pegfp c3 Takara Search Results


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  • 91
    TaKaRa pegfp c3
    Expression plasmids used in this study. The genes encoding HCV proteins and their mutants were cloned into pcDNA3.1FlagHA, pcDNA3.1/ myc -His C, or <t>pEGFP-C3</t> as described in Materials and Methods. Other plasmids are described in the text or in the other figure legends.
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    TaKaRa plasmid pegfp c3
    Steady-state reporter mRNA analysis with overexpression of Flag-AUF1 proteins. (A) ARE sequences cloned into the 3′ UTR of β-Gal reporter plasmids, depicted as RNA nucleotides with the canonical AUUUA motifs underlined. AU, wild-type ARE from the GM-CSF 3′ UTR; GC, AU sequence with G and C point mutations. Also shown is the 3′ UTR of the control plasmid <t>pEGFP-C3.</t> (B) CHO cells were cotransfected with 1.0 μg of either the Flag expression plasmid or each individual Flag-AUF1 isoform per 10 7 cells and plasmids encoding mRNAs containing the GM-CSF ARE (AU) or the GC mutant ARE (GC). Cells were transfected with 0.5 μg of a GFP expression vector that lacks a significant AU-rich 3′ UTR. At 24 h posttransfection, total RNA was isolated, and equal amounts were analyzed by Northern blot hybridization using probes prepared from the lacZ gene. A representative blot is shown. Autoradiograms were quantified by densitometry, and the ratio of the β-Gal/GFP mRNAs for the vector Flag sample (lane 1) was set to 100%. The ratio of normalized β-Gal to GFP mRNA indicates the percent abundance of β-Gal mRNA relative to that of the untreated vector sample.
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    TaKaRa enzyme reagents plasmid pegfp c3
    Steady-state reporter mRNA analysis with overexpression of Flag-AUF1 proteins. (A) ARE sequences cloned into the 3′ UTR of β-Gal reporter plasmids, depicted as RNA nucleotides with the canonical AUUUA motifs underlined. AU, wild-type ARE from the GM-CSF 3′ UTR; GC, AU sequence with G and C point mutations. Also shown is the 3′ UTR of the control plasmid <t>pEGFP-C3.</t> (B) CHO cells were cotransfected with 1.0 μg of either the Flag expression plasmid or each individual Flag-AUF1 isoform per 10 7 cells and plasmids encoding mRNAs containing the GM-CSF ARE (AU) or the GC mutant ARE (GC). Cells were transfected with 0.5 μg of a GFP expression vector that lacks a significant AU-rich 3′ UTR. At 24 h posttransfection, total RNA was isolated, and equal amounts were analyzed by Northern blot hybridization using probes prepared from the lacZ gene. A representative blot is shown. Autoradiograms were quantified by densitometry, and the ratio of the β-Gal/GFP mRNAs for the vector Flag sample (lane 1) was set to 100%. The ratio of normalized β-Gal to GFP mRNA indicates the percent abundance of β-Gal mRNA relative to that of the untreated vector sample.
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    TaKaRa mammalian expression vector pegfp c3
    Steady-state reporter mRNA analysis with overexpression of Flag-AUF1 proteins. (A) ARE sequences cloned into the 3′ UTR of β-Gal reporter plasmids, depicted as RNA nucleotides with the canonical AUUUA motifs underlined. AU, wild-type ARE from the GM-CSF 3′ UTR; GC, AU sequence with G and C point mutations. Also shown is the 3′ UTR of the control plasmid <t>pEGFP-C3.</t> (B) CHO cells were cotransfected with 1.0 μg of either the Flag expression plasmid or each individual Flag-AUF1 isoform per 10 7 cells and plasmids encoding mRNAs containing the GM-CSF ARE (AU) or the GC mutant ARE (GC). Cells were transfected with 0.5 μg of a GFP expression vector that lacks a significant AU-rich 3′ UTR. At 24 h posttransfection, total RNA was isolated, and equal amounts were analyzed by Northern blot hybridization using probes prepared from the lacZ gene. A representative blot is shown. Autoradiograms were quantified by densitometry, and the ratio of the β-Gal/GFP mRNAs for the vector Flag sample (lane 1) was set to 100%. The ratio of normalized β-Gal to GFP mRNA indicates the percent abundance of β-Gal mRNA relative to that of the untreated vector sample.
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    TaKaRa promoter less pegfp c3
    Steady-state reporter mRNA analysis with overexpression of Flag-AUF1 proteins. (A) ARE sequences cloned into the 3′ UTR of β-Gal reporter plasmids, depicted as RNA nucleotides with the canonical AUUUA motifs underlined. AU, wild-type ARE from the GM-CSF 3′ UTR; GC, AU sequence with G and C point mutations. Also shown is the 3′ UTR of the control plasmid <t>pEGFP-C3.</t> (B) CHO cells were cotransfected with 1.0 μg of either the Flag expression plasmid or each individual Flag-AUF1 isoform per 10 7 cells and plasmids encoding mRNAs containing the GM-CSF ARE (AU) or the GC mutant ARE (GC). Cells were transfected with 0.5 μg of a GFP expression vector that lacks a significant AU-rich 3′ UTR. At 24 h posttransfection, total RNA was isolated, and equal amounts were analyzed by Northern blot hybridization using probes prepared from the lacZ gene. A representative blot is shown. Autoradiograms were quantified by densitometry, and the ratio of the β-Gal/GFP mRNAs for the vector Flag sample (lane 1) was set to 100%. The ratio of normalized β-Gal to GFP mRNA indicates the percent abundance of β-Gal mRNA relative to that of the untreated vector sample.
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    TaKaRa fluorescent protein
    Steady-state reporter mRNA analysis with overexpression of Flag-AUF1 proteins. (A) ARE sequences cloned into the 3′ UTR of β-Gal reporter plasmids, depicted as RNA nucleotides with the canonical AUUUA motifs underlined. AU, wild-type ARE from the GM-CSF 3′ UTR; GC, AU sequence with G and C point mutations. Also shown is the 3′ UTR of the control plasmid <t>pEGFP-C3.</t> (B) CHO cells were cotransfected with 1.0 μg of either the Flag expression plasmid or each individual Flag-AUF1 isoform per 10 7 cells and plasmids encoding mRNAs containing the GM-CSF ARE (AU) or the GC mutant ARE (GC). Cells were transfected with 0.5 μg of a GFP expression vector that lacks a significant AU-rich 3′ UTR. At 24 h posttransfection, total RNA was isolated, and equal amounts were analyzed by Northern blot hybridization using probes prepared from the lacZ gene. A representative blot is shown. Autoradiograms were quantified by densitometry, and the ratio of the β-Gal/GFP mRNAs for the vector Flag sample (lane 1) was set to 100%. The ratio of normalized β-Gal to GFP mRNA indicates the percent abundance of β-Gal mRNA relative to that of the untreated vector sample.
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    TaKaRa control vector pegfp c3
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    TaKaRa green fluorescence protein encoding pegfp c3
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    TaKaRa nhei linearized pegfpc3
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    TaKaRa pegfpc3 vector
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    TaKaRa expression vector pegfpc3
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    TaKaRa pegfpc3 clontech plasmid backbone
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    TaKaRa nhe i linearized pegfpc3 vector
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    TaKaRa pegfpc3 mammalian expression vector
    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with <t>pEGFP</t> ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P
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    Image Search Results


    Expression plasmids used in this study. The genes encoding HCV proteins and their mutants were cloned into pcDNA3.1FlagHA, pcDNA3.1/ myc -His C, or pEGFP-C3 as described in Materials and Methods. Other plasmids are described in the text or in the other figure legends.

    Journal: Journal of Virology

    Article Title: Intramembrane Proteolysis and Endoplasmic Reticulum Retention of Hepatitis C Virus Core Protein

    doi: 10.1128/JVI.78.12.6370-6380.2004

    Figure Lengend Snippet: Expression plasmids used in this study. The genes encoding HCV proteins and their mutants were cloned into pcDNA3.1FlagHA, pcDNA3.1/ myc -His C, or pEGFP-C3 as described in Materials and Methods. Other plasmids are described in the text or in the other figure legends.

    Article Snippet: The genes encoding core proteins with the region between amino acids 128 and 151 deleted and replacement of Leu139 , Val140 , and Leu144 with Ala were generated by the method of splicing by overlap extension ( , , ) and introduced into pEGFP-C3; these constructs are designated EGFP-Core Δ128-151 and EGFP-Core LVL/3A, respectively (Fig. ).

    Techniques: Expressing, Clone Assay

    Deficiency of uptake oxLDL by pEGFP-C3-CD36 was partially rescued by surface binding . The transfection was same as described in Fig. 4. After 48 hours of transfection, cells were rinsed with PBS twice and fixed with 4% paraformaldehyde for 30 min, and then incubated with Dil-OxLDL at 10 μg/ml for 2 hours at room temperature. After washed for three times with PBS, cells were collected and assayed with flow cytometry. The results are an average of three experiments. Dark box: oxLDL uptaking and grey box: oxLDL surface binding.

    Journal: Lipids in Health and Disease

    Article Title: Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells

    doi: 10.1186/1476-511X-6-24

    Figure Lengend Snippet: Deficiency of uptake oxLDL by pEGFP-C3-CD36 was partially rescued by surface binding . The transfection was same as described in Fig. 4. After 48 hours of transfection, cells were rinsed with PBS twice and fixed with 4% paraformaldehyde for 30 min, and then incubated with Dil-OxLDL at 10 μg/ml for 2 hours at room temperature. After washed for three times with PBS, cells were collected and assayed with flow cytometry. The results are an average of three experiments. Dark box: oxLDL uptaking and grey box: oxLDL surface binding.

    Article Snippet: Chemicals and materials pEGFP-C3 and pEGFP-N3 plasmid DNA were purchased from Clontech Laboratories, Inc. (Pulo Alto, CA, USA).

    Techniques: Binding Assay, Transfection, Incubation, Flow Cytometry, Cytometry

    Confocal microscopy to observe both GFP and huCD36 protein expression . Constructs of pEGFP-C3-CD36, pEGFP-N3-CD36, and pEGFP-N3 vector alone, were transit-transfected into CHO cells for 48 hours, and the transfected cells were then immunostained with anti-CD36 antibody, counter-stained with TRIC-conjugated anti-mouse IgG secondary antibody. After washing several times, cells were mounted on slides and observed under confocal microscope. Top panel: pEGFP-N3 transfected alone; Middle panel: cells transfected with pEGFP-C3-CD36; Bottom panel: pEGFP-N3-CD36 transfected. Both GFP and CD36 were expressed in two constructs.

    Journal: Lipids in Health and Disease

    Article Title: Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells

    doi: 10.1186/1476-511X-6-24

    Figure Lengend Snippet: Confocal microscopy to observe both GFP and huCD36 protein expression . Constructs of pEGFP-C3-CD36, pEGFP-N3-CD36, and pEGFP-N3 vector alone, were transit-transfected into CHO cells for 48 hours, and the transfected cells were then immunostained with anti-CD36 antibody, counter-stained with TRIC-conjugated anti-mouse IgG secondary antibody. After washing several times, cells were mounted on slides and observed under confocal microscope. Top panel: pEGFP-N3 transfected alone; Middle panel: cells transfected with pEGFP-C3-CD36; Bottom panel: pEGFP-N3-CD36 transfected. Both GFP and CD36 were expressed in two constructs.

    Article Snippet: Chemicals and materials pEGFP-C3 and pEGFP-N3 plasmid DNA were purchased from Clontech Laboratories, Inc. (Pulo Alto, CA, USA).

    Techniques: Confocal Microscopy, Expressing, Construct, Plasmid Preparation, Transfection, Staining, Microscopy

    pEGFP-C3-CD36 limited OxLDL uptake, but not for pEGFP-N3-CD36 . pEGFP-C3-CD36 and pEGFP-N3-CD36, as well as pEGFP-N3 alone were transit-transfected into CHO cells. After transfection for 48 hours, cells were rinsed twice with PBS and Dil-oxLDL at 10 μg/ml was incubated with the transfected cells for 1 hour. After rinsed for three times with PBS, cells were mounted on coverlids and observed under confocal microscope. Typical transfected and Dil-oxLDL was photographed. Dil-oxLDL was only weakly bound to pEGFP-C3-CD36 transfected cells.

