murine cd4 t cells  (ATCC)


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    ATCC murine cd4 t cells
    TRAIL-R inhibits proximal TCR signaling and T cell activation. a Flow cytometry analyses of T cell activation markers — CD69 and CD25 (24 h), ( b ) carboxyfluorescein diacetate succinimidyl diester dilution assays (96 h), and ( c ) intracellular staining of IL-2 (24 h) on Trail-r +/+ or Trail-r –/– murine splenic <t>CD4</t> + T cells stimulated with anti-CD3 (3 µg/ml) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL). Data in a–c represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. d Trail-r +/+ murine splenic CD4 + T cells were stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Total RNA was extracted and sequenced on the Illumina platform. Principal component analysis represented correlations among groups. Network analysis of biological process Gene Ontology term enrichment among significant genes in the indicated comparisons. Node color is proportional to p -adjusted enrichment value; node size proportional to number of genes in each Gene Ontology term. Heatmap showing two differentially expressed genes in TCR signaling pathway. Color bars indicate scores of log 2 -fold change for each comparison. e ELISAs of lysates from Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Data represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. f Immunoblotting of phosphorylation of TCR tyrosine kinases in Trail-r + / + or Trail-r −/− murine splenic CD4 + T cells at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. g Trail-r + / + or Trail-r −/− CD4 + T cells were stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in presence/absence of TRAIL (10 µg/mL) for 30 min, then lysed and fractionated as raft and non-raft layers; Lck, ZAP70, LAT, and PLCγ1 were immunoblotted from pooled raft or non-raft fractions. h Representative confocal images of Trail-r + / + murine splenic CD4 + T cells following staining with anti-GM-1 (red) and anti-Lck (green), or anti-ZAP70 (green) Abs, as indicated. Colocalization of GM-1 with Lck or ZAP70 is indicated by yellow areas. Scale bar: 4 µm
    Murine Cd4 T Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck"

    Article Title: Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck

    Journal: Journal of Biomedical Science

    doi: 10.1186/s12929-024-01023-8

    TRAIL-R inhibits proximal TCR signaling and T cell activation. a Flow cytometry analyses of T cell activation markers — CD69 and CD25 (24 h), ( b ) carboxyfluorescein diacetate succinimidyl diester dilution assays (96 h), and ( c ) intracellular staining of IL-2 (24 h) on Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/ml) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL). Data in a–c represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. d Trail-r +/+ murine splenic CD4 + T cells were stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Total RNA was extracted and sequenced on the Illumina platform. Principal component analysis represented correlations among groups. Network analysis of biological process Gene Ontology term enrichment among significant genes in the indicated comparisons. Node color is proportional to p -adjusted enrichment value; node size proportional to number of genes in each Gene Ontology term. Heatmap showing two differentially expressed genes in TCR signaling pathway. Color bars indicate scores of log 2 -fold change for each comparison. e ELISAs of lysates from Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Data represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. f Immunoblotting of phosphorylation of TCR tyrosine kinases in Trail-r + / + or Trail-r −/− murine splenic CD4 + T cells at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. g Trail-r + / + or Trail-r −/− CD4 + T cells were stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in presence/absence of TRAIL (10 µg/mL) for 30 min, then lysed and fractionated as raft and non-raft layers; Lck, ZAP70, LAT, and PLCγ1 were immunoblotted from pooled raft or non-raft fractions. h Representative confocal images of Trail-r + / + murine splenic CD4 + T cells following staining with anti-GM-1 (red) and anti-Lck (green), or anti-ZAP70 (green) Abs, as indicated. Colocalization of GM-1 with Lck or ZAP70 is indicated by yellow areas. Scale bar: 4 µm
    Figure Legend Snippet: TRAIL-R inhibits proximal TCR signaling and T cell activation. a Flow cytometry analyses of T cell activation markers — CD69 and CD25 (24 h), ( b ) carboxyfluorescein diacetate succinimidyl diester dilution assays (96 h), and ( c ) intracellular staining of IL-2 (24 h) on Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/ml) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL). Data in a–c represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. d Trail-r +/+ murine splenic CD4 + T cells were stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Total RNA was extracted and sequenced on the Illumina platform. Principal component analysis represented correlations among groups. Network analysis of biological process Gene Ontology term enrichment among significant genes in the indicated comparisons. Node color is proportional to p -adjusted enrichment value; node size proportional to number of genes in each Gene Ontology term. Heatmap showing two differentially expressed genes in TCR signaling pathway. Color bars indicate scores of log 2 -fold change for each comparison. e ELISAs of lysates from Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Data represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. f Immunoblotting of phosphorylation of TCR tyrosine kinases in Trail-r + / + or Trail-r −/− murine splenic CD4 + T cells at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. g Trail-r + / + or Trail-r −/− CD4 + T cells were stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in presence/absence of TRAIL (10 µg/mL) for 30 min, then lysed and fractionated as raft and non-raft layers; Lck, ZAP70, LAT, and PLCγ1 were immunoblotted from pooled raft or non-raft fractions. h Representative confocal images of Trail-r + / + murine splenic CD4 + T cells following staining with anti-GM-1 (red) and anti-Lck (green), or anti-ZAP70 (green) Abs, as indicated. Colocalization of GM-1 with Lck or ZAP70 is indicated by yellow areas. Scale bar: 4 µm

    Techniques Used: Activation Assay, Flow Cytometry, Staining, MANN-WHITNEY, Comparison, Western Blot, Two Tailed Test

    TRAIL-R inhibits proximal TCR signaling without activation of apoptosis signaling. a Immunoblotting of caspase-8, caspase-3, and proximal TCR signaling molecules (30 min), and ( b ) Flow cytometry of Annexin V + apoptotic cells (24 h) from murine splenic CD4. + T cells (WT) or Jurkat cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs with or without TRAIL (10 µg/mL) in the presence or absence of pan-caspase inhibitor, Z-VAD-FMK (10 µg/mL). Data in ( b ) represent analyses from three independent experiments. Statistical significance was determined using the Mann–Whitney U test; NS, no significance; *** p < 0.001
    Figure Legend Snippet: TRAIL-R inhibits proximal TCR signaling without activation of apoptosis signaling. a Immunoblotting of caspase-8, caspase-3, and proximal TCR signaling molecules (30 min), and ( b ) Flow cytometry of Annexin V + apoptotic cells (24 h) from murine splenic CD4. + T cells (WT) or Jurkat cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs with or without TRAIL (10 µg/mL) in the presence or absence of pan-caspase inhibitor, Z-VAD-FMK (10 µg/mL). Data in ( b ) represent analyses from three independent experiments. Statistical significance was determined using the Mann–Whitney U test; NS, no significance; *** p < 0.001

    Techniques Used: Activation Assay, Western Blot, Flow Cytometry, MANN-WHITNEY

    SHP-1 is associated with TRAIL-R in T cells. a, b Immunoprecipitation analyses of tyrosine phosphatases SHP-1, SHP-2, Cbl, and Csk with TRAIL-R in murine splenic CD4 + T cells in the presence of TRAIL (10 µg/mL) at indicated time point. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; * p < 0.05; *** p < 0.001. c, d Co-immunoprecipitation of TRAIL-R with SHP-1 or SHP-2 from murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. e Immunoprecipitation analyses of TRAIL-R with SHP-1 or SHP-2 in TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min
    Figure Legend Snippet: SHP-1 is associated with TRAIL-R in T cells. a, b Immunoprecipitation analyses of tyrosine phosphatases SHP-1, SHP-2, Cbl, and Csk with TRAIL-R in murine splenic CD4 + T cells in the presence of TRAIL (10 µg/mL) at indicated time point. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; * p < 0.05; *** p < 0.001. c, d Co-immunoprecipitation of TRAIL-R with SHP-1 or SHP-2 from murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. e Immunoprecipitation analyses of TRAIL-R with SHP-1 or SHP-2 in TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min

