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  • 92
    Addgene inc pcdna3 1
    Schematic representation of ATF/ SOX2 ( A ) Design of Artificial zinc finger protein (AZP) to target a 19 bp sequence (-161: TGCCCCCTCCTCCCCCGGC:-143) in human SOX2 distal promoter region. TSS; transcription start site. ( B ) The Artificial Transcription Factor (ATF) contains the KOX suppressor domain, a nuclear localization signal (NLS), the Artificial zinc finger protein (AZP) and a FLAG tag. We termed this ATF as ATF/ SOX2 . ( C ) Schematic representation of Ad-null, Ad-sh SOX2 and Ad-ATF/ SOX2. The PCR-generated expression cassette of ATF/ SOX2 from <t>pcDNA3.1</t> ATF/ SOX2 or sh SOX2 from pBAsi-mU6 sh SOX2 (described in Materials and Methods section) were subcloned into the linearized E1 deleted adenovirus type 5 genome. E1; Adenovirus early region 1, E3; Adenovirus early region 3, LITR; Left Inverted Terminal Repeat, RITR; Right Inverted Terminal Repeat.
    Pcdna3 1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 970 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa pcdna3 1
    FOXM1 binds to human HK2 promoter and directly enhances its transcription A. putative FOXM1-binding sites in the HK2 promoter and construction of reporter plasmids. B. ChIP analysis of the HK2 promoter using antibodies against FOXM1 in A2780 and SKOV3 cells. C. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or FOXM1 shRNA plasmid. D. the transcriptional activity of FOXM1 on HK2-luc wide type (WT) or mutants (MT) was analyzed by luciferase reporter assay in A2780 and SKOV3 cells. E. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or <t>pcDNA3.1-FOXM1</t> plasmid. Promoter activity was examined using a dual luciferase assay kit. The data represent three independent experiments, each bar represents mean ± SD. P values were calculated using a Student t-test (** P
    Pcdna3 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 94/100, based on 1445 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Shanghai GenePharma pcdna3 1
    FOXM1 binds to human HK2 promoter and directly enhances its transcription A. putative FOXM1-binding sites in the HK2 promoter and construction of reporter plasmids. B. ChIP analysis of the HK2 promoter using antibodies against FOXM1 in A2780 and SKOV3 cells. C. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or FOXM1 shRNA plasmid. D. the transcriptional activity of FOXM1 on HK2-luc wide type (WT) or mutants (MT) was analyzed by luciferase reporter assay in A2780 and SKOV3 cells. E. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or <t>pcDNA3.1-FOXM1</t> plasmid. Promoter activity was examined using a dual luciferase assay kit. The data represent three independent experiments, each bar represents mean ± SD. P values were calculated using a Student t-test (** P
    Pcdna3 1, supplied by Shanghai GenePharma, used in various techniques. Bioz Stars score: 91/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pcdna3 1
    Fig. 4. γ 1 –σ 1 AP-1 subcomplex is retained on rabaptin-5α beads. ( A ) GST or GST–rabaptin-5α(301–592) were incubated with glutathione–Sepharose and a HeLa cell extract. The western blot of bound (B) and non-bound (NB) fractions was probed with antibodies against γ 1 , β 1/2 , σ 1 , µ 1 and clathrin. ( B ) IF of clathrin and rabaptin-5α in cells transfected with rabaptin-5α or co-transfected with rabaptin-5α and γ 1 -adaptin. Cells were permeabilized, fixed and labelled with a rabbit antibody against rabaptin-5α (green) and X-22 against clathrin (red). ( C ) HeLa cells were labelled with [ 35 S]methionine and the lysate was incubated with GST–rabaptin-5α(301–592). Bound material was eluted with glutathione. Eluate and cell lysate were incubated with antibodies against γ 1 (100/3), β 1/2 (100/1), µ 1 and σ 1 , and protein A beads. Immunoprecipitates were resolved by SDS–PAGE and analysed by phosphorimaging. To detect σ 1 in the GSH eluate, gels were exposed 10 times longer than for γ 1 -adaptin (σ1 contains four times less methionine residues than γ 1 -adaptin). ( D ) Rabaptin-5α and γ 1 -adaptin co-localize on endosomes in the absence of intact AP-1. µ 1 A–/– and µ 1 A+/+ fibroblasts were transfected with <t>rabaptin-5α-pcDNA3.1His.</t> For γ 1 -adaptin labelling in µ 1 A+/+ fibroblasts, cells were extracted with saponin before fixation. Note that γ 1 -adaptin in these cells is not only present on the structures containing rabaptin-5α (arrows), but also in the TGN area (arrow heads). Saponin treatment of µ 1 A–/– cells removed all γ 1 -adaptin labelling (not shown). Cells were fixed, and labelled with a rabbit antibody against rabaptin-5α (red) and mouse γ 1 -adaptin antibody (Transduction labs) (green). Bar, 10 µm.
    Pcdna3 1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 49713 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GenePharma Company pcdna3 1
    Carnosic acid inhibits LX2 activation by inhibiting HMGB1. LX2 cells were randomly divided into three groups: <t>pcDNA3.1-control,</t> pcDNA3.1-control + CA (20 μM), and pcDNA3.1-HMGB1 + CA (20 μM). After transfection with the plasmid for 24 h, the cells were treated with CA for 12 h, and protein was then extracted. The protein expression levels of α-SMA, HMGB1, TLR4 and nuclear NF-κB p65 in LX2 cells were detected by western blot ( n = 3). The data are presented as the means ± SD. ∗∗ P
    Pcdna3 1, supplied by GenePharma Company, used in various techniques. Bioz Stars score: 93/100, based on 436 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega pcdna3 1
