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  • 99
    ATCC thp 1 cells
    TRAM and SLAMF1 are essential for the killing of E. coli by human macrophages. (A) Flow cytometry analysis of dihydrorhodamine 123 (DHR-123) fluorescence to access ROS activation in control siRNA or SLAMF1 siRNA human macrophages upon stimulation by E. coli red pHrodo particles. One of three experiments shown. (B and C) Bacterial killing assays by SLAMF1-silenced and control <t>THP-1</t> cells (B) as well as TRAM KO and control THP-1 cells (C) infected with a DH5α strain at MOI 40. (D and E) Western blot analysis of pAkt (S473) and pIRF3 (S396) levels induced by E. coli particles in THP-1 WT and TRAM KO cells (D) as well as SLAMF1-silenced or control oligonucleotide–treated cells (E). Graphs (right) on Western blotting show quantification of protein levels relative to β-tubulin obtained with Odyssey software. (F) Western blot showing phospho-(S396) IRF3 and phospho-(S473) Akt levels in lysates of THP-1 cells coincubated with E. coli particles for 1 h in the presence or absence of TBK1-IKKε inhibitor (MRT67307), pan-Akt allosteric inhibitor (MK2206), or DMSO. Molecular weight is given in kilodaltons. (G) Bacterial killing assays by THP-1 cells with DMSO (
    Thp 1 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 5906 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore genejuice transfection reagent
    TRAM and SLAMF1 are essential for the killing of E. coli by human macrophages. (A) Flow cytometry analysis of dihydrorhodamine 123 (DHR-123) fluorescence to access ROS activation in control siRNA or SLAMF1 siRNA human macrophages upon stimulation by E. coli red pHrodo particles. One of three experiments shown. (B and C) Bacterial killing assays by SLAMF1-silenced and control <t>THP-1</t> cells (B) as well as TRAM KO and control THP-1 cells (C) infected with a DH5α strain at MOI 40. (D and E) Western blot analysis of pAkt (S473) and pIRF3 (S396) levels induced by E. coli particles in THP-1 WT and TRAM KO cells (D) as well as SLAMF1-silenced or control oligonucleotide–treated cells (E). Graphs (right) on Western blotting show quantification of protein levels relative to β-tubulin obtained with Odyssey software. (F) Western blot showing phospho-(S396) IRF3 and phospho-(S473) Akt levels in lysates of THP-1 cells coincubated with E. coli particles for 1 h in the presence or absence of TBK1-IKKε inhibitor (MRT67307), pan-Akt allosteric inhibitor (MK2206), or DMSO. Molecular weight is given in kilodaltons. (G) Bacterial killing assays by THP-1 cells with DMSO (
    Genejuice Transfection Reagent, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2481 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa plvx ires zsgreen1
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Plvx Ires Zsgreen1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 327 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa lenti x 293t cells
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Lenti X 293t Cells, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1770 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa ecori
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
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    TaKaRa 293t cells
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
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    TaKaRa in fusion hd cloning kit
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    In Fusion Hd Cloning Kit, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 15962 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa bicistronic lentiviral expression vector plvx ef1α ires zsgreen1
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Bicistronic Lentiviral Expression Vector Plvx Ef1α Ires Zsgreen1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 95/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    TaKaRa lentiviral vector
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Lentiviral Vector, supplied by TaKaRa, used in various techniques. Bioz Stars score: 94/100, based on 571 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa lentiviral expression vector
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Lentiviral Expression Vector, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 217 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa plvx puro
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Plvx Puro, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 504 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Addgene inc packaging plasmids
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Packaging Plasmids, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1524 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa lenti x packaging system
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
    Lenti X Packaging System, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa lenti x htx packaging systems
    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with <t>pLVX-ORF2-IRES-zsGreen</t> and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P
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    Image Search Results


