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control cells  (ATCC)


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    Structured Review

    ATCC control cells
    Control Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 2200 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/control cells/product/ATCC
    Average 98 stars, based on 2200 article reviews
    control cells - by Bioz Stars, 2026-05
    98/100 stars

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    Modulation of intracellular signaling pathways in HD, RA, and SLE cells exposed to environmental contaminants. Heatmap showing the relative expression and phosphorylation levels of key signaling proteins involved in immune regulation, inflammation, and cell survival (STAT1, STAT3, <t>p38,</t> AKT, and NFκB) and their phosphorylated forms in HD, RA, and SLE after exposure to PM, silica, and TCDD. Data are represented as z-score normalized values. Asterisks indicate statistically significant differences compared with the unstimulated control within each group (p < 0.05). AKT: protein kinase B; HD: healthy donors; NFκB: nuclear factor kappa-light-chain-enhancer of activated B cells; P: phosphorylated form; p38: p38 <t>mitogen-activated</t> <t>protein</t> <t>kinase;</t> PM: particulate matter; RA: rheumatoid arthritis; SLE: systemic lupus erythematosus; STAT: signal transducer and activator of transcription; TCDD: 2,3,7,8-tetrachlorodibenzo-p-dioxin.
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    Comprehensive functional validation of CTT Platform after cryopreservation and simulated transport. A) Schematic illustration of the experimental workflow. Fresh or cryopreserved PM@NSC (at −80 °C or −196 °C for 3 months) were thawed and subjected to a 4-h simulated transport at 4 °C prior to in vitro analysis or in vivo transplantation for SCI repair. B) Representative confocal microscopy images assessing post-thaw cell cytoskeletal integrity of NSCs loaded onto PM. Phalloidin (green) for F-actin; DAPI (blue) for nucleus. Scale bar: 50 μm. C) Western blot bands of Nestin, Sox2, and Ki67 show no significant differences in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. D) Representative confocal microscopy images assessing post-thaw cell viability of NSCs loaded onto PM. Calcein AM (green) for live cells; PI (red) for dead cells. Scale bar: 50 μm. E) Western blot bands of <t>Cleaved-Caspase3,</t> Bcl-2, and Bax protein expression in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. F) Quantitative analysis of cell survival rate of NSC in each group (n = 5). G) Quantitative analysis of Nestin/GAPDH, Ki67/GAPDH, and Sox2/β-Actin ratios in each group (n = 3). H) Quantitative analysis of Cleaved-Caspase3/GAPDH, Bcl-2/GAPDH and Bax/GAPDH ratios in each group (n = 3). I) Representative photographs of rat hindlimb motor functions in each group, 8 weeks after SCI. J) MEP results show variations in latency and amplitude in the left hind leg of each group 56 days after SCI K) H&E staining of gastrocnemius muscles indicated variations in muscle fiber morphology among the groups 56 days after SCI. Scale bar: 200 μm L) Sagittal and axial T2-weighted MRI images of rats in each group 56 days after SCI. M) Footprint analysis with print views, footfall patterns, 3D footprints, and 2D footprints revealing differences in gait patterns among separate groups. N) BBB scores demonstrate comparable locomotor functional recovery across all groups, including the Control group and the Cryopreserved-Transport treated group (n = 5). O) Quantitative analysis of gastrocnemius muscle fiber cross-sectional area, indicating similar muscle functional recovery (n = 5). P) Quantitative analysis of MEP latency and amplitude in the left hind leg in each group (n = 5). Q) Quantitative analysis of T2 density in sagittal and coronal planes in spinal cord lesions among groups (n = 5). R) Quantitative footprint analysis on day 56 post-injury included the maximum footprint intensity, footprint positioning, and the regularity index of the left hindlimb (n = 10). All data are presented as the mean ± SEM. Statistical analysis showed no significant differences (n.s.) among the experimental groups. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.
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    Comprehensive functional validation of CTT Platform after cryopreservation and simulated transport. A) Schematic illustration of the experimental workflow. Fresh or cryopreserved PM@NSC (at −80 °C or −196 °C for 3 months) were thawed and subjected to a 4-h simulated transport at 4 °C prior to in vitro analysis or in vivo transplantation for SCI repair. B) Representative confocal microscopy images assessing post-thaw cell cytoskeletal integrity of NSCs loaded onto PM. Phalloidin (green) for F-actin; DAPI (blue) for nucleus. Scale bar: 50 μm. C) Western blot bands of Nestin, Sox2, and Ki67 show no significant differences in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. D) Representative confocal microscopy images assessing post-thaw cell viability of NSCs loaded onto PM. Calcein AM (green) for live cells; PI (red) for dead cells. Scale bar: 50 μm. E) Western blot bands of <t>Cleaved-Caspase3,</t> Bcl-2, and Bax protein expression in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. F) Quantitative analysis of cell survival rate of NSC in each group (n = 5). G) Quantitative analysis of Nestin/GAPDH, Ki67/GAPDH, and Sox2/β-Actin ratios in each group (n = 3). H) Quantitative analysis of Cleaved-Caspase3/GAPDH, Bcl-2/GAPDH and Bax/GAPDH ratios in each group (n = 