    PRRX1 promotes myoblast proliferation. (A,C) The overexpression efficiency of the <t>pcDNA3.1</t> with PRRX1 in CPMs and QM-7 cells. (B,D) The interference efficiency of PRRX1 SiRNA in CPMs and QM-7 cells. (E,G) Cell cycle after overexpression of PRRX1 in CPMs and QM-7 cells. (F,H) Cell cycle after interference of PRRX1 in CPMs and QM-7 cells. (I–L) Cell growth curves were measured following the transfection of PRRX1 overexpression vector and SiRNA in CPMs and QM-7 cells. (M,O) Evaluation of the proliferation of PRRX1 -transfected CPMs and QM-7 cells by EdU incorporation, EdU-stained cell proportions were counted. (N,P) Evaluation of the proliferation of PRRX1 SiRNA-transfected CPMs and QM-7 cells by EdU incorporation, EdU-stained cell proportions were counted. The results of all groups are shown as mean ± S.E.M., and the data represent three independent assessment methods. Statistical significance of the mean difference was assessed using an unpaired two-sample t -tests ( ∗ p
    Pcdna3 1, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 1435 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene pcdna3 1
    Elevated expression of PLD1 suppresses DNA damage-induced increases in the level of p53 in cells where PLD provides survival signals. (A) 3Y1 c-Src and 3Y1 c-Src ). (B) 3Y1 and 3Y1-P1 cells were treated with CPT, ADR, and PonA, and p53 levels were determined as described above. (C) MCF-7 cells stably transfected with <t>pcDNA3.1(−)-PLD2</t> or the parental pcDNA3.1(−) vector were treated with either CPT or ADR, and p53 levels were determined as described above. (D) The relative levels of PLD2 protein determined by Western blot and PLD activity in the MCF-7 cells stably expressing PLD2 and transfected with the parental empty vector are shown. The data shown are representative of results obtained at least three times.
    Pcdna3 1, supplied by Stratagene, used in various techniques. Bioz Stars score: 92/100, based on 885 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Sangon Biotech pcdna3 1
    Effects of transfection on Sirtuin 1 (Sirt1) expression. BaF3 cells were transfected with empty <t>pcDNA3.1,</t> pc-Sirt1, scrambled shRNA, or shRNA against Sirt1 respectively, and then the transfection efficiency was tested by RT-PCR ( A ) and Western blot analysis ( B ). GAPDH was used as an internal control. * p
    Pcdna3 1, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 91/100, based on 167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GenScript pcdna3 1
    Reciprocal proliferation effects of GLI1 and <t>FOXS1;</t> FOXS1 inhibits GLI1 activity. EdU incorporation assay of Rh36 cells (A) and Daoy cells (B) following transfection with siRNA combinations of siControl + siControl, siControl + siGLI1, siControl + siFOXS1, or siGLI1 + siFOXS1. Data from one representative experiment are shown in the histogram. EdU incorporation assay of Daoy cells (C) following transfection/transduction with siControl + Ad‐Vector, siControl + Ad‐GLI1, siFOXS1 + Ad‐Vector, or siFOXS1 + Ad‐GLI1. Adenoviruses were added 6 h after siRNA transfection. Data from one representative experiment are shown in the histogram. (D) A schematic diagram of the proposed model for the FOXS1/GLI1 feedback loop. The transcription factor GLI1 positively regulates the expression of the FOXS1 transcription factor, while FOXS1 negatively regulates GLI1. GLI1 promotes cell proliferation, whereas FOXS1 inhibits cell proliferation. (E) FOXS1 expression reduces GLI1 transcriptional activity. HEK293A cells were co‐transfected with <t>pcDNA3.1</t> vector (pcDNA), pGL3 basic luciferase empty vector (pGL3), pCMV‐GLI1‐flag (pGLI1), or pcDNA3.1‐FOXS1 (pFOXS1), together with the reporter plasmid 12xGLIBS and the control plasmid Renilla. Data from one representative experiment are shown. Error bars indicate standard deviation. Statistical significant, ## P
    Pcdna3 1, supplied by GenScript, used in various techniques. Bioz Stars score: 93/100, based on 627 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Genewiz pcdna3 1
    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the <t>pcDNA3.1</t> expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is
    Pcdna3 1, supplied by Genewiz, used in various techniques. Bioz Stars score: 92/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Sino Biological pcdna3 1
    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the <t>pcDNA3.1</t> expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is
    Pcdna3 1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Genechem pcdna3 1
    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the <t>pcDNA3.1</t> expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is
    Pcdna3 1, supplied by Genechem, used in various techniques. Bioz Stars score: 92/100, based on 128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio Basic Canada pcdna3 1
    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the <t>pcDNA3.1</t> expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is
    Pcdna3 1, supplied by Bio Basic Canada, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Glaxo Smith pcdna3 1
    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the <t>pcDNA3.1</t> expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is
    Pcdna3 1, supplied by Glaxo Smith, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology pcdna3 1