    TRAM and SLAMF1 are essential for the killing of E. coli by human macrophages. (A) Flow cytometry analysis of dihydrorhodamine 123 (DHR-123) fluorescence to access ROS activation in control siRNA or SLAMF1 siRNA human macrophages upon stimulation by E. coli red pHrodo particles. One of three experiments shown. (B and C) Bacterial killing assays by SLAMF1-silenced and control THP-1 cells (B) as well as TRAM KO and control THP-1 cells (C) infected with a DH5α strain at MOI 40. (D and E) Western blot analysis of pAkt (S473) and pIRF3 (S396) levels induced by E. coli particles in THP-1 WT and TRAM KO cells (D) as well as SLAMF1-silenced or control oligonucleotide–treated cells (E). Graphs (right) on Western blotting show quantification of protein levels relative to β-tubulin obtained with Odyssey software. (F) Western blot showing phospho-(S396) IRF3 and phospho-(S473) Akt levels in lysates of THP-1 cells coincubated with E. coli particles for 1 h in the presence or absence of TBK1-IKKε inhibitor (MRT67307), pan-Akt allosteric inhibitor (MK2206), or DMSO. Molecular weight is given in kilodaltons. (G) Bacterial killing assays by THP-1 cells with DMSO (

    Journal: The Journal of Cell Biology

    Article Title: SLAMF1 is required for TLR4-mediated TRAM-TRIF–dependent signaling in human macrophages

    doi: 10.1083/jcb.201707027

    Figure Lengend Snippet: TRAM and SLAMF1 are essential for the killing of E. coli by human macrophages. (A) Flow cytometry analysis of dihydrorhodamine 123 (DHR-123) fluorescence to access ROS activation in control siRNA or SLAMF1 siRNA human macrophages upon stimulation by E. coli red pHrodo particles. One of three experiments shown. (B and C) Bacterial killing assays by SLAMF1-silenced and control THP-1 cells (B) as well as TRAM KO and control THP-1 cells (C) infected with a DH5α strain at MOI 40. (D and E) Western blot analysis of pAkt (S473) and pIRF3 (S396) levels induced by E. coli particles in THP-1 WT and TRAM KO cells (D) as well as SLAMF1-silenced or control oligonucleotide–treated cells (E). Graphs (right) on Western blotting show quantification of protein levels relative to β-tubulin obtained with Odyssey software. (F) Western blot showing phospho-(S396) IRF3 and phospho-(S473) Akt levels in lysates of THP-1 cells coincubated with E. coli particles for 1 h in the presence or absence of TBK1-IKKε inhibitor (MRT67307), pan-Akt allosteric inhibitor (MK2206), or DMSO. Molecular weight is given in kilodaltons. (G) Bacterial killing assays by THP-1 cells with DMSO (

    Article Snippet: Transduced THP-1 cells were selected with puromycin (1 μg/ml) for 1 mo and then tested for TRAM protein expression by Western blotting.

    Techniques: Flow Cytometry, Cytometry, Fluorescence, Activation Assay, Infection, Western Blot, Software, Molecular Weight

    Knockdown of SLAMF1 in macrophages results in strongly reduced TLR4-mediated IFNβ mRNA expression and protein secretion as well as some decrease of TNF, IL-6, and CXCL10 secretion. (A and B) Quantification of SLAMF1 , IFNβ , and TNF mRNA expression by qPCR in THP-1 cells (A) and macrophages (B) treated by 100 ng/ml ultrapure K12 LPS. (C and D) IFNβ and TNF secretion levels by THP-1 cells (C) and macrophages (D) in response to LPS (4 and 6 h) assessed by ELISA. (E and F) Secretion levels of IL-1β, IL-6, IL-8, and CXCL-10 (6 h LPS) analyzed by multiplex assays. Data are presented as means with SD for combined data from three independent experiments (A, C, and E), for three biological replicates from one of six donors (B and D), or one of three donors (F). *, P

