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molt 3  (ATCC)


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    ATCC molt 3
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    CEM Corporation molt 3
    Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and <t>MOLT-3</t> cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.
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    1) Product Images from "Schlafen14 Impairs HIV-1 Expression in a Codon Usage-Dependent Manner"

    Article Title: Schlafen14 Impairs HIV-1 Expression in a Codon Usage-Dependent Manner

    Journal: Viruses

    doi: 10.3390/v16040502

    Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and MOLT-3 cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.
    Figure Legend Snippet: Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and MOLT-3 cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.

    Techniques Used: Expressing, Western Blot, Transfection, Plasmid Preparation, Membrane, Derivative Assay, Agarose Gel Electrophoresis, Reverse Transcription Polymerase Chain Reaction, Positive Control, Molecular Weight, Marker, Mutagenesis, Activity Assay, Luciferase


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    Fluxion Biosciences 2 12 2 flow assays molt 3 t cell interactions
    2 12 2 Flow Assays Molt 3 T Cell Interactions, supplied by Fluxion Biosciences, 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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    molt 3 t cells  (R&D Systems)


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    CEM Corporation molt 3 cells
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    molt 3  (ATCC)


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    Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and <t>MOLT-3</t> cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.
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    Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and <t>MOLT-3</t> cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.
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    Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and <t>MOLT-3</t> cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.
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    Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and MOLT-3 cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.

    Journal: Viruses

    Article Title: Schlafen14 Impairs HIV-1 Expression in a Codon Usage-Dependent Manner

    doi: 10.3390/v16040502

    Figure Lengend Snippet: Expression of SLFN14 in immune cells. ( A ). Immunoblot analysis of SLFN14 expression in HEK293T co-transfected with an empty plasmid (Control) or a plasmid expressing human SLFN14, and in non-transfected SUP-T1, CEM, and MOLT-3 cells. The MOLT-3 cell lysate was in the same immunoblot membrane than the other samples but separated by irrelevant samples that were removed from the image presented. Anti-SLFN14 antibodies recognizing the N- or the C-terminus of the protein were used as indicated, and α-tubulin levels were determined as a loading control with a specific antibody. ( B ) Immunoblot analysis of SLFN14 expression in PBMCs ( I ), and PBMC-derived CD4+ T lymphocytes ( II ), and monocytes ( III ) with an anti-C-terminal SLFN14 antibody. α-tubulin was determined as a loading control. Cells were subjected to the stimuli indicated. Positive controls were HEK293T cells co-transfected with human SLFN14 (HEK393T/SLFN14) and SUP-T1 cells. ( C ) Analysis of SLFN14 mRNA in MOLT-3 cells. ( I ). Agarose gel electrophoresis analysis of the reverse transcription (RT)-PCR evaluating SLFN14 expression in MOLT-3 cells with primers SS1 and CV43. Samples were loaded in the gel in the following order: Lane 1 RT-PCR with RNA, Lane 2 No RT control (PCR with RNA), Lane 3 No template control (RT-PCR with no RNA), Lane 4 Positive control (RT-PCR with SLFN14 expression plasmid), and Lane 5 DNA Molecular Weight Marker (MWM). ( II ). Agarose gel electrophoresis analysis of the digestion with NsiI of the RT-PCR products obtained with primers SS1 and CV43 using as template RNA extracted from MOLT-3 cells (lane 2) or the SLFN14 expression plasmid (lane 3). DNA molecular weight markers (MWM) are in lanes 1 and 4. ( D ) Effect of D249A mutation on the activity of human (h) SLFN14 on transgene expression. HEK293T cells were co-transfected with a plasmid encoding an HIV-1 expressing firefly luciferase and either, an empty plasmid (control cells) or a plasmid expressing human SLFN14 WT or D249A mutant. HIV-1 p24 levels ( I ) and luciferase activity ( II ) were expressed as % of control cells. ( III ) SLFN14 expression was validated by immunoblotting as described in A(III). Statistically significant differences were calculated with two-way ANOVA and Dunnett post hoc tests. **** p ≤ 0.0001. Data correspond to a triplicate experiment and are representative of three independent experiments. Figure is created by Valenzuela et al.

    Article Snippet: In addition, SUP-T1 cells (lymphoblastic lymphoma-derived CD4+ T cell line), and the acute lymphoblastic leukemia-derived CD4+ T cell lines CEM and MOLT-3, were evaluated by immunoblot with these antibodies.

    Techniques: Expressing, Western Blot, Transfection, Plasmid Preparation, Membrane, Derivative Assay, Agarose Gel Electrophoresis, Reverse Transcription Polymerase Chain Reaction, Positive Control, Molecular Weight, Marker, Mutagenesis, Activity Assay, Luciferase