    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the <t>pcDNA3.1</t> expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is
    Pcdna3 1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    BIO-CAT pcdna3 1
    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the <t>pcDNA3.1</t> expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is
    Pcdna3 1, supplied by BIO-CAT, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Genecopoeia pcdna3 1
    Involvement of matrix metalloproteinases (MMPs) and E-cadherin in Src-promoted keratinocyte migration. (A and B) Western blot analysis of MMP-2, MMP-9 and E-cadherin expression in keratinocytes following transfection with overexpressing Src <t>[pcDNA3.1(+)-Src]</t> or silencing Src (Src-siRNA), or the corresponding controls. Controls used were untransfected cells (control) and pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA. Actin was used as a loading control. Bars represent the means ± SEM of n=4 tissue samples. * P
    Pcdna3 1, supplied by Genecopoeia, used in various techniques. Bioz Stars score: 90/100, based on 86 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pcdna3 1 pc3 1 expression vector
    Involvement of matrix metalloproteinases (MMPs) and E-cadherin in Src-promoted keratinocyte migration. (A and B) Western blot analysis of MMP-2, MMP-9 and E-cadherin expression in keratinocytes following transfection with overexpressing Src <t>[pcDNA3.1(+)-Src]</t> or silencing Src (Src-siRNA), or the corresponding controls. Controls used were untransfected cells (control) and pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA. Actin was used as a loading control. Bars represent the means ± SEM of n=4 tissue samples. * P
    Pcdna3 1 Pc3 1 Expression Vector, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pcdna3 1 a
    Involvement of matrix metalloproteinases (MMPs) and E-cadherin in Src-promoted keratinocyte migration. (A and B) Western blot analysis of MMP-2, MMP-9 and E-cadherin expression in keratinocytes following transfection with overexpressing Src <t>[pcDNA3.1(+)-Src]</t> or silencing Src (Src-siRNA), or the corresponding controls. Controls used were untransfected cells (control) and pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA. Actin was used as a loading control. Bars represent the means ± SEM of n=4 tissue samples. * P
    Pcdna3 1 A, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa pcdna3 1 clontech
    Involvement of matrix metalloproteinases (MMPs) and E-cadherin in Src-promoted keratinocyte migration. (A and B) Western blot analysis of MMP-2, MMP-9 and E-cadherin expression in keratinocytes following transfection with overexpressing Src <t>[pcDNA3.1(+)-Src]</t> or silencing Src (Src-siRNA), or the corresponding controls. Controls used were untransfected cells (control) and pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA. Actin was used as a loading control. Bars represent the means ± SEM of n=4 tissue samples. * P
    Pcdna3 1 Clontech, supplied by TaKaRa, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pcdna3 1 myc
    WDR5 bound to SMC-marker gene promoter loci. A , stable cell lines containing either empty or Myc-WDR5 expression plasmid had comparable differentiation potential to the original A404 cell line. Control stable , stable A404 cell line containing empty <t>pcDNA3.1</t>
    Pcdna3 1 Myc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 737 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pcdna3 1 mrfp
    WDR5 bound to SMC-marker gene promoter loci. A , stable cell lines containing either empty or Myc-WDR5 expression plasmid had comparable differentiation potential to the original A404 cell line. Control stable , stable A404 cell line containing empty <t>pcDNA3.1</t>
    Pcdna3 1 Mrfp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pcdna3 1 mychisa
    WDR5 bound to SMC-marker gene promoter loci. A , stable cell lines containing either empty or Myc-WDR5 expression plasmid had comparable differentiation potential to the original A404 cell line. Control stable , stable A404 cell line containing empty <t>pcDNA3.1</t>
    Pcdna3 1 Mychisa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GenScript pcdna3 1 sox2
    WDR5 bound to SMC-marker gene promoter loci. A , stable cell lines containing either empty or Myc-WDR5 expression plasmid had comparable differentiation potential to the original A404 cell line. Control stable , stable A404 cell line containing empty <t>pcDNA3.1</t>
    Pcdna3 1 Sox2, supplied by GenScript, used in various techniques. Bioz Stars score: 94/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Schematic representation of ATF/ SOX2 ( A ) Design of Artificial zinc finger protein (AZP) to target a 19 bp sequence (-161: TGCCCCCTCCTCCCCCGGC:-143) in human SOX2 distal promoter region. TSS; transcription start site. ( B ) The Artificial Transcription Factor (ATF) contains the KOX suppressor domain, a nuclear localization signal (NLS), the Artificial zinc finger protein (AZP) and a FLAG tag. We termed this ATF as ATF/ SOX2 . ( C ) Schematic representation of Ad-null, Ad-sh SOX2 and Ad-ATF/ SOX2. The PCR-generated expression cassette of ATF/ SOX2 from pcDNA3.1 ATF/ SOX2 or sh SOX2 from pBAsi-mU6 sh SOX2 (described in Materials and Methods section) were subcloned into the linearized E1 deleted adenovirus type 5 genome. E1; Adenovirus early region 1, E3; Adenovirus early region 3, LITR; Left Inverted Terminal Repeat, RITR; Right Inverted Terminal Repeat.