    Journal: The Journal of Cell Biology

    Article Title: SLAMF1 is required for TLR4-mediated TRAM-TRIF–dependent signaling in human macrophages

    doi: 10.1083/jcb.201707027

    Figure Lengend Snippet: Knockdown of SLAMF1 in macrophages results in strongly reduced TLR4-mediated IFNβ mRNA expression and protein secretion as well as some decrease of TNF, IL-6, and CXCL10 secretion. (A and B) Quantification of SLAMF1 , IFNβ , and TNF mRNA expression by qPCR in THP-1 cells (A) and macrophages (B) treated by 100 ng/ml ultrapure K12 LPS. (C and D) IFNβ and TNF secretion levels by THP-1 cells (C) and macrophages (D) in response to LPS (4 and 6 h) assessed by ELISA. (E and F) Secretion levels of IL-1β, IL-6, IL-8, and CXCL-10 (6 h LPS) analyzed by multiplex assays. Data are presented as means with SD for combined data from three independent experiments (A, C, and E), for three biological replicates from one of six donors (B and D), or one of three donors (F). *, P

    Article Snippet: Transduced THP-1 cells were selected with puromycin (1 μg/ml) for 1 mo and then tested for TRAM protein expression by Western blotting.

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Multiplex Assay

    SLAMF1 is enriched in the Rab11-positive ERCs in unstimulated macrophages, and SLAMF1 expression is induced by LPS and several other TLR ligands in primary human monocytes and macrophages. (A) Monocytes, macrophages, and differentiated THP-1 cells stained with antibodies against SLAMF1 (green) and GM130 (red) and imaged by confocal microscopy. (B) 3D model of cis-Golgi (GM130) and SLAMF1 in THP-1 cells. Z stacks from the GM130 and SLAMF1 channels were obtained using high-resolution confocal microscopy followed by 3D modeling in IMARIS software. (C) Macrophages stained for SLAMF1 and Rab11 (ERC marker). Representative image. Overlapping pixels for SLAMF1 and Rab11 are shown in the white overlap. tM1 = 0.683 ± 0.08 (mean with SD) for z stacks of ERCs as ROIs (30 ROIs analyzed per donor) where tM1 was the Manders’s colocalization coefficient with thresholds calculated in the Coloc 2 Fiji plugin with anti-SLAMF1 staining as first channel. (D) Macrophages costained for SLAMF1 and EEA1. (E) Macrophages costained for SLAMF1 and LAMP1. Colocalization accessed for z stacks for at least 30 cells for each experiment (four total) showing no colocalization for markers in both D and E. (F) Flow cytometry analysis of SLAMF1 surface expression by primary macrophages and differentiated THP-1 cells. Cells were costained for SLAMF1 and CD14 and gated for CD14-positive cells (primary cells) or stained for SLAMF1 (THP-1 cells). (G) Flow cytometry analysis of SLAMF1 surface expression by human macrophages stimulated by ultrapure K12 LPS (100 ng/ml) for 2, 4, and 6 h. (H) Western blot analysis of lysates from primary human macrophages stimulated by LPS for 2, 4, and 6 h. Graphs present mean values for three biological replicates with SD. Molecular weight is given in kilodaltons. (I and J ) Quantification of SLAMF1 mRNA expression by qPCR in monocytes (I) and macrophages (J) stimulated by TLRs’ ligands FSL-1 (20 ng/ml), K12 LPS (100 ng/ml), and CL075 (1 μg/ml; both I and J) as well as R848 (1 μg/ml), Pam3Cys (P3C; 1 μg/ml), or K12 E. coli particles (20/cell; I only). Results are presented as means with SD. Statistical significance between groups was evaluated by a two-tailed t test. *, P

    Journal: The Journal of Cell Biology

    Article Title: SLAMF1 is required for TLR4-mediated TRAM-TRIF–dependent signaling in human macrophages

    doi: 10.1083/jcb.201707027

    Figure Lengend Snippet: SLAMF1 is enriched in the Rab11-positive ERCs in unstimulated macrophages, and SLAMF1 expression is induced by LPS and several other TLR ligands in primary human monocytes and macrophages. (A) Monocytes, macrophages, and differentiated THP-1 cells stained with antibodies against SLAMF1 (green) and GM130 (red) and imaged by confocal microscopy. (B) 3D model of cis-Golgi (GM130) and SLAMF1 in THP-1 cells. Z stacks from the GM130 and SLAMF1 channels were obtained using high-resolution confocal microscopy followed by 3D modeling in IMARIS software. (C) Macrophages stained for SLAMF1 and Rab11 (ERC marker). Representative image. Overlapping pixels for SLAMF1 and Rab11 are shown in the white overlap. tM1 = 0.683 ± 0.08 (mean with SD) for z stacks of ERCs as ROIs (30 ROIs analyzed per donor) where tM1 was the Manders’s colocalization coefficient with thresholds calculated in the Coloc 2 Fiji plugin with anti-SLAMF1 staining as first channel. (D) Macrophages costained for SLAMF1 and EEA1. (E) Macrophages costained for SLAMF1 and LAMP1. Colocalization accessed for z stacks for at least 30 cells for each experiment (four total) showing no colocalization for markers in both D and E. (F) Flow cytometry analysis of SLAMF1 surface expression by primary macrophages and differentiated THP-1 cells. Cells were costained for SLAMF1 and CD14 and gated for CD14-positive cells (primary cells) or stained for SLAMF1 (THP-1 cells). (G) Flow cytometry analysis of SLAMF1 surface expression by human macrophages stimulated by ultrapure K12 LPS (100 ng/ml) for 2, 4, and 6 h. (H) Western blot analysis of lysates from primary human macrophages stimulated by LPS for 2, 4, and 6 h. Graphs present mean values for three biological replicates with SD. Molecular weight is given in kilodaltons. (I and J ) Quantification of SLAMF1 mRNA expression by qPCR in monocytes (I) and macrophages (J) stimulated by TLRs’ ligands FSL-1 (20 ng/ml), K12 LPS (100 ng/ml), and CL075 (1 μg/ml; both I and J) as well as R848 (1 μg/ml), Pam3Cys (P3C; 1 μg/ml), or K12 E. coli particles (20/cell; I only). Results are presented as means with SD. Statistical significance between groups was evaluated by a two-tailed t test. *, P

    Article Snippet: Transduced THP-1 cells were selected with puromycin (1 μg/ml) for 1 mo and then tested for TRAM protein expression by Western blotting.

    Techniques: Expressing, Staining, Confocal Microscopy, Software, Marker, Flow Cytometry, Cytometry, Western Blot, Molecular Weight, Real-time Polymerase Chain Reaction, Two Tailed Test

    ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with pLVX-ORF2-IRES-zsGreen and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Hepatitis E virus ORF3 is a functional ion channel required for release of infectious particles

    doi: 10.1073/pnas.1614955114

    Figure Lengend Snippet: ORF2 and ORF3 are required for releasing viral particles to infect naïve HepG2C3A cells. ( A ) Schematic representation of the transcomplementation system for packaging HEV virions. ( B ) Representative flow cytometry plots demonstrating efficient ORF2 and ORF3 expression. HepG2C3A cells were transduced with pLVX-ORF2-IRES-zsGreen and/or pLEX-ORF3-IRES-mCherry or not transduced. Flow cytometric analysis was performed 4 d following transduction to quantify the frequencies of ORF2 and/or ORF3 expressing cells. ( C ) Infection kinetics of transcomplemented HEV in HepG2C3A cells. Cell culture supernatants from naïve HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, were collected 5 d posttransfection with rHEVΔORF2/3[Gluc] RNA. Naïve HepG2C3A cells were incubated with these supernatants. After 12 h, cells were washed and Gaussia luciferase activity quantified in the cell culture supernatants at the indicated time points. ( D ) Five days following transfection of rHEVΔORF2/3[Gluc] RNA into HepG2C3A, or HepG2C3A cells transduced with HEV ORF2 or/and ORF3, lysates were used to infect naïve HepG2C3A cells. Gluc activity was measured in the supernatants 4 d postinfection. Shown are averages and SDs of triplicate measurements of three independent experiments. * P

    Article Snippet: To construct a lentiviral construct that encodes Kernow C1/p6 ORF2 or Kernow C1/p6 ORF3, the Kernow C1/p6 ORF2 or Kernow C1/p6 ORF3 cDNA was amplified by PCR from the HEV Kernow C1/p6 construct (a kind gift from Suzanne Emerson, NIH, Bethesda, MD) and then cloned into pLVX-IRES-zsGreen1 or pLEX-IRES-mCherry vectors using the In-Fusion HD Cloning Kit (Clontech).