3). I) Representative photographs of rat hindlimb motor functions in each group, 8 weeks after SCI. J) MEP results show variations in latency and amplitude in the left hind leg of each group 56 days after SCI K) H&E staining of gastrocnemius muscles indicated variations in muscle fiber morphology among the groups 56 days after SCI. Scale bar: 200 μm L) Sagittal and axial T2-weighted MRI images of rats in each group 56 days after SCI. M) Footprint analysis with print views, footfall patterns, 3D footprints, and 2D footprints revealing differences in gait patterns among separate groups. N) BBB scores demonstrate comparable locomotor functional recovery across all groups, including the Control group and the Cryopreserved-Transport treated group (n = 5). O) Quantitative analysis of gastrocnemius muscle fiber cross-sectional area, indicating similar muscle functional recovery (n = 5). P) Quantitative analysis of MEP latency and amplitude in the left hind leg in each group (n = 5). Q) Quantitative analysis of T2 density in sagittal and coronal planes in spinal cord lesions among groups (n = 5). R) Quantitative footprint analysis on day 56 post-injury included the maximum footprint intensity, footprint positioning, and the regularity index of the left hindlimb (n = 10). All data are presented as the mean ± SEM. Statistical analysis showed no significant differences (n.s.) among the experimental groups. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.
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    Comprehensive functional validation of CTT Platform after cryopreservation and simulated transport. A) Schematic illustration of the experimental workflow. Fresh or cryopreserved PM@NSC (at −80 °C or −196 °C for 3 months) were thawed and subjected to a 4-h simulated transport at 4 °C prior to in vitro analysis or in vivo transplantation for SCI repair. B) Representative confocal microscopy images assessing post-thaw cell cytoskeletal integrity of NSCs loaded onto PM. Phalloidin (green) for F-actin; DAPI (blue) for nucleus. Scale bar: 50 μm. C) Western blot bands of Nestin, Sox2, and Ki67 show no significant differences in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. D) Representative confocal microscopy images assessing post-thaw cell viability of NSCs loaded onto PM. Calcein AM (green) for live cells; PI (red) for dead cells. Scale bar: 50 μm. E) Western blot bands of <t>Cleaved-Caspase3,</t> Bcl-2, and Bax protein expression in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. F) Quantitative analysis of cell survival rate of NSC in each group (n = 5). G) Quantitative analysis of Nestin/GAPDH, Ki67/GAPDH, and Sox2/β-Actin ratios in each group (n = 3). H) Quantitative analysis of Cleaved-Caspase3/GAPDH, Bcl-2/GAPDH and Bax/GAPDH ratios in each group (n = 3). I) Representative photographs of rat hindlimb motor functions in each group, 8 weeks after SCI. J) MEP results show variations in latency and amplitude in the left hind leg of each group 56 days after SCI K) H&E staining of gastrocnemius muscles indicated variations in muscle fiber morphology among the groups 56 days after SCI. Scale bar: 200 μm L) Sagittal and axial T2-weighted MRI images of rats in each group 56 days after SCI. M) Footprint analysis with print views, footfall patterns, 3D footprints, and 2D footprints revealing differences in gait patterns among separate groups. N) BBB scores demonstrate comparable locomotor functional recovery across all groups, including the Control group and the Cryopreserved-Transport treated group (n = 5). O) Quantitative analysis of gastrocnemius muscle fiber cross-sectional area, indicating similar muscle functional recovery (n = 5). P) Quantitative analysis of MEP latency and amplitude in the left hind leg in each group (n = 5). Q) Quantitative analysis of T2 density in sagittal and coronal planes in spinal cord lesions among groups (n = 5). R) Quantitative footprint analysis on day 56 post-injury included the maximum footprint intensity, footprint positioning, and the regularity index of the left hindlimb (n = 10). All data are presented as the mean ± SEM. Statistical analysis showed no significant differences (n.s.) among the experimental groups. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.
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    Expression levels of both initiator and effector caspases. (a) Caspase‐2, (b) caspase‐8, (c) caspase‐9, (d) caspase‐12, (e) caspase‐6, and (f) caspase‐3/7 activities in SNCA‐overexpressed <t>MRC‐5,</t> A549, and NCI‐H2170 were determined. Data were expressed as mean ± SEM of three independent experiments performed in triplicate ( n = 3). ∗ represents statistical significance (two‐way ANOVA followed by Tukey′s post hoc test, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001). SEM: standard error of mean; SNCA: alpha‐synuclein.
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    WiCell Research Institute Inc ips imr90 4 control ips cell line wicell
    Expression levels of both initiator and effector caspases. (a) Caspase‐2, (b) caspase‐8, (c) caspase‐9, (d) caspase‐12, (e) caspase‐6, and (f) caspase‐3/7 activities in SNCA‐overexpressed <t>MRC‐5,</t> A549, and NCI‐H2170 were determined. Data were expressed as mean ± SEM of three independent experiments performed in triplicate ( n = 3). ∗ represents statistical significance (two‐way ANOVA followed by Tukey′s post hoc test, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001). SEM: standard error of mean; SNCA: alpha‐synuclein.
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    Image Search Results