    Journal: Oncotarget

    Article Title: Targeted silencing of SOX2 by an artificial transcription factor showed antitumor effect in lung and esophageal squamous cell carcinoma

    doi: 10.18632/oncotarget.21523

    Figure Lengend Snippet: Schematic representation of ATF/ SOX2 ( A ) Design of Artificial zinc finger protein (AZP) to target a 19 bp sequence (-161: TGCCCCCTCCTCCCCCGGC:-143) in human SOX2 distal promoter region. TSS; transcription start site. ( B ) The Artificial Transcription Factor (ATF) contains the KOX suppressor domain, a nuclear localization signal (NLS), the Artificial zinc finger protein (AZP) and a FLAG tag. We termed this ATF as ATF/ SOX2 . ( C ) Schematic representation of Ad-null, Ad-sh SOX2 and Ad-ATF/ SOX2. The PCR-generated expression cassette of ATF/ SOX2 from pcDNA3.1 ATF/ SOX2 or sh SOX2 from pBAsi-mU6 sh SOX2 (described in Materials and Methods section) were subcloned into the linearized E1 deleted adenovirus type 5 genome. E1; Adenovirus early region 1, E3; Adenovirus early region 3, LITR; Left Inverted Terminal Repeat, RITR; Right Inverted Terminal Repeat.

    Article Snippet: To enrich for transfected cells, plasmid with puromycin resistant cassette pPUR (0.5 μg, Takara Bio, Inc.) was co-transfected with pcDNA3.1, pGFPZFN1.4-B2H, pGFPZFN2-B2H, pST1374, pPIGAZFN-L1 and pPIGAZFN-R2 (2 μg, obtained from Addgene, Cambridge, MA) [ ].

    Techniques: Sequencing, FLAG-tag, Polymerase Chain Reaction, Generated, Expressing

    Repression of SOX2 transcriptional activity and protein expression by ATF/ SOX2 in lung and esophageal SCC cells ( A ) Schematic representation of SOX2 distal and proximal promoter reporter constructs. TSS; transcription start site. Luc; Luciferase. ( B ) Transient transfection reporter assays in lung SCC cells and esophageal squamous carcinoma cells with the indicated luciferase reporter constructs (2 μg, pGL4), effector constructs (2 μg, pcDNA3.1) and pCMV. β-gal (1 μg). Results are presented as fold induction of relative light units normalized to β-galactosidase activity relative to that observed for control constructs. Statistical analysis was performed using Student’s t test (two-tailed, unpaired). Statistical significance was defined as * p