    Techniques Used: Immunoprecipitation, Two Tailed Test

    TRAIL-R/SHP-1 inhibits proximal TCR signaling and T cell activation via dephosphorylation of Lck. a, b Immunoprecipitation with anti-TRAIL-R (a) or anti-Lck (b) Ab and then immunoblotting with p-SHP-1 and SHP-1 in murine splenic CD4 + T cells treated with TRAIL (10 µg/mL) at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. c Immunoprecipitation with anti-TRAIL-R Ab and then immunoblotting with p-Lck (Y394) and Lck in murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. d, e Immunoblotting of Lck in lysates ( d ) and pooled raft or non-raft fractions ( e ) of TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel
    Figure Legend Snippet: TRAIL-R/SHP-1 inhibits proximal TCR signaling and T cell activation via dephosphorylation of Lck. a, b Immunoprecipitation with anti-TRAIL-R (a) or anti-Lck (b) Ab and then immunoblotting with p-SHP-1 and SHP-1 in murine splenic CD4 + T cells treated with TRAIL (10 µg/mL) at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. c Immunoprecipitation with anti-TRAIL-R Ab and then immunoblotting with p-Lck (Y394) and Lck in murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. d, e Immunoblotting of Lck in lysates ( d ) and pooled raft or non-raft fractions ( e ) of TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel

    Techniques Used: Activation Assay, De-Phosphorylation Assay, Immunoprecipitation, Western Blot, Two Tailed Test

    SHP-1 knockdown abolished TRAIL-R-mediated inhibition on Lck phosphorylation, lipid raft recruitment and T cell activation. a Immunoblotting of phosphorylation of Lck and other proximal TCR signaling molecules (30 min), ( b ) immunoblotting of Lck and other proximal TCR signaling molecules in pooled raft fractions (30 min), ( c ) representative confocal images of co-localization of GM-1 with Lck (30 min), ( d ) flow cytometry of T cell activation markers CD69 and CD25 (24 h) (Scale bar, 4 µm), and ( e ) intracellular staining of IL-2 from murine splenic CD4. + T cells transfected with scramble or SHP-1 siRNA, followed by stimulation with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL) for 24 h. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data d–e represent analyses from three independent experiments and statistics determined using Mann–Whitney U test. NS, not significant; *** p < 0.001. f Model of TRAIL-R/SHP-1 repressing TCR signaling and T cell activation through dephosphorylation of Lck at Y394. Upon TCR ligation, Lck binds to, and phosphorylates TCR and Zap70 to form an immunological synapse in the lipid raft, which transduces proximal TCR signaling downstream, resulting in T cell activation (Left). TRAIL engagement reduces Lck (Y394) phosphorylation along with the increased phosphorylated SHP-1 in the TRAIL-R/SHP-1/Lck complex, leading to the dissociation of the co-receptor-Lck complex from the lipid raft, which in turn limits downstream TCR signaling to restrain T cell activation (Right)
    Figure Legend Snippet: SHP-1 knockdown abolished TRAIL-R-mediated inhibition on Lck phosphorylation, lipid raft recruitment and T cell activation. a Immunoblotting of phosphorylation of Lck and other proximal TCR signaling molecules (30 min), ( b ) immunoblotting of Lck and other proximal TCR signaling molecules in pooled raft fractions (30 min), ( c ) representative confocal images of co-localization of GM-1 with Lck (30 min), ( d ) flow cytometry of T cell activation markers CD69 and CD25 (24 h) (Scale bar, 4 µm), and ( e ) intracellular staining of IL-2 from murine splenic CD4. + T cells transfected with scramble or SHP-1 siRNA, followed by stimulation with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL) for 24 h. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data d–e represent analyses from three independent experiments and statistics determined using Mann–Whitney U test. NS, not significant; *** p < 0.001. f Model of TRAIL-R/SHP-1 repressing TCR signaling and T cell activation through dephosphorylation of Lck at Y394. Upon TCR ligation, Lck binds to, and phosphorylates TCR and Zap70 to form an immunological synapse in the lipid raft, which transduces proximal TCR signaling downstream, resulting in T cell activation (Left). TRAIL engagement reduces Lck (Y394) phosphorylation along with the increased phosphorylated SHP-1 in the TRAIL-R/SHP-1/Lck complex, leading to the dissociation of the co-receptor-Lck complex from the lipid raft, which in turn limits downstream TCR signaling to restrain T cell activation (Right)

    Techniques Used: Inhibition, Activation Assay, Western Blot, Flow Cytometry, Staining, Transfection, MANN-WHITNEY, De-Phosphorylation Assay, Ligation

    cd4 t cell line jurkat  (ATCC)


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    ATCC cd4 t cell line jurkat
    A . TIRF microscopy images of representative <t>CD4+</t> T cells (control or edited to knockout PRL-1, PRL-2 or WDR1 encoding genes) activated on ALBs. The UCHT-1, F-actin and WDR1 channels are displayed in pseudocolor. Pseudocolor bar is shown. The green WDR1 and red F-actin merged are shown. Scale bar corresponds to 5 μm. B . Graph indicates Pearson coefficients to assess the colocalisation between WDR1 and F-actin in each condition. C . Graph indicates the central hypodense F-actin cleared area of each analysed interaction. In B and C, dots represent individual cells analysed, the mean ± standard deviation of each sample from n=2 independent experiments are shown, and samples were compared by a one-way ANOVA with a Tukey’s multiple comparison test. **p<0.01 and ***p<0.001.
    Cd4 T Cell Line Jurkat, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Phosphatases of regenerating liver balance F-actin rearrangements during T cell activation through WD repeat containing protein 1"

    Article Title: Phosphatases of regenerating liver balance F-actin rearrangements during T cell activation through WD repeat containing protein 1

    Journal: bioRxiv

    doi: 10.1101/2023.12.28.573244

    A . TIRF microscopy images of representative CD4+ T cells (control or edited to knockout PRL-1, PRL-2 or WDR1 encoding genes) activated on ALBs. The UCHT-1, F-actin and WDR1 channels are displayed in pseudocolor. Pseudocolor bar is shown. The green WDR1 and red F-actin merged are shown. Scale bar corresponds to 5 μm. B . Graph indicates Pearson coefficients to assess the colocalisation between WDR1 and F-actin in each condition. C . Graph indicates the central hypodense F-actin cleared area of each analysed interaction. In B and C, dots represent individual cells analysed, the mean ± standard deviation of each sample from n=2 independent experiments are shown, and samples were compared by a one-way ANOVA with a Tukey’s multiple comparison test. **p<0.01 and ***p<0.001.
    Figure Legend Snippet: A . TIRF microscopy images of representative CD4+ T cells (control or edited to knockout PRL-1, PRL-2 or WDR1 encoding genes) activated on ALBs. The UCHT-1, F-actin and WDR1 channels are displayed in pseudocolor. Pseudocolor bar is shown. The green WDR1 and red F-actin merged are shown. Scale bar corresponds to 5 μm. B . Graph indicates Pearson coefficients to assess the colocalisation between WDR1 and F-actin in each condition. C . Graph indicates the central hypodense F-actin cleared area of each analysed interaction. In B and C, dots represent individual cells analysed, the mean ± standard deviation of each sample from n=2 independent experiments are shown, and samples were compared by a one-way ANOVA with a Tukey’s multiple comparison test. **p<0.01 and ***p<0.001.

    Techniques Used: Microscopy, Knock-Out, Standard Deviation, Comparison

    cd4 t cells  (ATCC)


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    ATCC cd4 t cells
    Cd4 T Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    influenza ha107 119 cd4 t cell epitope • lm gucy2c  (ATCC)


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    ATCC influenza ha107 119 cd4 t cell epitope • lm gucy2c
    Graphical abstract. (A) CRC epidemiology. Global impact of colorectal cancer. (B) Gene expression in CRC. suppressed expression in <t>GUCY2C</t> , GUCA2A , and GUCA2B in Cancerous vs. Normal Enterocytes. (C) GC-C role in CRC. Here, we also explored the molecular mechanism and role of this pathway in the pathogenesis of colon cancer. (D) Future prospects. Our study highlights the potential of the Guanylate cyclase-c (GC-C) signaling pathway as a diagnostic biomarker, prognostic indicator, and target for new therapeutic strategies in colorectal cancer. GUCY2C , Guanylate Cyclase 2C; GUCA2A , Guanylyl cyclase-activating protein 2A; GUCA2B , Guanylate Cyclase Activator 2B; GC-C, Guanylate Cyclase-C; CRC, Colorectal Cancer. Created with BioRender.com .
    Influenza Ha107 119 Cd4 T Cell Epitope • Lm Gucy2c, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Guanylate cyclase-C Signaling Axis as a theragnostic target in colorectal cancer: a systematic review of literature"

    Article Title: Guanylate cyclase-C Signaling Axis as a theragnostic target in colorectal cancer: a systematic review of literature

    Journal: Frontiers in Oncology

    doi: 10.3389/fonc.2023.1277265

    Graphical abstract. (A) CRC epidemiology. Global impact of colorectal cancer. (B) Gene expression in CRC. suppressed expression in GUCY2C , GUCA2A , and GUCA2B in Cancerous vs. Normal Enterocytes. (C) GC-C role in CRC. Here, we also explored the molecular mechanism and role of this pathway in the pathogenesis of colon cancer. (D) Future prospects. Our study highlights the potential of the Guanylate cyclase-c (GC-C) signaling pathway as a diagnostic biomarker, prognostic indicator, and target for new therapeutic strategies in colorectal cancer. GUCY2C , Guanylate Cyclase 2C; GUCA2A , Guanylyl cyclase-activating protein 2A; GUCA2B , Guanylate Cyclase Activator 2B; GC-C, Guanylate Cyclase-C; CRC, Colorectal Cancer. Created with BioRender.com .
    Figure Legend Snippet: Graphical abstract. (A) CRC epidemiology. Global impact of colorectal cancer. (B) Gene expression in CRC. suppressed expression in GUCY2C , GUCA2A , and GUCA2B in Cancerous vs. Normal Enterocytes. (C) GC-C role in CRC. Here, we also explored the molecular mechanism and role of this pathway in the pathogenesis of colon cancer. (D) Future prospects. Our study highlights the potential of the Guanylate cyclase-c (GC-C) signaling pathway as a diagnostic biomarker, prognostic indicator, and target for new therapeutic strategies in colorectal cancer. GUCY2C , Guanylate Cyclase 2C; GUCA2A , Guanylyl cyclase-activating protein 2A; GUCA2B , Guanylate Cyclase Activator 2B; GC-C, Guanylate Cyclase-C; CRC, Colorectal Cancer. Created with BioRender.com .

    Techniques Used: Expressing, Diagnostic Assay, Biomarker Assay

    Search strategy performed in PubMed.
    Figure Legend Snippet: Search strategy performed in PubMed.

    Techniques Used:

     GUCY2C-associated  studies included in the systematic review.
    Figure Legend Snippet: GUCY2C-associated studies included in the systematic review.

    Techniques Used: Amplification, Expressing, Quantitative RT-PCR, Radioactivity, Activity Assay, Modification, Purification, Labeling, In Vivo, Mouse Assay, In Vitro, Viability Assay, Release Assay, Fluorescence, Staining, Immunofluorescence, Enzyme-linked Immunospot, Luciferase, Cell Culture, Activation Assay, Histopathology, Immunohistochemistry, Western Blot, Isolation, Sequencing, Transduction, Variant Assay, Generated, Ex Vivo, Conjugation Assay, Flow Cytometry, Cytotoxicity Assay, Injection, Imaging, Mutagenesis, Knock-Out, Transformation Assay, Plasmid Preparation, Neutralization, Vaccines, Marker, Cell Isolation, Adoptive Transfer Assay, Transgenic Assay, Binding Assay, Cytotoxic T Lymphocyte Assay, Animal Model, Digital PCR, Positron Emission Tomography, Comparison, Stability Assay, Recombinant, RNA Sequencing Assay, Clone Assay, CRISPR, Chromatin Immunoprecipitation

    GUCY2A-associated studies included in the systematic review.
    Figure Legend Snippet: GUCY2A-associated studies included in the systematic review.

    Techniques Used: Isolation, Reverse Transcription Polymerase Chain Reaction, Western Blot, Expressing, Quantitative RT-PCR, Diagnostic Assay, Real-time Polymerase Chain Reaction, Selection, Biomarker Assay

    cd4 t cells  (ATCC)


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    ATCC cd4 t cells
    Cd4 T Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cd4 helper t cell subset phenotyping primary human cd4 helper t cells  (ATCC)


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    ATCC cd4 helper t cell subset phenotyping primary human cd4 helper t cells
    Cd4 Helper T Cell Subset Phenotyping Primary Human Cd4 Helper T Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC human cd4 t cells
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    ATCC cd4 t cells
    ( A ) QVOA measurements of inducible, replication-competent proviruses among resting <t>CD4</t> + T cells of PWH on ART for more than 7 years (mean 20.6 years). Virus was isolated in 54 of 61 assays from 42 participants. For negative assays (open symbols), a posterior median estimate is given . Black line, median value; n , number of assays. ( B ) Violin plots of the frequencies of latently infected cells in positive QVOAs on resting CD4 + T cells from 59 PWH on short-term ART (pink) and 38 PWH on long-term ART (orange). Mean duration of suppressive ART at sampling is on the x axis. Boxes and whiskers indicate middle quartiles and maximum and minimum values, respectively. Red horizontal lines, median; black circles, geometric mean. Expected decay with t 1/2 = 44.2 months over the relevant time interval is indicated (dashed line). Short-term ART data are from the 2003 study . Short- and long-term frequencies were not statistically different ( P = 0.54) by Student’s t test on log-transformed values. ( C ) Violin plots of the frequencies of intact proviruses as measured in positive IPDAs on samples from 62 PWH on short-term ART (pink) and 34 PWH on long-term ART (orange). Short-term ART data are from ref. using samples obtained between 0.5 and 7 years after ART initiation. Expected decay with t 1/2 = 44.2 months over the relevant time interval is indicated (dashed line). Log-transformed values were compared using Student’s t test. ( D ) IPDA measurements of the frequency of intact and defective proviruses (3′ deleted/hypermutated and 5′ deleted) in resting CD4 + T cells of PWH on suppressive ART for more than 7 years (mean = 22.0 years). Bars indicate median values. For negative assays (open symbols), maximum value based on the number of cells plated is shown. Significance values for multiple comparisons with the log-transformed frequencies of intact proviruses were determined using Dunnett’s test. n , number of assays.
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    1) Product Images from "The latent reservoir of inducible, infectious HIV-1 does not decrease despite decades of antiretroviral therapy"

    Article Title: The latent reservoir of inducible, infectious HIV-1 does not decrease despite decades of antiretroviral therapy