    Techniques: Flow Cytometry, Cytometry, Expressing, Transduction, Infection, Cell Culture, Incubation, Luciferase, Activity Assay, Transfection

    HEV ORF1 is able to function in trans to replicate HEV RNA. (a) Schematic representation of the ORF1 transcomplementation system. (b) Representative flow cytometry plots demonstrating efficient ORF1 expression. HepG2C3A cells were transduced with pLVX-ORF1-IRES-zsGreen (wild type [wt] or GAD mutant) or not transduced. Flow cytometric analysis was performed 3 days following transduction to quantify the frequencies of ORF1-expressing cells. FSC, forward scatter. (c) Replication kinetics of HEV RNA in ORF1 transcomplemented HepG2C3A cells. Cell culture supernatants from naive HepG2C3A cells, or HepG2C3A cells transduced with HEV ORF1 or its GAD mutant, were collected at the indicated time points posttransfection with rHEVΔORF2/3[Gluc] Pol- RNA or RNA from its mutants, and Gaussia luciferase (Gluc) activity was quantified. Values are means plus standard deviations (SD) (error bars) ( n = 3). Values that are significantly different ( P

    Journal: mBio

    Article Title: Identification of the Intragenomic Promoter Controlling Hepatitis E Virus Subgenomic RNA Transcription

    doi: 10.1128/mBio.00769-18

    Figure Lengend Snippet: HEV ORF1 is able to function in trans to replicate HEV RNA. (a) Schematic representation of the ORF1 transcomplementation system. (b) Representative flow cytometry plots demonstrating efficient ORF1 expression. HepG2C3A cells were transduced with pLVX-ORF1-IRES-zsGreen (wild type [wt] or GAD mutant) or not transduced. Flow cytometric analysis was performed 3 days following transduction to quantify the frequencies of ORF1-expressing cells. FSC, forward scatter. (c) Replication kinetics of HEV RNA in ORF1 transcomplemented HepG2C3A cells. Cell culture supernatants from naive HepG2C3A cells, or HepG2C3A cells transduced with HEV ORF1 or its GAD mutant, were collected at the indicated time points posttransfection with rHEVΔORF2/3[Gluc] Pol- RNA or RNA from its mutants, and Gaussia luciferase (Gluc) activity was quantified. Values are means plus standard deviations (SD) (error bars) ( n = 3). Values that are significantly different ( P

    Article Snippet: To construct lentiviral constructs encoding ORF1 of Kernow C1/p6 (GenBank accession number JQ679013 ), the Kernow C1/p6 ORF1 cDNA was amplified by PCR from a plasmid encoding the full-length (FL) infectious HEV clone Kernow C1/p6 (a kind gift from Suzanne Emerson, NIH) and then cloned into pLVX-IRES-zsGreen1 vector using an In-Fusion HD cloning kit (Clontech, Mountain View, CA, USA).

    Techniques: Flow Cytometry, Cytometry, Expressing, Transduction, Mutagenesis, Cell Culture, Luciferase, Activity Assay

    The anti-leukemia effects of miR-375 in vivo. About 1х10 7 viable HL-60 cells transduced with MSCV-miR-375 or MSCV-NC were injected subcutaneously into right flank of each nude mouse. a A photograph of xenografted tumors in mice xenografted by HL-60 cells, which were transduced with MSCV-miR-375 or MSCV-NC. b Volumes of all xenografted tumors were measured when the experiment was terminated at 42 days after tumor cell inoculation. c Net weights of all xenografted tumors were measured at the termination of the experiment. d The protein expression of HOXB3 was detected in xenografted tumor lysates from HL-60 cells transduced with MSCV-miR-375 or MSCV-NC. e THP1 cells were transduced with lentivirus vector pLVX-IRES-ZsGreen1 and GFP-positive cells were sorted by flow cytometry. The GFP-positive cells were further transduced with MSCV-miR-375 or MSCV-NC and treated with puromycin for 1 week. Then, THP1-GFP-miR-375 or THP1-GFP-NC were xenografted into NSG mice. Peripheral blood cells were extracted from mice when the mice became moribund and GFP-positive cells were analyzed by flow cytometry. * P