    Journal: Oncotarget

    Article Title: Targeted silencing of SOX2 by an artificial transcription factor showed antitumor effect in lung and esophageal squamous cell carcinoma

    doi: 10.18632/oncotarget.21523

    Figure Lengend Snippet: Repression of SOX2 transcriptional activity and protein expression by ATF/ SOX2 in lung and esophageal SCC cells ( A ) Schematic representation of SOX2 distal and proximal promoter reporter constructs. TSS; transcription start site. Luc; Luciferase. ( B ) Transient transfection reporter assays in lung SCC cells and esophageal squamous carcinoma cells with the indicated luciferase reporter constructs (2 μg, pGL4), effector constructs (2 μg, pcDNA3.1) and pCMV. β-gal (1 μg). Results are presented as fold induction of relative light units normalized to β-galactosidase activity relative to that observed for control constructs. Statistical analysis was performed using Student’s t test (two-tailed, unpaired). Statistical significance was defined as * p

    Article Snippet: To enrich for transfected cells, plasmid with puromycin resistant cassette pPUR (0.5 μg, Takara Bio, Inc.) was co-transfected with pcDNA3.1, pGFPZFN1.4-B2H, pGFPZFN2-B2H, pST1374, pPIGAZFN-L1 and pPIGAZFN-R2 (2 μg, obtained from Addgene, Cambridge, MA) [ ].

    Techniques: Activity Assay, Expressing, Construct, Luciferase, Transfection, Two Tailed Test

    FOXM1 binds to human HK2 promoter and directly enhances its transcription A. putative FOXM1-binding sites in the HK2 promoter and construction of reporter plasmids. B. ChIP analysis of the HK2 promoter using antibodies against FOXM1 in A2780 and SKOV3 cells. C. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or FOXM1 shRNA plasmid. D. the transcriptional activity of FOXM1 on HK2-luc wide type (WT) or mutants (MT) was analyzed by luciferase reporter assay in A2780 and SKOV3 cells. E. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or pcDNA3.1-FOXM1 plasmid. Promoter activity was examined using a dual luciferase assay kit. The data represent three independent experiments, each bar represents mean ± SD. P values were calculated using a Student t-test (** P

    Journal: Oncotarget

    Article Title: FOXM1 promotes reprogramming of glucose metabolism in epithelial ovarian cancer cells via activation of GLUT1 and HK2 transcription

    doi: 10.18632/oncotarget.10103

    Figure Lengend Snippet: FOXM1 binds to human HK2 promoter and directly enhances its transcription A. putative FOXM1-binding sites in the HK2 promoter and construction of reporter plasmids. B. ChIP analysis of the HK2 promoter using antibodies against FOXM1 in A2780 and SKOV3 cells. C. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or FOXM1 shRNA plasmid. D. the transcriptional activity of FOXM1 on HK2-luc wide type (WT) or mutants (MT) was analyzed by luciferase reporter assay in A2780 and SKOV3 cells. E. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or pcDNA3.1-FOXM1 plasmid. Promoter activity was examined using a dual luciferase assay kit. The data represent three independent experiments, each bar represents mean ± SD. P values were calculated using a Student t-test (** P

    Article Snippet: The coding regions of FOXM1 were inserted into pcDNA3.1 (Clontech, Mountain View, CA).

    Techniques: Binding Assay, Chromatin Immunoprecipitation, Activity Assay, Construct, Plasmid Preparation, shRNA, Luciferase, Reporter Assay

    FOXM1 binds to human GLUT1 promoter and directly enhances its transcription A. a putative FOXM1-binding site in the GLUT1 promoter and construction of reporter plasmids. B. ChIP analysis of the GLUT1 promoter using antibodies against FOXM1 in A2780 and SKOV3 cells. C. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or FOXM1 shRNA plasmid. D. the transcriptional activity of FOXM1 on GLUT1-luc wide type (WT) or mutants (MT) was analyzed by luciferase reporter assay in A2780 and SKOV3 cells. E. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or pcDNA3.1-FOXM1 plasmid. Promoter activity was examined using a dual luciferase assay kit. The data represent three independent experiments, each bar represents mean ± SD. P values were calculated using a Student t-test (** P

