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ATCC
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ATCC
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ATCC
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DSMZ
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ATCC
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ATCC
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BioResource International Inc
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ATCC
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JCRB Cell Bank
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Image Search Results
Journal:
Article Title: The ? 1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors?
doi:
Figure Lengend Snippet: Detection of HLA-G transcripts in the K562 parental cell line, transfectants, and the JEG-3 cell line. Reversed RNAs were amplified using G.257 and G.1225 HLA-G-specific primers and Southern blot was hybridized with G.1200 or G.526 32P-labeled probe. Positive (+) and negative (−) lanes correspond to the RT+ and RT− templates, and the blank is a control performed using PCR mixture without the cDNA template, as described. To control the amount of RNA in all samples, RT-PCR amplification results obtained with β-actin-specific primers and Southern blots were hybridized with β-actin 32P-labeled probe.
Article Snippet: The
Techniques: Amplification, Southern Blot, Labeling, Control, Reverse Transcription Polymerase Chain Reaction
Journal:
Article Title: The ? 1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors?
doi:
Figure Lengend Snippet: Immunoprecipitation, SDS/PAGE, and Western blot analysis of biotin-labeled cell surface proteins. Biotinylated membrane lysates from K562 (lanes 1 and 2), K562-pRc/RSV (lanes 3 and 4), K562-HLA-G1 (lanes 5 and 6), K562-HLA-G2 (lanes 7 and 8), and JEG-3 (lanes 9 and 10) were immunoprecipitated with control mAb UPC-10 (lanes 1, 3, 5, 7, and 9) or with mAb W6/32 (lanes 2, 4, 6, 8, and 10) and analyzed by 10% SDS/PAGE under reducing conditions. Size markers in kDa are indicated at the right.
Article Snippet: The
Techniques: Immunoprecipitation, SDS Page, Western Blot, Labeling, Membrane, Control
Journal:
Article Title: The ? 1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors?
doi:
Figure Lengend Snippet: Expression of HLA molecules on the transfectants of the K562 cell line detected by cytofluorometry. Wild-type K562 cells (K562), K562 cells transfected with either the vector alone (K562 pRc/RSV), HLA-G1 (K562-HLA-G1) or with HLA-G2 (K562-HLA-G2), and JEG-3 cells were labeled by indirect immunofluorescence with the following primary mAbs (bold profiles): W6/32 (monomorphic anti-class I) (Left) and B1.G6 (anti-human β2m) (Right). Controls were the same cells stained with an isotype-matched control antibody (light profiles). After washing, cells were stained with phycoerythrin-conjugated F(ab′)2 goat anti-mouse IgG. One of four representative experiments is shown.
Article Snippet: The
Techniques: Expressing, Transfection, Plasmid Preparation, Labeling, Immunofluorescence, Staining, Control
Journal:
Article Title: The ? 1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors?
doi:
Figure Lengend Snippet: Effect of HLA-G1 and HLA-G2 expression on sensitivity to NK lysis of PBMC. K562 transfected with either the vector alone, with HLA-G1, or with HLA-G2 were used as targets. Freshly isolated PBMC from (A) donor 4010 (HLA-A3, -B44, -B56, and -Cw1), (B) donor 845 (HLA-A1, -A28, -B8, -B51, and -Cw7), and (C) donor 813 (HLA-A2, -B27, -B51, and -Cw1) were used as effectors. The results are expressed as the percentage lysis recorded in a 4-h 51Cr-release assay. The standard deviation of the mean of the triplicates was below 5%, and the spontaneous release never exceeded 10% of the maximum release.
Article Snippet: The
Techniques: Expressing, Lysis, Transfection, Plasmid Preparation, Isolation, Release Assay, Standard Deviation
Journal:
Article Title: The ? 1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors?
doi:
Figure Lengend Snippet: Effect of HLA-G1 and HLA-G2 expression on sensitivity to lysis of polyclonal NK cells. K562 transfected with either the vector alone, with HLA-G1, or with HLA-G2, were used as targets for NK cells (>90% CD3− CD16+ CD16+) isolated from donor 303 (HLA-A29, -B44, -B62, and -Cw3, -Cw5) at 1:1 effector/target (E/T) ratio, donor 395 (HLA-A2, -B13, -B44, and -Cw1) at 1:1 E/T ratio, and donor 481 (HLA-A3, -A26, -B27, -B35, and -Cw4, -Cw2) at 5:1 E/T ratio. The results are expressed as the percentage lysis recorded in a 4-h 51Cr-release assay. The standard deviation of the mean of the triplicates was below 5%, and the spontaneous release never exceeded 10% of the maximum release.