    Journal: The Journal of Clinical Investigation

    doi: 10.1172/JCI171554

    ( A ) QVOA measurements of inducible, replication-competent proviruses among resting CD4 + T cells of PWH on ART for more than 7 years (mean 20.6 years). Virus was isolated in 54 of 61 assays from 42 participants. For negative assays (open symbols), a posterior median estimate is given . Black line, median value; n , number of assays. ( B ) Violin plots of the frequencies of latently infected cells in positive QVOAs on resting CD4 + T cells from 59 PWH on short-term ART (pink) and 38 PWH on long-term ART (orange). Mean duration of suppressive ART at sampling is on the x axis. Boxes and whiskers indicate middle quartiles and maximum and minimum values, respectively. Red horizontal lines, median; black circles, geometric mean. Expected decay with t 1/2 = 44.2 months over the relevant time interval is indicated (dashed line). Short-term ART data are from the 2003 study . Short- and long-term frequencies were not statistically different ( P = 0.54) by Student’s t test on log-transformed values. ( C ) Violin plots of the frequencies of intact proviruses as measured in positive IPDAs on samples from 62 PWH on short-term ART (pink) and 34 PWH on long-term ART (orange). Short-term ART data are from ref. using samples obtained between 0.5 and 7 years after ART initiation. Expected decay with t 1/2 = 44.2 months over the relevant time interval is indicated (dashed line). Log-transformed values were compared using Student’s t test. ( D ) IPDA measurements of the frequency of intact and defective proviruses (3′ deleted/hypermutated and 5′ deleted) in resting CD4 + T cells of PWH on suppressive ART for more than 7 years (mean = 22.0 years). Bars indicate median values. For negative assays (open symbols), maximum value based on the number of cells plated is shown. Significance values for multiple comparisons with the log-transformed frequencies of intact proviruses were determined using Dunnett’s test. n , number of assays.
    Figure Legend Snippet: ( A ) QVOA measurements of inducible, replication-competent proviruses among resting CD4 + T cells of PWH on ART for more than 7 years (mean 20.6 years). Virus was isolated in 54 of 61 assays from 42 participants. For negative assays (open symbols), a posterior median estimate is given . Black line, median value; n , number of assays. ( B ) Violin plots of the frequencies of latently infected cells in positive QVOAs on resting CD4 + T cells from 59 PWH on short-term ART (pink) and 38 PWH on long-term ART (orange). Mean duration of suppressive ART at sampling is on the x axis. Boxes and whiskers indicate middle quartiles and maximum and minimum values, respectively. Red horizontal lines, median; black circles, geometric mean. Expected decay with t 1/2 = 44.2 months over the relevant time interval is indicated (dashed line). Short-term ART data are from the 2003 study . Short- and long-term frequencies were not statistically different ( P = 0.54) by Student’s t test on log-transformed values. ( C ) Violin plots of the frequencies of intact proviruses as measured in positive IPDAs on samples from 62 PWH on short-term ART (pink) and 34 PWH on long-term ART (orange). Short-term ART data are from ref. using samples obtained between 0.5 and 7 years after ART initiation. Expected decay with t 1/2 = 44.2 months over the relevant time interval is indicated (dashed line). Log-transformed values were compared using Student’s t test. ( D ) IPDA measurements of the frequency of intact and defective proviruses (3′ deleted/hypermutated and 5′ deleted) in resting CD4 + T cells of PWH on suppressive ART for more than 7 years (mean = 22.0 years). Bars indicate median values. For negative assays (open symbols), maximum value based on the number of cells plated is shown. Significance values for multiple comparisons with the log-transformed frequencies of intact proviruses were determined using Dunnett’s test. n , number of assays.

    Techniques Used: Virus, Isolation, Infection, Sampling, Transformation Assay

    ( A ) QVOA measurements of the frequencies of resting CD4 + T cells with inducible, replication-competent proviruses in 4 PWH from the original 2003 study who were sampled again after a total of 15–27 years on suppressive ART. Frequencies for the first 7 years of ART from other participants in Siliciano et al. are shown by red circles. For assays with no outgrowth, the median posterior estimate of infected-cell frequency based on input cell number was plotted (open symbols). Monophasic decay with t 1/2 = 44 months is indicated by the dashed red line. ( B ) QVOA measurements for all participants in the current study. Lines connect longitudinal measurements in the same donor. A best fit model for segmented exponential decay (thick gray line) shows initial decay with t 1/2 = 44 months followed by an inflection at 7 years and then a slow increase (doubling time = 23 years). See for details. ( C ) IPDA measurements of the decay of intact proviruses in PWH on very long-term ART. Frequencies for the initial years of ART (red circles) were replotted from Peluso et al. . Results are expressed as the DNA shearing index–corrected (DSI-corrected) geometric mean frequency of intact proviruses in resting CD4 + T cells . For assays in which no intact proviruses were detected, results are reported as the inverse of the number of cell equivalents analyzed (open symbols). The DSI was below 0.5 for all participants. Monophasic decay with a half-life of 44.2 months is indicated by the dashed line. A model for segmented exponential decay (thick gray line) shows initial decay with t 1/2 = 46 months followed by an inflection at 7 years and slower subsequent decay ( t 1/2 = 9 years). See for details.
    Figure Legend Snippet: ( A ) QVOA measurements of the frequencies of resting CD4 + T cells with inducible, replication-competent proviruses in 4 PWH from the original 2003 study who were sampled again after a total of 15–27 years on suppressive ART. Frequencies for the first 7 years of ART from other participants in Siliciano et al. are shown by red circles. For assays with no outgrowth, the median posterior estimate of infected-cell frequency based on input cell number was plotted (open symbols). Monophasic decay with t 1/2 = 44 months is indicated by the dashed red line. ( B ) QVOA measurements for all participants in the current study. Lines connect longitudinal measurements in the same donor. A best fit model for segmented exponential decay (thick gray line) shows initial decay with t 1/2 = 44 months followed by an inflection at 7 years and then a slow increase (doubling time = 23 years). See for details. ( C ) IPDA measurements of the decay of intact proviruses in PWH on very long-term ART. Frequencies for the initial years of ART (red circles) were replotted from Peluso et al. . Results are expressed as the DNA shearing index–corrected (DSI-corrected) geometric mean frequency of intact proviruses in resting CD4 + T cells . For assays in which no intact proviruses were detected, results are reported as the inverse of the number of cell equivalents analyzed (open symbols). The DSI was below 0.5 for all participants. Monophasic decay with a half-life of 44.2 months is indicated by the dashed line. A model for segmented exponential decay (thick gray line) shows initial decay with t 1/2 = 46 months followed by an inflection at 7 years and slower subsequent decay ( t 1/2 = 9 years). See for details.

    Techniques Used: Infection

    ( A ) QVOA/IPDA analysis of inducibility. Inducibility was measured as the ratio of the frequency of inducible, replication-competent proviruses per 10 6 resting CD4 + T cells over the frequency of intact proviruses per 10 6 resting CD4 + T cells in the same sample (QVOA/IPDA). Short-term ART data are from a study by Bruner et al. . The mean duration of treatment with suppressive ART at the time of sampling is shown for each group on the x axis. The geometric mean values (thick line) and statistical significance (Student’s t test on log-transformed values) are indicated. This analysis was performed using data from samples for which both assays were positive. ( B ) Data from A together with results from samples for which one of the frequencies was below the limit of detection (BLD). For these samples, frequencies were estimated as described in the legend to Figure 2.
    Figure Legend Snippet: ( A ) QVOA/IPDA analysis of inducibility. Inducibility was measured as the ratio of the frequency of inducible, replication-competent proviruses per 10 6 resting CD4 + T cells over the frequency of intact proviruses per 10 6 resting CD4 + T cells in the same sample (QVOA/IPDA). Short-term ART data are from a study by Bruner et al. . The mean duration of treatment with suppressive ART at the time of sampling is shown for each group on the x axis. The geometric mean values (thick line) and statistical significance (Student’s t test on log-transformed values) are indicated. This analysis was performed using data from samples for which both assays were positive. ( B ) Data from A together with results from samples for which one of the frequencies was below the limit of detection (BLD). For these samples, frequencies were estimated as described in the legend to Figure 2.

    Techniques Used: Sampling, Transformation Assay

    Maximum-likelihood phylogenetic trees of env sequences for 6 representative participants (R01, R03, R10, R16, R18, and R21), each rooted using HXB2, are shown. Single-genome sequencing of env was performed on cDNA reverse-transcribed from viral RNA extracted from supernatants of QVOA wells scored positive for viral outgrowth (red) or on proviral DNA from resting CD4 + T cells (rCD4, gray). Near-full-length genome sequences were obtained using the same proviral DNA and are annotated as intact (yellow) or defective (blue). Genetic distance is represented by the scale in nucleotides. A measure of the clonality of QVOA isolates (see article text) is indicated as a boxed value for each participant.
    Figure Legend Snippet: Maximum-likelihood phylogenetic trees of env sequences for 6 representative participants (R01, R03, R10, R16, R18, and R21), each rooted using HXB2, are shown. Single-genome sequencing of env was performed on cDNA reverse-transcribed from viral RNA extracted from supernatants of QVOA wells scored positive for viral outgrowth (red) or on proviral DNA from resting CD4 + T cells (rCD4, gray). Near-full-length genome sequences were obtained using the same proviral DNA and are annotated as intact (yellow) or defective (blue). Genetic distance is represented by the scale in nucleotides. A measure of the clonality of QVOA isolates (see article text) is indicated as a boxed value for each participant.

    Techniques Used: Sequencing

    ( A ) Clonality of QVOA isolates. Clonality was estimated as the fraction of env sequences that exactly matched another env sequence from an independent isolate obtained in the same QVOA. Clonality of outgrowth sequences for participants with over 10 positive QVOA outgrowth wells was compared between PWH on very long-term ART (R01, R02, R03, R10, R16, R18, and R21; orange symbols) and PWH on ART for an average of 9.0 years (red symbols) from 5 previous studies ( – , , ). In those 5 studies, clonality measurements included sequences obtained only from the first time point using the same QVOA methods with only 1 round of stimulation and from participants who experienced no analytical treatment interruptions and had no additional treatments besides ART. The mean values (thick line) and statistical significance (Student’s t test) are indicated. ( B ) Difference in clonality between QVOA isolates and proviral env sequences. Clonality of outgrowth sequences for very long-term ART participants with over 10 positive QVOA outgrowth wells (R01, R03, R10, R16, R18, and R21) was compared with the clonality of proviral sequences obtained from resting CD4 + T (rCD4) cells of the same participant. Statistical significance (Student’s paired t test) is indicated.
    Figure Legend Snippet: ( A ) Clonality of QVOA isolates. Clonality was estimated as the fraction of env sequences that exactly matched another env sequence from an independent isolate obtained in the same QVOA. Clonality of outgrowth sequences for participants with over 10 positive QVOA outgrowth wells was compared between PWH on very long-term ART (R01, R02, R03, R10, R16, R18, and R21; orange symbols) and PWH on ART for an average of 9.0 years (red symbols) from 5 previous studies ( – , , ). In those 5 studies, clonality measurements included sequences obtained only from the first time point using the same QVOA methods with only 1 round of stimulation and from participants who experienced no analytical treatment interruptions and had no additional treatments besides ART. The mean values (thick line) and statistical significance (Student’s t test) are indicated. ( B ) Difference in clonality between QVOA isolates and proviral env sequences. Clonality of outgrowth sequences for very long-term ART participants with over 10 positive QVOA outgrowth wells (R01, R03, R10, R16, R18, and R21) was compared with the clonality of proviral sequences obtained from resting CD4 + T (rCD4) cells of the same participant. Statistical significance (Student’s paired t test) is indicated.

    Techniques Used: Sequencing

    Levels of plasma HIV-1 RNA in copies/mL (orange squares) and CD4 + T cells in cells/μL (blue circles) are plotted as a function of time on suppressive ART. Plasma HIV-1 RNA values below the limit of detection are denoted by open orange squares and are plotted at the limit of detection of the assay used. The limits of detection of assays used at various times are shown by orange lines along the y axis. The ART regimens are given by the colored bars at the top of each plot. Times of sampling for reservoir assays are indicated (black arrows). Pre-ART plasma HIV-1 RNA levels for R31 were not available. The first available measurement was obtained while the participant was taking azidothymidine and lamivudine.
    Figure Legend Snippet: Levels of plasma HIV-1 RNA in copies/mL (orange squares) and CD4 + T cells in cells/μL (blue circles) are plotted as a function of time on suppressive ART. Plasma HIV-1 RNA values below the limit of detection are denoted by open orange squares and are plotted at the limit of detection of the assay used. The limits of detection of assays used at various times are shown by orange lines along the y axis. The ART regimens are given by the colored bars at the top of each plot. Times of sampling for reservoir assays are indicated (black arrows). Pre-ART plasma HIV-1 RNA levels for R31 were not available. The first available measurement was obtained while the participant was taking azidothymidine and lamivudine.

    Techniques Used: Sampling

    cd4 cxcr4 jurkat ce6 1 t cell line  (ATCC)


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    TRAIL-R inhibits proximal TCR signaling and T cell activation. a Flow cytometry analyses of T cell activation markers — CD69 and CD25 (24 h), ( b ) carboxyfluorescein diacetate succinimidyl diester dilution assays (96 h), and ( c ) intracellular staining of IL-2 (24 h) on Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/ml) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL). Data in a–c represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. d Trail-r +/+ murine splenic CD4 + T cells were stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Total RNA was extracted and sequenced on the Illumina platform. Principal component analysis represented correlations among groups. Network analysis of biological process Gene Ontology term enrichment among significant genes in the indicated comparisons. Node color is proportional to p -adjusted enrichment value; node size proportional to number of genes in each Gene Ontology term. Heatmap showing two differentially expressed genes in TCR signaling pathway. Color bars indicate scores of log 2 -fold change for each comparison. e ELISAs of lysates from Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Data represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. f Immunoblotting of phosphorylation of TCR tyrosine kinases in Trail-r + / + or Trail-r −/− murine splenic CD4 + T cells at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. g Trail-r + / + or Trail-r −/− CD4 + T cells were stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in presence/absence of TRAIL (10 µg/mL) for 30 min, then lysed and fractionated as raft and non-raft layers; Lck, ZAP70, LAT, and PLCγ1 were immunoblotted from pooled raft or non-raft fractions. h Representative confocal images of Trail-r + / + murine splenic CD4 + T cells following staining with anti-GM-1 (red) and anti-Lck (green), or anti-ZAP70 (green) Abs, as indicated. Colocalization of GM-1 with Lck or ZAP70 is indicated by yellow areas. Scale bar: 4 µm

    Journal: Journal of Biomedical Science

    Article Title: Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck

    doi: 10.1186/s12929-024-01023-8

    Figure Lengend Snippet: TRAIL-R inhibits proximal TCR signaling and T cell activation. a Flow cytometry analyses of T cell activation markers — CD69 and CD25 (24 h), ( b ) carboxyfluorescein diacetate succinimidyl diester dilution assays (96 h), and ( c ) intracellular staining of IL-2 (24 h) on Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/ml) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL). Data in a–c represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. d Trail-r +/+ murine splenic CD4 + T cells were stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Total RNA was extracted and sequenced on the Illumina platform. Principal component analysis represented correlations among groups. Network analysis of biological process Gene Ontology term enrichment among significant genes in the indicated comparisons. Node color is proportional to p -adjusted enrichment value; node size proportional to number of genes in each Gene Ontology term. Heatmap showing two differentially expressed genes in TCR signaling pathway. Color bars indicate scores of log 2 -fold change for each comparison. e ELISAs of lysates from Trail-r +/+ or Trail-r –/– murine splenic CD4 + T cells stimulated with CD3 (3 µg/mL) and CD28 (2 µg/ml) Abs in the presence/absence of TRAIL (10 µg/mL) for 24 h. Data represent analyses from three independent experiments; statistical significance determined by Mann–Whitney U test; NS, no significance; * p < 0.05; *** p < 0.001. f Immunoblotting of phosphorylation of TCR tyrosine kinases in Trail-r + / + or Trail-r −/− murine splenic CD4 + T cells at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. g Trail-r + / + or Trail-r −/− CD4 + T cells were stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in presence/absence of TRAIL (10 µg/mL) for 30 min, then lysed and fractionated as raft and non-raft layers; Lck, ZAP70, LAT, and PLCγ1 were immunoblotted from pooled raft or non-raft fractions. h Representative confocal images of Trail-r + / + murine splenic CD4 + T cells following staining with anti-GM-1 (red) and anti-Lck (green), or anti-ZAP70 (green) Abs, as indicated. Colocalization of GM-1 with Lck or ZAP70 is indicated by yellow areas. Scale bar: 4 µm