    Journal: Lipids in Health and Disease

    Article Title: Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells

    doi: 10.1186/1476-511X-6-24

    Figure Lengend Snippet: pEGFP-C3-CD36 limited OxLDL uptake, but not for pEGFP-N3-CD36 . pEGFP-C3-CD36 and pEGFP-N3-CD36, as well as pEGFP-N3 alone were transit-transfected into CHO cells. After transfection for 48 hours, cells were rinsed twice with PBS and Dil-oxLDL at 10 μg/ml was incubated with the transfected cells for 1 hour. After rinsed for three times with PBS, cells were mounted on coverlids and observed under confocal microscope. Typical transfected and Dil-oxLDL was photographed. Dil-oxLDL was only weakly bound to pEGFP-C3-CD36 transfected cells.

    Article Snippet: Chemicals and materials pEGFP-C3 and pEGFP-N3 plasmid DNA were purchased from Clontech Laboratories, Inc. (Pulo Alto, CA, USA).

    Techniques: Transfection, Incubation, Microscopy

    Both N- and C-terminal tagged huCD36 bind normally to pRBCs . After transfection with pEGFP-C3-CD36, pEGFP-N3-CD36 or pEGFP-N3 alone, cells were fixed with 4% paraformaldehyde for 20 min and then rinsed twice with PBS. The cells were then incubated with pRBCs for 4 hours at room temperature with gent shacking. pRBCs bindings were observed under fluorescent microscope and typical binding cells were photographed. pRBCs were bound to both pEGFP-C3-CD36 and pEGFP-N3-CD36 transfected cells.

    Journal: Lipids in Health and Disease

    Article Title: Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells

    doi: 10.1186/1476-511X-6-24

    Figure Lengend Snippet: Both N- and C-terminal tagged huCD36 bind normally to pRBCs . After transfection with pEGFP-C3-CD36, pEGFP-N3-CD36 or pEGFP-N3 alone, cells were fixed with 4% paraformaldehyde for 20 min and then rinsed twice with PBS. The cells were then incubated with pRBCs for 4 hours at room temperature with gent shacking. pRBCs bindings were observed under fluorescent microscope and typical binding cells were photographed. pRBCs were bound to both pEGFP-C3-CD36 and pEGFP-N3-CD36 transfected cells.

    Article Snippet: Chemicals and materials pEGFP-C3 and pEGFP-N3 plasmid DNA were purchased from Clontech Laboratories, Inc. (Pulo Alto, CA, USA).

    Techniques: Transfection, Incubation, Microscopy, Binding Assay

    Schematic diagram of p-EGFP-C3-CD36 and peGFP-N3-Cd36 constructs . A, the coding sites of vectors, pEGFP-C3 and pEGFP-N3, were restriction enzymatically cut with both Hind III and Kpn I and the DNA fragments were purified. The inserts, PCR-amplified hCD36 coding sequences after purification, were ligated into the vectors, resulted in recombinant constructs of pEGFP-C3-CD36 or pEGFP-N3-CD36. B, 2% agarose gel to confirm the DNA constructs. Lane 1 and 2, Hind III and Kpn I cut and then purified pEGFP-C3 and pEGFP-N3 plasmid DNAs; Lane 3, purified PCR-amplified huCD36 cDNAs; Lane 4, PEGFP-C3-huCD36 constructs; Lane 5, pEGFP-N3-huCD36 constructs; Lane 6 and 7 are re-digested pEGF-C3-hCD36 and pEGFP-N3-hCD36 with Hind III and Kpn I. Lane 8, 1 Kb DNA markers.

    Journal: Lipids in Health and Disease

    Article Title: Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells

    doi: 10.1186/1476-511X-6-24

    Figure Lengend Snippet: Schematic diagram of p-EGFP-C3-CD36 and peGFP-N3-Cd36 constructs . A, the coding sites of vectors, pEGFP-C3 and pEGFP-N3, were restriction enzymatically cut with both Hind III and Kpn I and the DNA fragments were purified. The inserts, PCR-amplified hCD36 coding sequences after purification, were ligated into the vectors, resulted in recombinant constructs of pEGFP-C3-CD36 or pEGFP-N3-CD36. B, 2% agarose gel to confirm the DNA constructs. Lane 1 and 2, Hind III and Kpn I cut and then purified pEGFP-C3 and pEGFP-N3 plasmid DNAs; Lane 3, purified PCR-amplified huCD36 cDNAs; Lane 4, PEGFP-C3-huCD36 constructs; Lane 5, pEGFP-N3-huCD36 constructs; Lane 6 and 7 are re-digested pEGF-C3-hCD36 and pEGFP-N3-hCD36 with Hind III and Kpn I. Lane 8, 1 Kb DNA markers.