    Journal: Oncotarget

    Article Title: FOXM1 promotes reprogramming of glucose metabolism in epithelial ovarian cancer cells via activation of GLUT1 and HK2 transcription

    doi: 10.18632/oncotarget.10103

    Figure Lengend Snippet: FOXM1 binds to human GLUT1 promoter and directly enhances its transcription A. a putative FOXM1-binding site in the GLUT1 promoter and construction of reporter plasmids. B. ChIP analysis of the GLUT1 promoter using antibodies against FOXM1 in A2780 and SKOV3 cells. C. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or FOXM1 shRNA plasmid. D. the transcriptional activity of FOXM1 on GLUT1-luc wide type (WT) or mutants (MT) was analyzed by luciferase reporter assay in A2780 and SKOV3 cells. E. the promoter activity of two truncated constructs was measured in A2780 and SKOV3 cells when cotransfected with the control plasmid or pcDNA3.1-FOXM1 plasmid. Promoter activity was examined using a dual luciferase assay kit. The data represent three independent experiments, each bar represents mean ± SD. P values were calculated using a Student t-test (** P

    Article Snippet: The coding regions of FOXM1 were inserted into pcDNA3.1 (Clontech, Mountain View, CA).

    Techniques: Binding Assay, Chromatin Immunoprecipitation, Activity Assay, Construct, Plasmid Preparation, shRNA, Luciferase, Reporter Assay

    Fig. 4. γ 1 –σ 1 AP-1 subcomplex is retained on rabaptin-5α beads. ( A ) GST or GST–rabaptin-5α(301–592) were incubated with glutathione–Sepharose and a HeLa cell extract. The western blot of bound (B) and non-bound (NB) fractions was probed with antibodies against γ 1 , β 1/2 , σ 1 , µ 1 and clathrin. ( B ) IF of clathrin and rabaptin-5α in cells transfected with rabaptin-5α or co-transfected with rabaptin-5α and γ 1 -adaptin. Cells were permeabilized, fixed and labelled with a rabbit antibody against rabaptin-5α (green) and X-22 against clathrin (red). ( C ) HeLa cells were labelled with [ 35 S]methionine and the lysate was incubated with GST–rabaptin-5α(301–592). Bound material was eluted with glutathione. Eluate and cell lysate were incubated with antibodies against γ 1 (100/3), β 1/2 (100/1), µ 1 and σ 1 , and protein A beads. Immunoprecipitates were resolved by SDS–PAGE and analysed by phosphorimaging. To detect σ 1 in the GSH eluate, gels were exposed 10 times longer than for γ 1 -adaptin (σ1 contains four times less methionine residues than γ 1 -adaptin). ( D ) Rabaptin-5α and γ 1 -adaptin co-localize on endosomes in the absence of intact AP-1. µ 1 A–/– and µ 1 A+/+ fibroblasts were transfected with rabaptin-5α-pcDNA3.1His. For γ 1 -adaptin labelling in µ 1 A+/+ fibroblasts, cells were extracted with saponin before fixation. Note that γ 1 -adaptin in these cells is not only present on the structures containing rabaptin-5α (arrows), but also in the TGN area (arrow heads). Saponin treatment of µ 1 A–/– cells removed all γ 1 -adaptin labelling (not shown). Cells were fixed, and labelled with a rabbit antibody against rabaptin-5α (red) and mouse γ 1 -adaptin antibody (Transduction labs) (green). Bar, 10 µm.

    Journal: The EMBO Journal

    Article Title: Rabaptin-5?/rabaptin-4 serves as a linker between rab4 and ?1-adaptin in membrane recycling from endosomes

    doi: 10.1093/emboj/cdg257

    Figure Lengend Snippet: Fig. 4. γ 1 –σ 1 AP-1 subcomplex is retained on rabaptin-5α beads. ( A ) GST or GST–rabaptin-5α(301–592) were incubated with glutathione–Sepharose and a HeLa cell extract. The western blot of bound (B) and non-bound (NB) fractions was probed with antibodies against γ 1 , β 1/2 , σ 1 , µ 1 and clathrin. ( B ) IF of clathrin and rabaptin-5α in cells transfected with rabaptin-5α or co-transfected with rabaptin-5α and γ 1 -adaptin. Cells were permeabilized, fixed and labelled with a rabbit antibody against rabaptin-5α (green) and X-22 against clathrin (red). ( C ) HeLa cells were labelled with [ 35 S]methionine and the lysate was incubated with GST–rabaptin-5α(301–592). Bound material was eluted with glutathione. Eluate and cell lysate were incubated with antibodies against γ 1 (100/3), β 1/2 (100/1), µ 1 and σ 1 , and protein A beads. Immunoprecipitates were resolved by SDS–PAGE and analysed by phosphorimaging. To detect σ 1 in the GSH eluate, gels were exposed 10 times longer than for γ 1 -adaptin (σ1 contains four times less methionine residues than γ 1 -adaptin). ( D ) Rabaptin-5α and γ 1 -adaptin co-localize on endosomes in the absence of intact AP-1. µ 1 A–/– and µ 1 A+/+ fibroblasts were transfected with rabaptin-5α-pcDNA3.1His. For γ 1 -adaptin labelling in µ 1 A+/+ fibroblasts, cells were extracted with saponin before fixation. Note that γ 1 -adaptin in these cells is not only present on the structures containing rabaptin-5α (arrows), but also in the TGN area (arrow heads). Saponin treatment of µ 1 A–/– cells removed all γ 1 -adaptin labelling (not shown). Cells were fixed, and labelled with a rabbit antibody against rabaptin-5α (red) and mouse γ 1 -adaptin antibody (Transduction labs) (green). Bar, 10 µm.