    Article Snippet: Murine CD4 + T cells and Jurkat T cells (American Type Cell Culture [ATCC]: TIB-152) were cultured in RPMI-1640 medium (Invitrogen, Carlsbad, CA), containing 10% fetal calf serum (Invitrogen), penicillin (10 units/mL; Invitrogen), and streptomycin (10 µg/mL; Invitrogen).

    Techniques: Activation Assay, Flow Cytometry, Staining, MANN-WHITNEY, Comparison, Western Blot, Two Tailed Test

    TRAIL-R inhibits proximal TCR signaling without activation of apoptosis signaling. a Immunoblotting of caspase-8, caspase-3, and proximal TCR signaling molecules (30 min), and ( b ) Flow cytometry of Annexin V + apoptotic cells (24 h) from murine splenic CD4. + T cells (WT) or Jurkat cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs with or without TRAIL (10 µg/mL) in the presence or absence of pan-caspase inhibitor, Z-VAD-FMK (10 µg/mL). Data in ( b ) represent analyses from three independent experiments. Statistical significance was determined using the Mann–Whitney U test; NS, no significance; *** p < 0.001

    Journal: Journal of Biomedical Science

    Article Title: Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck

    doi: 10.1186/s12929-024-01023-8

    Figure Lengend Snippet: TRAIL-R inhibits proximal TCR signaling without activation of apoptosis signaling. a Immunoblotting of caspase-8, caspase-3, and proximal TCR signaling molecules (30 min), and ( b ) Flow cytometry of Annexin V + apoptotic cells (24 h) from murine splenic CD4. + T cells (WT) or Jurkat cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs with or without TRAIL (10 µg/mL) in the presence or absence of pan-caspase inhibitor, Z-VAD-FMK (10 µg/mL). Data in ( b ) represent analyses from three independent experiments. Statistical significance was determined using the Mann–Whitney U test; NS, no significance; *** p < 0.001

    Article Snippet: Murine CD4 + T cells and Jurkat T cells (American Type Cell Culture [ATCC]: TIB-152) were cultured in RPMI-1640 medium (Invitrogen, Carlsbad, CA), containing 10% fetal calf serum (Invitrogen), penicillin (10 units/mL; Invitrogen), and streptomycin (10 µg/mL; Invitrogen).

    Techniques: Activation Assay, Western Blot, Flow Cytometry, MANN-WHITNEY

    SHP-1 is associated with TRAIL-R in T cells. a, b Immunoprecipitation analyses of tyrosine phosphatases SHP-1, SHP-2, Cbl, and Csk with TRAIL-R in murine splenic CD4 + T cells in the presence of TRAIL (10 µg/mL) at indicated time point. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; * p < 0.05; *** p < 0.001. c, d Co-immunoprecipitation of TRAIL-R with SHP-1 or SHP-2 from murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. e Immunoprecipitation analyses of TRAIL-R with SHP-1 or SHP-2 in TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min

    Journal: Journal of Biomedical Science

    Article Title: Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck

    doi: 10.1186/s12929-024-01023-8

    Figure Lengend Snippet: SHP-1 is associated with TRAIL-R in T cells. a, b Immunoprecipitation analyses of tyrosine phosphatases SHP-1, SHP-2, Cbl, and Csk with TRAIL-R in murine splenic CD4 + T cells in the presence of TRAIL (10 µg/mL) at indicated time point. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; * p < 0.05; *** p < 0.001. c, d Co-immunoprecipitation of TRAIL-R with SHP-1 or SHP-2 from murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. e Immunoprecipitation analyses of TRAIL-R with SHP-1 or SHP-2 in TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min

    Article Snippet: Murine CD4 + T cells and Jurkat T cells (American Type Cell Culture [ATCC]: TIB-152) were cultured in RPMI-1640 medium (Invitrogen, Carlsbad, CA), containing 10% fetal calf serum (Invitrogen), penicillin (10 units/mL; Invitrogen), and streptomycin (10 µg/mL; Invitrogen).

    Techniques: Immunoprecipitation, Two Tailed Test

    TRAIL-R/SHP-1 inhibits proximal TCR signaling and T cell activation via dephosphorylation of Lck. a, b Immunoprecipitation with anti-TRAIL-R (a) or anti-Lck (b) Ab and then immunoblotting with p-SHP-1 and SHP-1 in murine splenic CD4 + T cells treated with TRAIL (10 µg/mL) at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. c Immunoprecipitation with anti-TRAIL-R Ab and then immunoblotting with p-Lck (Y394) and Lck in murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. d, e Immunoblotting of Lck in lysates ( d ) and pooled raft or non-raft fractions ( e ) of TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel

    Journal: Journal of Biomedical Science

    Article Title: Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck

    doi: 10.1186/s12929-024-01023-8

    Figure Lengend Snippet: TRAIL-R/SHP-1 inhibits proximal TCR signaling and T cell activation via dephosphorylation of Lck. a, b Immunoprecipitation with anti-TRAIL-R (a) or anti-Lck (b) Ab and then immunoblotting with p-SHP-1 and SHP-1 in murine splenic CD4 + T cells treated with TRAIL (10 µg/mL) at indicated time points. Quantification of phosphorylated protein levels are shown at the bottom of the panel. c Immunoprecipitation with anti-TRAIL-R Ab and then immunoblotting with p-Lck (Y394) and Lck in murine splenic CD4 + T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data represent analyses from at least three independent experiments; statistical significance determined by two-tailed Student’s t test; NS, no significance; *** p < 0.001. d, e Immunoblotting of Lck in lysates ( d ) and pooled raft or non-raft fractions ( e ) of TRAIL-R WT -FLAG or TRAIL-R △DD -FLAG T cells stimulated with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence or absence of TRAIL (10 µg/mL) for 30 min. Quantification of phosphorylated protein levels are shown at the bottom of the panel

    Article Snippet: Murine CD4 + T cells and Jurkat T cells (American Type Cell Culture [ATCC]: TIB-152) were cultured in RPMI-1640 medium (Invitrogen, Carlsbad, CA), containing 10% fetal calf serum (Invitrogen), penicillin (10 units/mL; Invitrogen), and streptomycin (10 µg/mL; Invitrogen).