    Modulation of intracellular signaling pathways in HD, RA, and SLE cells exposed to environmental contaminants. Heatmap showing the relative expression and phosphorylation levels of key signaling proteins involved in immune regulation, inflammation, and cell survival (STAT1, STAT3, p38, AKT, and NFκB) and their phosphorylated forms in HD, RA, and SLE after exposure to PM, silica, and TCDD. Data are represented as z-score normalized values. Asterisks indicate statistically significant differences compared with the unstimulated control within each group (p < 0.05). AKT: protein kinase B; HD: healthy donors; NFκB: nuclear factor kappa-light-chain-enhancer of activated B cells; P: phosphorylated form; p38: p38 mitogen-activated protein kinase; PM: particulate matter; RA: rheumatoid arthritis; SLE: systemic lupus erythematosus; STAT: signal transducer and activator of transcription; TCDD: 2,3,7,8-tetrachlorodibenzo-p-dioxin.

    Journal: Journal of Translational Autoimmunity

    Article Title: Exploring the immunomodulatory effects of environmental contaminants on autoimmune patients: An in vitro approach

    doi: 10.1016/j.jtauto.2025.100341

    Figure Lengend Snippet: Modulation of intracellular signaling pathways in HD, RA, and SLE cells exposed to environmental contaminants. Heatmap showing the relative expression and phosphorylation levels of key signaling proteins involved in immune regulation, inflammation, and cell survival (STAT1, STAT3, p38, AKT, and NFκB) and their phosphorylated forms in HD, RA, and SLE after exposure to PM, silica, and TCDD. Data are represented as z-score normalized values. Asterisks indicate statistically significant differences compared with the unstimulated control within each group (p < 0.05). AKT: protein kinase B; HD: healthy donors; NFκB: nuclear factor kappa-light-chain-enhancer of activated B cells; P: phosphorylated form; p38: p38 mitogen-activated protein kinase; PM: particulate matter; RA: rheumatoid arthritis; SLE: systemic lupus erythematosus; STAT: signal transducer and activator of transcription; TCDD: 2,3,7,8-tetrachlorodibenzo-p-dioxin.

    Article Snippet: Membranes were stripped and re-probed for total AKT, NFκB p65, p38 MAPK, STAT1, STAT3, and β-actin (Cell Signaling Technology, Danvers, MA, USA; Santa Cruz Biotechnology, Dallas, TX, USA) as a loading control.