    Article Snippet: Rabaptin constructs were cloned in pcDNA3 and pcDNA3.1His (Invitrogen, Leek, The Netherlands).

    Techniques: Incubation, Western Blot, Transfection, SDS Page, Transduction

    Fig. 2. Rabaptin-5α–γ-adaptin complex is localized on endosomes. HeLa cells were transfected with rabaptin-5α-pcDNA3.1His (left panels) or with rabaptin-5α and γ 1 -adaptin-pcDNA3 (right panels). Transfected cells were labelled for rabaptin-5α (green) and γ 1 -adaptin (red). Note the co-localization of rabaptin-5α and γ 1 -adaptin in transfected cells, and the distinct localization of γ 1 -adaptin in non-transfected cells (arrow) ( A and A ′). Cells were incubated with Alexa594-Tf for 60 min at 37°C and subsequently labelled with anti-Xpress antibody and Alexa488-conjugated IgG ( B and B ′). The TGN marker TGN46 does not relocate to enlarged endosomes. Transfected cells were labelled for rabaptin-5α (red) and TGN46 (green) ( C and C ′). Bar, 10 µm.

    Journal: The EMBO Journal

    Article Title: Rabaptin-5?/rabaptin-4 serves as a linker between rab4 and ?1-adaptin in membrane recycling from endosomes

    doi: 10.1093/emboj/cdg257

    Figure Lengend Snippet: Fig. 2. Rabaptin-5α–γ-adaptin complex is localized on endosomes. HeLa cells were transfected with rabaptin-5α-pcDNA3.1His (left panels) or with rabaptin-5α and γ 1 -adaptin-pcDNA3 (right panels). Transfected cells were labelled for rabaptin-5α (green) and γ 1 -adaptin (red). Note the co-localization of rabaptin-5α and γ 1 -adaptin in transfected cells, and the distinct localization of γ 1 -adaptin in non-transfected cells (arrow) ( A and A ′). Cells were incubated with Alexa594-Tf for 60 min at 37°C and subsequently labelled with anti-Xpress antibody and Alexa488-conjugated IgG ( B and B ′). The TGN marker TGN46 does not relocate to enlarged endosomes. Transfected cells were labelled for rabaptin-5α (red) and TGN46 (green) ( C and C ′). Bar, 10 µm.

    Article Snippet: Rabaptin constructs were cloned in pcDNA3 and pcDNA3.1His (Invitrogen, Leek, The Netherlands).

    Techniques: Transfection, Incubation, Marker

    Fig. 6. Transfected rabaptin-5α delays Tf recycling. ( A ) HeLa cells were transfected with rabaptin-5α-pcDNA3.1His or with rabaptin-5α-pcDNA3.1His and γ 1 -adaptin-pcDNA3. The cells were incubated with 15 µg/ml Alexa-Tf at 16°C for 30 min, and subsequently chased at 37°C. Cells were fixed after different periods of time and stained for rabaptin-5α. Quantitation of the fraction of rabaptin-5α-positive endosomes containing Alexa488-Tf at 0, 10 and 50 min of chase. Error bars denote the standard deviation ( n = 10). ( B ) Rab4 and γ 1 -adaptin interaction domains in rabaptin-5α are required to retard Tf recycling. HeLa cells were transfected with rabaptin-5α(1–390), rabaptin-5α(301–592), rabaptin-5α(1–592) and rabaptin-5α. The cells were subjected to the pulse–chase protocol as above, fixed and labelled with anti-Xpress followed by Alexa488-labelled anti-mouse IgG. Note that only the rabaptin-5α truncation containing both rab4- and γ 1 -adaptin-binding sites retarded Tf recycling. Bar, 10 µm.