    Techniques: Activation Assay, De-Phosphorylation Assay, Immunoprecipitation, Western Blot, Two Tailed Test

    SHP-1 knockdown abolished TRAIL-R-mediated inhibition on Lck phosphorylation, lipid raft recruitment and T cell activation. a Immunoblotting of phosphorylation of Lck and other proximal TCR signaling molecules (30 min), ( b ) immunoblotting of Lck and other proximal TCR signaling molecules in pooled raft fractions (30 min), ( c ) representative confocal images of co-localization of GM-1 with Lck (30 min), ( d ) flow cytometry of T cell activation markers CD69 and CD25 (24 h) (Scale bar, 4 µm), and ( e ) intracellular staining of IL-2 from murine splenic CD4. + T cells transfected with scramble or SHP-1 siRNA, followed by stimulation with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL) for 24 h. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data d–e represent analyses from three independent experiments and statistics determined using Mann–Whitney U test. NS, not significant; *** p < 0.001. f Model of TRAIL-R/SHP-1 repressing TCR signaling and T cell activation through dephosphorylation of Lck at Y394. Upon TCR ligation, Lck binds to, and phosphorylates TCR and Zap70 to form an immunological synapse in the lipid raft, which transduces proximal TCR signaling downstream, resulting in T cell activation (Left). TRAIL engagement reduces Lck (Y394) phosphorylation along with the increased phosphorylated SHP-1 in the TRAIL-R/SHP-1/Lck complex, leading to the dissociation of the co-receptor-Lck complex from the lipid raft, which in turn limits downstream TCR signaling to restrain T cell activation (Right)

    Journal: Journal of Biomedical Science

    Article Title: Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck

    doi: 10.1186/s12929-024-01023-8

    Figure Lengend Snippet: SHP-1 knockdown abolished TRAIL-R-mediated inhibition on Lck phosphorylation, lipid raft recruitment and T cell activation. a Immunoblotting of phosphorylation of Lck and other proximal TCR signaling molecules (30 min), ( b ) immunoblotting of Lck and other proximal TCR signaling molecules in pooled raft fractions (30 min), ( c ) representative confocal images of co-localization of GM-1 with Lck (30 min), ( d ) flow cytometry of T cell activation markers CD69 and CD25 (24 h) (Scale bar, 4 µm), and ( e ) intracellular staining of IL-2 from murine splenic CD4. + T cells transfected with scramble or SHP-1 siRNA, followed by stimulation with anti-CD3 (3 µg/mL) and anti-CD28 (2 µg/mL) Abs in the presence/absence of TRAIL (0–1 µg/mL) for 24 h. Quantification of phosphorylated protein levels are shown at the bottom of the panel. Data d–e represent analyses from three independent experiments and statistics determined using Mann–Whitney U test. NS, not significant; *** p < 0.001. f Model of TRAIL-R/SHP-1 repressing TCR signaling and T cell activation through dephosphorylation of Lck at Y394. Upon TCR ligation, Lck binds to, and phosphorylates TCR and Zap70 to form an immunological synapse in the lipid raft, which transduces proximal TCR signaling downstream, resulting in T cell activation (Left). TRAIL engagement reduces Lck (Y394) phosphorylation along with the increased phosphorylated SHP-1 in the TRAIL-R/SHP-1/Lck complex, leading to the dissociation of the co-receptor-Lck complex from the lipid raft, which in turn limits downstream TCR signaling to restrain T cell activation (Right)

    Article Snippet: Murine CD4 + T cells and Jurkat T cells (American Type Cell Culture [ATCC]: TIB-152) were cultured in RPMI-1640 medium (Invitrogen, Carlsbad, CA), containing 10% fetal calf serum (Invitrogen), penicillin (10 units/mL; Invitrogen), and streptomycin (10 µg/mL; Invitrogen).

    Techniques: Inhibition, Activation Assay, Western Blot, Flow Cytometry, Staining, Transfection, MANN-WHITNEY, De-Phosphorylation Assay, Ligation

    A . TIRF microscopy images of representative CD4+ T cells (control or edited to knockout PRL-1, PRL-2 or WDR1 encoding genes) activated on ALBs. The UCHT-1, F-actin and WDR1 channels are displayed in pseudocolor. Pseudocolor bar is shown. The green WDR1 and red F-actin merged are shown. Scale bar corresponds to 5 μm. B . Graph indicates Pearson coefficients to assess the colocalisation between WDR1 and F-actin in each condition. C . Graph indicates the central hypodense F-actin cleared area of each analysed interaction. In B and C, dots represent individual cells analysed, the mean ± standard deviation of each sample from n=2 independent experiments are shown, and samples were compared by a one-way ANOVA with a Tukey’s multiple comparison test. **p<0.01 and ***p<0.001.

    Journal: bioRxiv

    Article Title: Phosphatases of regenerating liver balance F-actin rearrangements during T cell activation through WD repeat containing protein 1

    doi: 10.1101/2023.12.28.573244

    Figure Lengend Snippet: A . TIRF microscopy images of representative CD4+ T cells (control or edited to knockout PRL-1, PRL-2 or WDR1 encoding genes) activated on ALBs. The UCHT-1, F-actin and WDR1 channels are displayed in pseudocolor. Pseudocolor bar is shown. The green WDR1 and red F-actin merged are shown. Scale bar corresponds to 5 μm. B . Graph indicates Pearson coefficients to assess the colocalisation between WDR1 and F-actin in each condition. C . Graph indicates the central hypodense F-actin cleared area of each analysed interaction. In B and C, dots represent individual cells analysed, the mean ± standard deviation of each sample from n=2 independent experiments are shown, and samples were compared by a one-way ANOVA with a Tukey’s multiple comparison test. **p<0.01 and ***p<0.001.

    Article Snippet: CD4 T cell line Jurkat (JK, clone E6-1, code TIB-152 in atcc.org ) was cultured in RPMI 1640 with fetal bovine serum (FBS) (10 %), penicillin (100 U/ml), streptomycin (100 μg/ml), L-Glutamine (2 mM), sodium pyruvate (2 mM) and non-essential aminoacids (1x) (JK medium).

    Techniques: Microscopy, Knock-Out, Standard Deviation, Comparison

    Graphical abstract. (A) CRC epidemiology. Global impact of colorectal cancer. (B) Gene expression in CRC. suppressed expression in GUCY2C , GUCA2A , and GUCA2B in Cancerous vs. Normal Enterocytes. (C) GC-C role in CRC. Here, we also explored the molecular mechanism and role of this pathway in the pathogenesis of colon cancer. (D) Future prospects. Our study highlights the potential of the Guanylate cyclase-c (GC-C) signaling pathway as a diagnostic biomarker, prognostic indicator, and target for new therapeutic strategies in colorectal cancer. GUCY2C , Guanylate Cyclase 2C; GUCA2A , Guanylyl cyclase-activating protein 2A; GUCA2B , Guanylate Cyclase Activator 2B; GC-C, Guanylate Cyclase-C; CRC, Colorectal Cancer. Created with BioRender.com .

    Journal: Frontiers in Oncology

    Article Title: Guanylate cyclase-C Signaling Axis as a theragnostic target in colorectal cancer: a systematic review of literature

    doi: 10.3389/fonc.2023.1277265

    Figure Lengend Snippet: Graphical abstract. (A) CRC epidemiology. Global impact of colorectal cancer. (B) Gene expression in CRC. suppressed expression in GUCY2C , GUCA2A , and GUCA2B in Cancerous vs. Normal Enterocytes. (C) GC-C role in CRC. Here, we also explored the molecular mechanism and role of this pathway in the pathogenesis of colon cancer. (D) Future prospects. Our study highlights the potential of the Guanylate cyclase-c (GC-C) signaling pathway as a diagnostic biomarker, prognostic indicator, and target for new therapeutic strategies in colorectal cancer. GUCY2C , Guanylate Cyclase 2C; GUCA2A , Guanylyl cyclase-activating protein 2A; GUCA2B , Guanylate Cyclase Activator 2B; GC-C, Guanylate Cyclase-C; CRC, Colorectal Cancer. Created with BioRender.com .