    Journal: BMC Cancer

    Article Title: A novel miR-375-HOXB3-CDCA3/DNMT3B regulatory circuitry contributes to leukemogenesis in acute myeloid leukemia

    doi: 10.1186/s12885-018-4097-z

    Figure Lengend Snippet: The anti-leukemia effects of miR-375 in vivo. About 1х10 7 viable HL-60 cells transduced with MSCV-miR-375 or MSCV-NC were injected subcutaneously into right flank of each nude mouse. a A photograph of xenografted tumors in mice xenografted by HL-60 cells, which were transduced with MSCV-miR-375 or MSCV-NC. b Volumes of all xenografted tumors were measured when the experiment was terminated at 42 days after tumor cell inoculation. c Net weights of all xenografted tumors were measured at the termination of the experiment. d The protein expression of HOXB3 was detected in xenografted tumor lysates from HL-60 cells transduced with MSCV-miR-375 or MSCV-NC. e THP1 cells were transduced with lentivirus vector pLVX-IRES-ZsGreen1 and GFP-positive cells were sorted by flow cytometry. The GFP-positive cells were further transduced with MSCV-miR-375 or MSCV-NC and treated with puromycin for 1 week. Then, THP1-GFP-miR-375 or THP1-GFP-NC were xenografted into NSG mice. Peripheral blood cells were extracted from mice when the mice became moribund and GFP-positive cells were analyzed by flow cytometry. * P

    Article Snippet: To produce plasmids expressing HOXB3 and DNMT3B, human HOXB3 and DNMT3B coding sequences were amplified by PCR and then cloned into lentivirus vector pLVX-IRES-ZsGreen1 (Clontech) and pMSCV-puro (Clontech), respectively.

    Techniques: In Vivo, Transduction, Injection, Mouse Assay, Expressing, Plasmid Preparation, Flow Cytometry, Cytometry

    Neural stem cells (NSC) produce and deliver BiTE LLON protein to tumors in vivo . BiTE transduced NSCs were sorted for the expression of A) ZsGreen1 (sample histogram) protein and evaluated for the production of BiTE proteins using immunocytochemistry by B) NSC LLON and C) NSC LLOFF cells immobilized on cover glass (cells-DAPI-nucleus(I), NSC-ZsGreen1(II), BiTE protein-α-His-Tag (III), and (IV) merged together, scale bar 50μm), and D) western blotting using anti-His Tag and anti-GAPDH antibodies. E) NSC LLON but not NSC LLOFF produced protein binding to IL13Rα2 protein immobilized on ELISA plates. F) Production dynamics of BiTE LLON by NSC LLON after 24 and 48 hours in culture (T-test, n=3, **p

    Journal: bioRxiv

    Article Title: Neural Stem Cells Secreting Bispecific T Cell Engager to Induce Selective Anti-Glioma Activity

    doi: 10.1101/2020.07.21.188441

    Figure Lengend Snippet: Neural stem cells (NSC) produce and deliver BiTE LLON protein to tumors in vivo . BiTE transduced NSCs were sorted for the expression of A) ZsGreen1 (sample histogram) protein and evaluated for the production of BiTE proteins using immunocytochemistry by B) NSC LLON and C) NSC LLOFF cells immobilized on cover glass (cells-DAPI-nucleus(I), NSC-ZsGreen1(II), BiTE protein-α-His-Tag (III), and (IV) merged together, scale bar 50μm), and D) western blotting using anti-His Tag and anti-GAPDH antibodies. E) NSC LLON but not NSC LLOFF produced protein binding to IL13Rα2 protein immobilized on ELISA plates. F) Production dynamics of BiTE LLON by NSC LLON after 24 and 48 hours in culture (T-test, n=3, **p

    Article Snippet: Generation of 293T and neural stem cells secreting BiTE protein The pLVX-IRES-ZsGreen1 plasmid (Takara Bio USA, Inc., Mountain View, CA) was used to generate construct encoding BiTE cDNA.

    Techniques: In Vivo, Expressing, Immunocytochemistry, Western Blot, Produced, Protein Binding, Enzyme-linked Immunosorbent Assay, T-Test