    Techniques: Protein-Protein interactions, Expressing, Phospho-proteomics, Control

    Comprehensive functional validation of CTT Platform after cryopreservation and simulated transport. A) Schematic illustration of the experimental workflow. Fresh or cryopreserved PM@NSC (at −80 °C or −196 °C for 3 months) were thawed and subjected to a 4-h simulated transport at 4 °C prior to in vitro analysis or in vivo transplantation for SCI repair. B) Representative confocal microscopy images assessing post-thaw cell cytoskeletal integrity of NSCs loaded onto PM. Phalloidin (green) for F-actin; DAPI (blue) for nucleus. Scale bar: 50 μm. C) Western blot bands of Nestin, Sox2, and Ki67 show no significant differences in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. D) Representative confocal microscopy images assessing post-thaw cell viability of NSCs loaded onto PM. Calcein AM (green) for live cells; PI (red) for dead cells. Scale bar: 50 μm. E) Western blot bands of Cleaved-Caspase3, Bcl-2, and Bax protein expression in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. F) Quantitative analysis of cell survival rate of NSC in each group (n = 5). G) Quantitative analysis of Nestin/GAPDH, Ki67/GAPDH, and Sox2/β-Actin ratios in each group (n = 3). H) Quantitative analysis of Cleaved-Caspase3/GAPDH, Bcl-2/GAPDH and Bax/GAPDH ratios in each group (n = 3). I) Representative photographs of rat hindlimb motor functions in each group, 8 weeks after SCI. J) MEP results show variations in latency and amplitude in the left hind leg of each group 56 days after SCI K) H&E staining of gastrocnemius muscles indicated variations in muscle fiber morphology among the groups 56 days after SCI. Scale bar: 200 μm L) Sagittal and axial T2-weighted MRI images of rats in each group 56 days after SCI. M) Footprint analysis with print views, footfall patterns, 3D footprints, and 2D footprints revealing differences in gait patterns among separate groups. N) BBB scores demonstrate comparable locomotor functional recovery across all groups, including the Control group and the Cryopreserved-Transport treated group (n = 5). O) Quantitative analysis of gastrocnemius muscle fiber cross-sectional area, indicating similar muscle functional recovery (n = 5). P) Quantitative analysis of MEP latency and amplitude in the left hind leg in each group (n = 5). Q) Quantitative analysis of T2 density in sagittal and coronal planes in spinal cord lesions among groups (n = 5). R) Quantitative footprint analysis on day 56 post-injury included the maximum footprint intensity, footprint positioning, and the regularity index of the left hindlimb (n = 10). All data are presented as the mean ± SEM. Statistical analysis showed no significant differences (n.s.) among the experimental groups. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.

    Journal: Bioactive Materials

    Article Title: Integrated cryopreservation-thawing-transplantation platform for neural stem cell-based spinal cord injury repair

    doi: 10.1016/j.bioactmat.2026.01.024

    Figure Lengend Snippet: Comprehensive functional validation of CTT Platform after cryopreservation and simulated transport. A) Schematic illustration of the experimental workflow. Fresh or cryopreserved PM@NSC (at −80 °C or −196 °C for 3 months) were thawed and subjected to a 4-h simulated transport at 4 °C prior to in vitro analysis or in vivo transplantation for SCI repair. B) Representative confocal microscopy images assessing post-thaw cell cytoskeletal integrity of NSCs loaded onto PM. Phalloidin (green) for F-actin; DAPI (blue) for nucleus. Scale bar: 50 μm. C) Western blot bands of Nestin, Sox2, and Ki67 show no significant differences in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. D) Representative confocal microscopy images assessing post-thaw cell viability of NSCs loaded onto PM. Calcein AM (green) for live cells; PI (red) for dead cells. Scale bar: 50 μm. E) Western blot bands of Cleaved-Caspase3, Bcl-2, and Bax protein expression in protein expression levels among control (fresh), cryopreserved (−80 °C/-196 °C), and cryopreservation (−80 °C/-196 °C)-transport groups. F) Quantitative analysis of cell survival rate of NSC in each group (n = 5). G) Quantitative analysis of Nestin/GAPDH, Ki67/GAPDH, and Sox2/β-Actin ratios in each group (n = 3). H) Quantitative analysis of Cleaved-Caspase3/GAPDH, Bcl-2/GAPDH and Bax/GAPDH ratios in each group (n = 3). I) Representative photographs of rat hindlimb motor functions in each group, 8 weeks after SCI. J) MEP results show variations in latency and amplitude in the left hind leg of each group 56 days after SCI K) H&E staining of gastrocnemius muscles indicated variations in muscle fiber morphology among the groups 56 days after SCI. Scale bar: 200 μm L) Sagittal and axial T2-weighted MRI images of rats in each group 56 days after SCI. M) Footprint analysis with print views, footfall patterns, 3D footprints, and 2D footprints revealing differences in gait patterns among separate groups. N) BBB scores demonstrate comparable locomotor functional recovery across all groups, including the Control group and the Cryopreserved-Transport treated group (n = 5). O) Quantitative analysis of gastrocnemius muscle fiber cross-sectional area, indicating similar muscle functional recovery (n = 5). P) Quantitative analysis of MEP latency and amplitude in the left hind leg in each group (n = 5). Q) Quantitative analysis of T2 density in sagittal and coronal planes in spinal cord lesions among groups (n = 5). R) Quantitative footprint analysis on day 56 post-injury included the maximum footprint intensity, footprint positioning, and the regularity index of the left hindlimb (n = 10). All data are presented as the mean ± SEM. Statistical analysis showed no significant differences (n.s.) among the experimental groups. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.