    Article Snippet: • Vaccine: Investigating a prime-boost approach involving a chimeric adenoviral vector (Ad5.F35) engineered to overcome pre-existing immunity, followed by recombinant Lm to enhance immune response toward the gastrointestinal cancer antigen GUCY2C. , • Vaccines: Ad-GUCY2C • Adenovirus expressing mouse GUCY2C1-429 fused to the influenza HA107-119 CD4+ T-cell epitope • Lm-GUCY2C and Lm-LacZ • mouse macrophage cell line J774A.1 (ATCC) • BALB/cJ mice , • In vitro infections • Immunizations • Ad5-neutralizing immunity studies • IFNγ ELISpot assay • Intracellular cytokine staining • In vivo tumor studies • Safety studies • Blood chemistry and cytokine analyses • Western blot , • Immunization with both heterologous Ad-GUCY2C and Lm-GUCY2C enhances CD8+ T-cell responses specific to GUCY2C and boosts antitumor immune activity. • Previous exposure to Ad5 restricts the effectiveness of Ad5.F35+Lm immunization protocols, whereas prior Lm exposure does not impose such limitations. • Alterations in the qualitative characteristics of the CD8+ T-cell population after a prime-boost vaccination regimen. • Lm-GUCY2C could potentially be employed to enhance GUCY2C-specific immune responses in patients undergoing clinical trials with adenovirus-based GUCY2C vaccines, aiming to prevent or manage recurrent GI cancer. , ( ) .

    Techniques: Expressing, Diagnostic Assay, Biomarker Assay

    Search strategy performed in PubMed.

    Journal: Frontiers in Oncology

    Article Title: Guanylate cyclase-C Signaling Axis as a theragnostic target in colorectal cancer: a systematic review of literature

    doi: 10.3389/fonc.2023.1277265

    Figure Lengend Snippet: Search strategy performed in PubMed.

    Article Snippet: • Vaccine: Investigating a prime-boost approach involving a chimeric adenoviral vector (Ad5.F35) engineered to overcome pre-existing immunity, followed by recombinant Lm to enhance immune response toward the gastrointestinal cancer antigen GUCY2C. , • Vaccines: Ad-GUCY2C • Adenovirus expressing mouse GUCY2C1-429 fused to the influenza HA107-119 CD4+ T-cell epitope • Lm-GUCY2C and Lm-LacZ • mouse macrophage cell line J774A.1 (ATCC) • BALB/cJ mice , • In vitro infections • Immunizations • Ad5-neutralizing immunity studies • IFNγ ELISpot assay • Intracellular cytokine staining • In vivo tumor studies • Safety studies • Blood chemistry and cytokine analyses • Western blot , • Immunization with both heterologous Ad-GUCY2C and Lm-GUCY2C enhances CD8+ T-cell responses specific to GUCY2C and boosts antitumor immune activity. • Previous exposure to Ad5 restricts the effectiveness of Ad5.F35+Lm immunization protocols, whereas prior Lm exposure does not impose such limitations. • Alterations in the qualitative characteristics of the CD8+ T-cell population after a prime-boost vaccination regimen. • Lm-GUCY2C could potentially be employed to enhance GUCY2C-specific immune responses in patients undergoing clinical trials with adenovirus-based GUCY2C vaccines, aiming to prevent or manage recurrent GI cancer. , ( ) .

    Techniques:

     GUCY2C-associated  studies included in the systematic review.

    Journal: Frontiers in Oncology

    Article Title: Guanylate cyclase-C Signaling Axis as a theragnostic target in colorectal cancer: a systematic review of literature

    doi: 10.3389/fonc.2023.1277265

    Figure Lengend Snippet: GUCY2C-associated studies included in the systematic review.

    Article Snippet: • Vaccine: Investigating a prime-boost approach involving a chimeric adenoviral vector (Ad5.F35) engineered to overcome pre-existing immunity, followed by recombinant Lm to enhance immune response toward the gastrointestinal cancer antigen GUCY2C. , • Vaccines: Ad-GUCY2C • Adenovirus expressing mouse GUCY2C1-429 fused to the influenza HA107-119 CD4+ T-cell epitope • Lm-GUCY2C and Lm-LacZ • mouse macrophage cell line J774A.1 (ATCC) • BALB/cJ mice , • In vitro infections • Immunizations • Ad5-neutralizing immunity studies • IFNγ ELISpot assay • Intracellular cytokine staining • In vivo tumor studies • Safety studies • Blood chemistry and cytokine analyses • Western blot , • Immunization with both heterologous Ad-GUCY2C and Lm-GUCY2C enhances CD8+ T-cell responses specific to GUCY2C and boosts antitumor immune activity. • Previous exposure to Ad5 restricts the effectiveness of Ad5.F35+Lm immunization protocols, whereas prior Lm exposure does not impose such limitations. • Alterations in the qualitative characteristics of the CD8+ T-cell population after a prime-boost vaccination regimen. • Lm-GUCY2C could potentially be employed to enhance GUCY2C-specific immune responses in patients undergoing clinical trials with adenovirus-based GUCY2C vaccines, aiming to prevent or manage recurrent GI cancer. , ( ) .

    Techniques: Amplification, Expressing, Quantitative RT-PCR, Radioactivity, Activity Assay, Modification, Purification, Labeling, In Vivo, Mouse Assay, In Vitro, Viability Assay, Release Assay, Fluorescence, Staining, Immunofluorescence, Enzyme-linked Immunospot, Luciferase, Cell Culture, Activation Assay, Histopathology, Immunohistochemistry, Western Blot, Isolation, Sequencing, Transduction, Variant Assay, Generated, Ex Vivo, Conjugation Assay, Flow Cytometry, Cytotoxicity Assay, Injection, Imaging, Mutagenesis, Knock-Out, Transformation Assay, Plasmid Preparation, Neutralization, Vaccines, Marker, Cell Isolation, Adoptive Transfer Assay, Transgenic Assay, Binding Assay, Cytotoxic T Lymphocyte Assay, Animal Model, Digital PCR, Positron Emission Tomography, Comparison, Stability Assay, Recombinant, RNA Sequencing Assay, Clone Assay, CRISPR, Chromatin Immunoprecipitation

    GUCY2A-associated studies included in the systematic review.

    Journal: Frontiers in Oncology

    Article Title: Guanylate cyclase-C Signaling Axis as a theragnostic target in colorectal cancer: a systematic review of literature

    doi: 10.3389/fonc.2023.1277265

    Figure Lengend Snippet: GUCY2A-associated studies included in the systematic review.

    Article Snippet: • Vaccine: Investigating a prime-boost approach involving a chimeric adenoviral vector (Ad5.F35) engineered to overcome pre-existing immunity, followed by recombinant Lm to enhance immune response toward the gastrointestinal cancer antigen GUCY2C. , • Vaccines: Ad-GUCY2C • Adenovirus expressing mouse GUCY2C1-429 fused to the influenza HA107-119 CD4+ T-cell epitope • Lm-GUCY2C and Lm-LacZ • mouse macrophage cell line J774A.1 (ATCC) • BALB/cJ mice , • In vitro infections • Immunizations • Ad5-neutralizing immunity studies • IFNγ ELISpot assay • Intracellular cytokine staining • In vivo tumor studies • Safety studies • Blood chemistry and cytokine analyses • Western blot , • Immunization with both heterologous Ad-GUCY2C and Lm-GUCY2C enhances CD8+ T-cell responses specific to GUCY2C and boosts antitumor immune activity. • Previous exposure to Ad5 restricts the effectiveness of Ad5.F35+Lm immunization protocols, whereas prior Lm exposure does not impose such limitations. • Alterations in the qualitative characteristics of the CD8+ T-cell population after a prime-boost vaccination regimen. • Lm-GUCY2C could potentially be employed to enhance GUCY2C-specific immune responses in patients undergoing clinical trials with adenovirus-based GUCY2C vaccines, aiming to prevent or manage recurrent GI cancer. , ( ) .

    Techniques: Isolation, Reverse Transcription Polymerase Chain Reaction, Western Blot, Expressing, Quantitative RT-PCR, Diagnostic Assay, Real-time Polymerase Chain Reaction, Selection, Biomarker Assay