model 680 automated gradient controller Search Results


elisa reader  (Bio-Rad)
93
Bio-Rad elisa reader
Elisa Reader, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/model+680+automated+gradient+controller/Lyphochek+Therapeutic+Drug+Monitoring+Control+(TDM)/pmc03773409-58-13-15
Average 93 stars, based on 1 article reviews
elisa reader - by Bioz Stars, 2026-08
93/100 stars
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phospho  (Cell Signaling Technology Inc)
97
Cell Signaling Technology Inc phospho
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Phospho, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/model+680+automated+gradient+controller/Phospho-p38+MAPK+(Thr180%2FTyr182)+Antibody/pm27605009-73-75-86
Average 97 stars, based on 1 article reviews
phospho - by Bioz Stars, 2026-08
97/100 stars
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manual injector  (Rheodyne lp)
90
Rheodyne lp manual injector
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Manual Injector, supplied by Rheodyne lp, 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/model+680+automated+gradient+controller/manual+injector/pm17329894-88-24-26
Average 90 stars, based on 1 article reviews
manual injector - by Bioz Stars, 2026-08
90/100 stars
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automated controlled-gradient freezing device  (Sy-Lab Gerate)
90
Sy-Lab Gerate automated controlled-gradient freezing device
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Automated Controlled Gradient Freezing Device, supplied by Sy-Lab Gerate, 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/model+680+automated+gradient+controller/automated+controlled+gradient+freezing+device/pmc03624011-49-6-9
Average 90 stars, based on 1 article reviews
automated controlled-gradient freezing device - by Bioz Stars, 2026-08
90/100 stars
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gradient controller  (Tosoh Corporation)
86
Tosoh Corporation gradient controller
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Gradient Controller, supplied by Tosoh Corporation, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/model+680+automated+gradient+controller/8020+ii+lc+model+multi+station+system/pm15966763-73-8-11
Average 86 stars, based on 1 article reviews
gradient controller - by Bioz Stars, 2026-08
86/100 stars
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k-mate controller  (Kongsberg Maritime Contros GmbH)
90
Kongsberg Maritime Contros GmbH k-mate controller
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
K Mate Controller, supplied by Kongsberg Maritime Contros GmbH, 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/model+680+automated+gradient+controller/k+mate+controller/10__3390_slash_rs12081344-144-0-4
Average 90 stars, based on 1 article reviews
k-mate controller - by Bioz Stars, 2026-08
90/100 stars
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kalman filtering  (Kongsberg Maritime Contros GmbH)
90
Kongsberg Maritime Contros GmbH kalman filtering
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Kalman Filtering, supplied by Kongsberg Maritime Contros GmbH, 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/model+680+automated+gradient+controller/kalman+filters/10__1016_slash_j__ifacol__2016__01__001-205-44-26
Average 90 stars, based on 1 article reviews
kalman filtering - by Bioz Stars, 2026-08
90/100 stars
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acoustic control systems  (Kongsberg Maritime Contros GmbH)
90
Kongsberg Maritime Contros GmbH acoustic control systems
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Acoustic Control Systems, supplied by Kongsberg Maritime Contros GmbH, 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/model+680+automated+gradient+controller/acoustic+control+systems/us09359853-692-0-7
Average 90 stars, based on 1 article reviews
acoustic control systems - by Bioz Stars, 2026-08
90/100 stars
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k-chief 600 alarm, monitoring, and control system  (Kongsberg Maritime Contros GmbH)
90
Kongsberg Maritime Contros GmbH k-chief 600 alarm, monitoring, and control system
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
K Chief 600 Alarm, Monitoring, And Control System, supplied by Kongsberg Maritime Contros GmbH, 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/model+680+automated+gradient+controller/k+chief+600+alarm++monitoring++control+system/10__3390_slash_jmse12101849-94-9-3
Average 90 stars, based on 1 article reviews
k-chief 600 alarm, monitoring, and control system - by Bioz Stars, 2026-08
90/100 stars
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air-defense systems  (Kongsberg Maritime Contros GmbH)
90
Kongsberg Maritime Contros GmbH air-defense systems
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Air Defense Systems, supplied by Kongsberg Maritime Contros GmbH, 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/model+680+automated+gradient+controller/air+defense+systems/10__1017_slash_eso__2021__54-74-20-12
Average 90 stars, based on 1 article reviews
air-defense systems - by Bioz Stars, 2026-08
90/100 stars
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ship control systems  (Kongsberg Maritime Contros GmbH)
90
Kongsberg Maritime Contros GmbH ship control systems
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
Ship Control Systems, supplied by Kongsberg Maritime Contros GmbH, 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/model+680+automated+gradient+controller/ship+control+systems/10__1017_slash_eso__2021__54-304-12-3
Average 90 stars, based on 1 article reviews
ship control systems - by Bioz Stars, 2026-08
90/100 stars
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sis (seafloor information system)  (Kongsberg Maritime Contros GmbH)
90
Kongsberg Maritime Contros GmbH sis (seafloor information system)
FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated <t>p38-MAPK</t> and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].
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FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated p38-MAPK and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: Stimulation of TLR4 Attenuates Alzheimer's Disease-Related Symptoms and Pathology in Tau-Transgenic Mice.