    Article Snippet: Chemicals and materials pEGFP-C3 and pEGFP-N3 plasmid DNA were purchased from Clontech Laboratories, Inc. (Pulo Alto, CA, USA).

    Techniques: Construct, Purification, Polymerase Chain Reaction, Amplification, Recombinant, Agarose Gel Electrophoresis, Plasmid Preparation

    Steady-state reporter mRNA analysis with overexpression of Flag-AUF1 proteins. (A) ARE sequences cloned into the 3′ UTR of β-Gal reporter plasmids, depicted as RNA nucleotides with the canonical AUUUA motifs underlined. AU, wild-type ARE from the GM-CSF 3′ UTR; GC, AU sequence with G and C point mutations. Also shown is the 3′ UTR of the control plasmid pEGFP-C3. (B) CHO cells were cotransfected with 1.0 μg of either the Flag expression plasmid or each individual Flag-AUF1 isoform per 10 7 cells and plasmids encoding mRNAs containing the GM-CSF ARE (AU) or the GC mutant ARE (GC). Cells were transfected with 0.5 μg of a GFP expression vector that lacks a significant AU-rich 3′ UTR. At 24 h posttransfection, total RNA was isolated, and equal amounts were analyzed by Northern blot hybridization using probes prepared from the lacZ gene. A representative blot is shown. Autoradiograms were quantified by densitometry, and the ratio of the β-Gal/GFP mRNAs for the vector Flag sample (lane 1) was set to 100%. The ratio of normalized β-Gal to GFP mRNA indicates the percent abundance of β-Gal mRNA relative to that of the untreated vector sample.

    Journal: Molecular and Cellular Biology

    Article Title: Selective Degradation of AU-Rich mRNAs Promoted by the p37 AUF1 Protein Isoform

    doi: 10.1128/MCB.23.18.6685-6693.2003

    Figure Lengend Snippet: Steady-state reporter mRNA analysis with overexpression of Flag-AUF1 proteins. (A) ARE sequences cloned into the 3′ UTR of β-Gal reporter plasmids, depicted as RNA nucleotides with the canonical AUUUA motifs underlined. AU, wild-type ARE from the GM-CSF 3′ UTR; GC, AU sequence with G and C point mutations. Also shown is the 3′ UTR of the control plasmid pEGFP-C3. (B) CHO cells were cotransfected with 1.0 μg of either the Flag expression plasmid or each individual Flag-AUF1 isoform per 10 7 cells and plasmids encoding mRNAs containing the GM-CSF ARE (AU) or the GC mutant ARE (GC). Cells were transfected with 0.5 μg of a GFP expression vector that lacks a significant AU-rich 3′ UTR. At 24 h posttransfection, total RNA was isolated, and equal amounts were analyzed by Northern blot hybridization using probes prepared from the lacZ gene. A representative blot is shown. Autoradiograms were quantified by densitometry, and the ratio of the β-Gal/GFP mRNAs for the vector Flag sample (lane 1) was set to 100%. The ratio of normalized β-Gal to GFP mRNA indicates the percent abundance of β-Gal mRNA relative to that of the untreated vector sample.

    Article Snippet: The DNA sequence of the 3′ UTR of the plasmid pEGFP-C3 was assigned GenBank accession no. .

    Techniques: Over Expression, Clone Assay, Sequencing, Plasmid Preparation, Expressing, Mutagenesis, Transfection, Isolation, Northern Blot, Hybridization

    Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with pEGFP ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P

    Journal: FEBS Open Bio

    Article Title: Neutral ceramidase‐enriched exosomes prevent palmitic acid‐induced insulin resistance in H4 IIEC3 hepatocytes

    doi: 10.1002/2211-5463.12125

    Figure Lengend Snippet: Neutral ceramidase‐Exos have a higher NCD ase activity than Con‐Exos. Exosomes from INS ‐1 cells transfected with pEGFP ‐C3‐ NCD ase ( NCD ase‐Exo) had higher NCD ase activity compared with the exosomes from INS ‐1 cells transfected with the control vector pEGFP ‐C3 (Con‐Exo), # vs. *: P

    Article Snippet: Similarly, exosomes from INS‐1 cells transfected with the control vector pEGFP‐C3 are termed Con‐Exos.

    Techniques: Activity Assay, Transfection, Plasmid Preparation