polytron pt 10 35 probe homogenizer Search Results


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In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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Bioanalytical Systems Inc microdialysis probes
In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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New England Biolabs target probe hybridization
In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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Corning Life Sciences tissue-culture treated culture dishes
In <t>vitro</t> <t>microdialysis</t> to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA <t>MWCO</t> membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.
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In vitro microdialysis to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA MWCO membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.

Journal: The Journal of Neuroscience

Article Title: In Vivo Assessment of Brain Interstitial Fluid with Microdialysis Reveals Plaque-Associated Changes in Amyloid-β Metabolism and Half-Life

doi: 10.1523/JNEUROSCI.23-26-08844.2003

Figure Lengend Snippet: In vitro microdialysis to measure Aβ. A, Diagram of exchangeable Aβ. Triangles represent potential Aβ binding molecules, e.g., apoE, clusterin, and α2M. Only highlighted Aβ molecules are of the appropriate size to pass through a 35 kDA MWCO membrane on the microdialysis probe. B, Interpolated zero flow method to quantify the pool of measurable Aβ1-x and Aβ40 within samples of human CSF (n = 4). At 2.2 μl/min, the percentage recovery of eAβ was 9.74 ± 1.53% (mean ± SEM). C, In vitro percentage recoveries for each Aβ species using the interpolated zero flow method. Each recovery point contains error bars and are overlapping for each species (n = 4). In vitro recovery of each Aβ species by microdialysis is the same. D, The concentration of eAβ and total soluble Aβ are highly correlated within a sample of human CSF (Pearson's r = 0.9487; p < 0.0001; n = 9). The mean concentrations of soluble Aβ1-x and eAβ1-x were 30.47 ± 4.23 ng/ml (mean ± SEM) and 196.2 ± 28.65pg/ml, respectively. E, F, Human CSF immunoprecipitated (IP'd) for Aβ has undetectable levels of total soluble Aβ and eAβ. Human CSF spiked with an amount of exogenous Aβ40 peptide expected to double Aβ concentration resulted in a 2.1-fold increase in total soluble Aβ and a 1.9-fold increase in eAβ.

Article Snippet: Microdialysis probes used for in vitro experiments had a 4 mm, 35 kDa molecular weight cutoff (MWCO) membrane (BR-4-10 probes; Bioanalytical Systems, West Lafayette, IN) and were connected to a microdialysis peristaltic pump (MAB20; SciPro, Sanborn, NY) using teflon (FEP) tubing (inner diameter, 0.12 mm; 1.2 μl/10 cm; SciPro).

Techniques: In Vitro, Binding Assay, Membrane, Concentration Assay, Immunoprecipitation