doi: 10.4049/jimmunol.1600873

Figure Lengend Snippet: FIGURE 7. Chronic mild stimulation of TLR4 facilitates autophagic–lysosomal degradation of phosphorylated Tau. Six-month-old Tau-transgenic mice were chronically treated with LPS and PBS. The brain was collected for the analysis of activated p38-MAPK and glycogen synthase kinase 3 with quantitative Western blot. (A–C) The ratios of phosphorylated (p-) and total protein (t-) of neither p38-MAPK (p38) nor glycogen synthase kinase 3a/b were altered by LPS treatments (t test, n = 6 per group). In the next experiment, brain sections of Tau-transgenic mice were analyzed under confocal microscope for the relationship between p-Tau and autophagic vacuoles. p-Tau was stained with red fluorescence and autophagic vacuoles were visualized by staining p62/SQSTM1 with green fluorophore–conjugated Abs. Colocalization of p-Tau and p62/SQSTM1 could be observed with yellow fluorescence, superimposing fluorescent images of p-Tau and p62/SQSTM1, in individual cells (D). The protein level of LAMP-1 in the whole-brain homogenate was also observed to be significantly higher in LPS-treated mice than in PBS-treated controls [(E); t test, n = 3 per group]. Thus, the lysosome-enriched brain homogenate fraction [(F), the fourth fraction] was isolated by Percoll gradient centrifugation. The p-Tau protein in the fourth fraction was quantified with Western blots with LAMP-1 as loading control. There was significantly more p-Tau protein in lysosomes isolated from LPS-treated Tau-transgenic mice than in lysosomes from PBS-treated littermate Tau mice [(G); t test, n = 4 and 3 for PBS- and LPS-treated mice, respectively]. To confirm autophagy- mediated p-Tau degradation, SH-SY5Y cells overexpressing DN and wt human ATG5 were cocultured with bone marrow–derived macrophages and treated with LPS at 0, 1, and 10 ng/ml. The p-Tau protein level in ATG5-wt cells was significantly decreased within 24 h after LPS treatment at 10 ng/ml, whereas the p-Tau protein in ATG5-DN cells was increased after the same treatment with LPS. (E and G) Group images from different parts of the same gel. [(H and I); two-way ANOVA showing effects of ATG5, and one-way ANOVA followed by Tukey post hoc tests showing effects of LPS treatments in ATG5 wt or DN cells; versus LPS treatment at 0 ng/ml: *p , 0.05, **p , 0.01; n = 3 per group].

Article Snippet: Proteins were then transferred onto polyvinylidene difluoride membranes and incubated overnight at 4 ̊C with the following Abs: rabbit mAbs against microtubule-associated protein 1 L chain 3B (LC3B; clone D11), beclin1 (clone D40C5), phospho– glycogen synthase kinase (GSK)-3a (clone D1G2), GSK-3a (clone D80E6), phospho–GSK-3b (clone D3A4), GSK-3b (clone 7C10), Munc18-1 (clone D4O6V), and lysosomal-associated membrane protein (Lamp)1 (clone C54H11) (all purchased from Cell Signaling Technology, Danvers, MA); rabbit polyclonal Abs against SQSTM1/p62 (catalog no. 5114), phospho–p38-MAPK (Thr180/Tyr182) (catalog no. 9211), p38MAPK (catalog no. 9212) (all from Cell Signaling Technology), and ionized calcium-binding adapter molecule (Iba)-1 (Wako Chemicals, Neuss, Germany); and mouse mAb against postsynaptic density protein 95 (PSD-95; clone 6G6-1C9; Abcam, Cambridge, U.K.).

Techniques: Transgenic Assay, Western Blot, Microscopy, Staining, Isolation, Gradient Centrifugation, Control, Derivative Assay