Article Snippet: The
Techniques: Expressing, Lysis, Transfection, Plasmid Preparation, Isolation, Release Assay, Standard Deviation
Journal:
Article Title: The ? 1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors?
doi:
Figure Lengend Snippet: Effect of HLA-G1 and HLA-G2 expression on sensitivity to cytotoxicity of the YT2C2 clone. K562 transfected with either the vector alone, HLA-G1, or HLA-G2 were used as targets. The results are expressed as the percentage lysis recorded in a 4-h 51Cr-release assay. The standard deviation of the mean of the triplicates was below 5%, and the spontaneous release never exceeded 10% of the maximum release. This experiment was repeated at least five times, giving the same pattern of protection. The expression of NKIRs on the YT2C2 clone was assessed by cytofluorometry. YT2C2 cells were labeled by indirect immunofluorescence with the following primary mAbs: EB6 (IgG1, anti-p58.1 or NKIR1), GL183 (IgG1, anti-p58.2 or NKIR2), and HP-3B1 (IgG2a, anti-CD94). Controls were the same cells stained with an isotype-matched control antibody. After washing, cells were stained with phycoerythrin-conjugated F(ab′)2 goat anti-mouse IgG. One of four representative experiments is shown.
Article Snippet: The
Techniques: Expressing, Transfection, Plasmid Preparation, Lysis, Release Assay, Standard Deviation, Labeling, Immunofluorescence, Staining, Control
Journal: International Journal of Peptides
Article Title: Diverse Effects of Glutathione and UPF Peptides on Antioxidant Defense System in Human Erythroleukemia Cells K562
doi: 10.1155/2012/124163
Figure Lengend Snippet: Modulation of CuZnSOD activity by GSH and UPF1 in K562 cells. The CuZnSOD activity of Co is 100%. * P < 0.05; ** P < 0.01, GSH and UPF1 versus Co; n = 4–8.
Article Snippet: The
Techniques: Activity Assay
Journal: International Journal of Peptides
Article Title: Diverse Effects of Glutathione and UPF Peptides on Antioxidant Defense System in Human Erythroleukemia Cells K562
doi: 10.1155/2012/124163
Figure Lengend Snippet: Modulation of CuZnSOD activity by GSH and α -GSH (10 μ M) in K562 cells. The CuZnSOD activity of Co is 100%. * P < 0.05; ** P < 0.01, 10 μ M GSH or α -GSH versus Co; n = 4–8.
Article Snippet: The
Techniques: Activity Assay
Journal: International Journal of Peptides
Article Title: Diverse Effects of Glutathione and UPF Peptides on Antioxidant Defense System in Human Erythroleukemia Cells K562
doi: 10.1155/2012/124163
Figure Lengend Snippet: Modulation of CuZnSOD activity by UPF1 and UPF17 (10 μ M) in K562 cells. The CuZnSOD activity of Co is 100%. * P < 0.05; ** P < 0.01, 10 μ M UPF1 or UPF17 versus Co; n = 4–8.
Article Snippet: The
Techniques: Activity Assay
Journal: International Journal of Peptides
Article Title: Diverse Effects of Glutathione and UPF Peptides on Antioxidant Defense System in Human Erythroleukemia Cells K562
doi: 10.1155/2012/124163
Figure Lengend Snippet: Alteration of tGSH concentration by UPF1 and UPF17 in K562 cells. The tGSH concentration of Co is 100%. * P < 0.05, *** P < 0.005, UPF1 or UPF17 versus Co; n = 6–8.
Article Snippet: The
Techniques: Concentration Assay
Journal: Archives of Medical Science : AMS
Article Title: Anticancer and anti-inflammatory activities of shallot ( Allium ascalonicum ) extract
doi: 10.5114/aoms.2011.20602
Figure Lengend Snippet: The cytotoxic effects of different concentrations of the aqueous extract of A. ascalonicum on K562, Jurkat and Wehi164, and HUVEC cell lines. The viability percentage of cell lines was assayed using Trypan blue 4% exclusion and LDH assays. Each data shown are one representative example of three independent experiments, expressed as a percentage of control and standard deviations were within 5% of all experimental values
Article Snippet: The cancer cell lines including Wehi164 (mouse fibrosarcoma cells), Jurkat (human–acute T-cell leukemia) and
Techniques: Control
Journal: Archives of Medical Science : AMS
Article Title: Anticancer and anti-inflammatory activities of shallot ( Allium ascalonicum ) extract
doi: 10.5114/aoms.2011.20602
Figure Lengend Snippet: IC50 and GI50 value data of the aqueous extract of A. ascalonicum, for K562, Jurkat and Wehi164, and HUVEC after 72 h of treatment
Article Snippet: The cancer cell lines including Wehi164 (mouse fibrosarcoma cells), Jurkat (human–acute T-cell leukemia) and
Techniques: