity and sensitivity of the assay.
Researchers can utilize the PubCompare.ai platform to optimize their Thioflavin S protocols by identifying the best methods from scientific literature, preprints, and patents.
This AI-driven approach ensures reproducibility and accelerates research progress in the field of neurodegenerative diseases.
The BX51 microscope is one of the instruments commonly used to visualize the Thioflavin S-stained amyloid deposits under fluorescent conditions.
Overall, Thioflavin S is a valuable tool in the study of amyloid-related disorders, and the PubCompare.ai platform can assist researchers in streamlining their experimental protocols and enhancing the quality of their research.
This dye binds to the cross-beta-sheet structure of amyloid proteins, emitting a bright green fluorescence upon binding.
This property makes Thioflavin S a valuable tool for visualizing the accumulation of amyloid plaques in tissues.
The FLUOstar Omega is a commonly used instrument for detecting and quantifying the fluorescence of Thioflavin S-bound amyloid fibrils.
Additionally, Thioflavin T, a related dye, is also employed in similar applications.
Bovine serum albumin (BSA) is sometimes used in conjunction with Thioflavin S to enhance the specificity and sensitivity of the assay.
Researchers can utilize the PubCompare.ai platform to optimize their Thioflavin S protocols by identifying the best methods from scientific literature, preprints, and patents.
This AI-driven approach ensures reproducibility and accelerates research progress in the field of neurodegenerative diseases.
The BX51 microscope is one of the instruments commonly used to visualize the Thioflavin S-stained amyloid deposits under fluorescent conditions.
Overall, Thioflavin S is a valuable tool in the study of amyloid-related disorders, and the PubCompare.ai platform can assist researchers in streamlining their experimental protocols and enhancing the quality of their research.