    Article Snippet: The primary antibodies used in this research are listed below: CD68 (Abcam, Cambridge, UK), CD206 (Abcam, Cambridge, UK), GFAP (Bioss, Beijing, China), iNOS (Abcam, Cambridge, UK), Tuj-1 (Abcam, Cambridge, UK), NF-200 (Invitrogen, CA, USA), MBP (Abcam, Cambridge, UK), HIF-1α (Abcam, Cambridge, UK), VEGFA (Abcam, Cambridge, UK), P-CaMKII (Abcam, Cambridge, UK), CaMKII (Abcam, Cambridge, UK), P-CREB (Cell Signaling Technology, USA), CREB (Cell Signaling Technology, USA), P-PI3K (Cell Signaling Technology, USA), PI3K (Cell Signaling Technology, USA), P-AKT (Cell Signaling Technology, USA), AKT (Cell Signaling Technology, USA), Cleaved-Caspase3 (Cell Signaling Technology, USA), Bcl-2 (Cell Signaling Technology, USA), Bax (Cell Signaling Technology, USA), GAPDH (Proteintech, IL, USA).

    Techniques: Functional Assay, Biomarker Discovery, In Vitro, In Vivo, Transplantation Assay, Confocal Microscopy, Western Blot, Expressing, Control, Staining, Muscles

    Expression levels of both initiator and effector caspases. (a) Caspase‐2, (b) caspase‐8, (c) caspase‐9, (d) caspase‐12, (e) caspase‐6, and (f) caspase‐3/7 activities in SNCA‐overexpressed MRC‐5, A549, and NCI‐H2170 were determined. Data were expressed as mean ± SEM of three independent experiments performed in triplicate ( n = 3). ∗ represents statistical significance (two‐way ANOVA followed by Tukey′s post hoc test, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001). SEM: standard error of mean; SNCA: alpha‐synuclein.

    Journal: BioMed Research International

    Article Title: SNCA Overexpression Induces Apoptosis in Non–Small Cell Lung Cancer via Caspase‐Dependent Signaling Pathways

    doi: 10.1155/bmri/2222343

    Figure Lengend Snippet: Expression levels of both initiator and effector caspases. (a) Caspase‐2, (b) caspase‐8, (c) caspase‐9, (d) caspase‐12, (e) caspase‐6, and (f) caspase‐3/7 activities in SNCA‐overexpressed MRC‐5, A549, and NCI‐H2170 were determined. Data were expressed as mean ± SEM of three independent experiments performed in triplicate ( n = 3). ∗ represents statistical significance (two‐way ANOVA followed by Tukey′s post hoc test, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001). SEM: standard error of mean; SNCA: alpha‐synuclein.

    Article Snippet: LUAD cell line (A549), LUSC cell line (NCI‐H2170), and human control lung cell (MRC‐5) were obtained from the American Tissue Cell Culture Collection (ATCC; Manassas, Virginia, United States).

    Techniques: Expressing