    Journal: The EMBO Journal

    Article Title: Rabaptin-5?/rabaptin-4 serves as a linker between rab4 and ?1-adaptin in membrane recycling from endosomes

    doi: 10.1093/emboj/cdg257

    Figure Lengend Snippet: Fig. 6. Transfected rabaptin-5α delays Tf recycling. ( A ) HeLa cells were transfected with rabaptin-5α-pcDNA3.1His or with rabaptin-5α-pcDNA3.1His and γ 1 -adaptin-pcDNA3. The cells were incubated with 15 µg/ml Alexa-Tf at 16°C for 30 min, and subsequently chased at 37°C. Cells were fixed after different periods of time and stained for rabaptin-5α. Quantitation of the fraction of rabaptin-5α-positive endosomes containing Alexa488-Tf at 0, 10 and 50 min of chase. Error bars denote the standard deviation ( n = 10). ( B ) Rab4 and γ 1 -adaptin interaction domains in rabaptin-5α are required to retard Tf recycling. HeLa cells were transfected with rabaptin-5α(1–390), rabaptin-5α(301–592), rabaptin-5α(1–592) and rabaptin-5α. The cells were subjected to the pulse–chase protocol as above, fixed and labelled with anti-Xpress followed by Alexa488-labelled anti-mouse IgG. Note that only the rabaptin-5α truncation containing both rab4- and γ 1 -adaptin-binding sites retarded Tf recycling. Bar, 10 µm.

    Article Snippet: Rabaptin constructs were cloned in pcDNA3 and pcDNA3.1His (Invitrogen, Leek, The Netherlands).

    Techniques: Transfection, Incubation, Staining, Quantitation Assay, Standard Deviation, Pulse Chase, Binding Assay

    Fig. 3. Rabaptin-5α and γ-adaptin co-localize to tubulo-vesicular membrane clusters. Ultrathin cryosections of HeLa cells transfected with rabaptin- 5α-pcDNA3.1His (A,C and E) or with rabaptin-5α and γ 1 -adaptin-pcDNA3 (B and D). Double labelling of rabaptin-5α (10 nm gold) and γ 1 -adaptin (15 nm gold). Rabaptin-5α is associated with clusters of vesicular tubular membranes, where it co-localized with endogenous ( A ) and overexpressed γ 1 -adaptin ( B ). The overall density and diameter of rabaptin-5α-positive membranes is reminiscent of recycling tubules. The dense cytosol between the membranes indicates the presence of high concentrations of cytosolic protein. Note that some of the membranes display a coating typical of the presence of clathrin (arrows in A and B). Double labelling of TGN46 (15 nm gold) and rabaptin-5α (10 nm gold) revealed that rabaptin-5α-positive membranes do not overlap with TGN membranes ( C ). Rabaptin-5α- (15 nm gold) positive membranes do not contain internalized BSA–5 nm gold. Arrows point to compartments that contain the endocytic marker 10 min after internalization ( D ). Double labelling of rabaptin-5α (15 nm gold) and clathrin (10 nm gold). Some of the membranes within or associated with rabaptin-5α-positive membranes also stained for clathrin (arrows). Note that the nearby endosomal vacuole (E) has a normal morphology ( E ). G = Golgi complex, L = lysosome. Bar, 200 nm.

    Journal: The EMBO Journal

    Article Title: Rabaptin-5?/rabaptin-4 serves as a linker between rab4 and ?1-adaptin in membrane recycling from endosomes

    doi: 10.1093/emboj/cdg257

    Figure Lengend Snippet: Fig. 3. Rabaptin-5α and γ-adaptin co-localize to tubulo-vesicular membrane clusters. Ultrathin cryosections of HeLa cells transfected with rabaptin- 5α-pcDNA3.1His (A,C and E) or with rabaptin-5α and γ 1 -adaptin-pcDNA3 (B and D). Double labelling of rabaptin-5α (10 nm gold) and γ 1 -adaptin (15 nm gold). Rabaptin-5α is associated with clusters of vesicular tubular membranes, where it co-localized with endogenous ( A ) and overexpressed γ 1 -adaptin ( B ). The overall density and diameter of rabaptin-5α-positive membranes is reminiscent of recycling tubules. The dense cytosol between the membranes indicates the presence of high concentrations of cytosolic protein. Note that some of the membranes display a coating typical of the presence of clathrin (arrows in A and B). Double labelling of TGN46 (15 nm gold) and rabaptin-5α (10 nm gold) revealed that rabaptin-5α-positive membranes do not overlap with TGN membranes ( C ). Rabaptin-5α- (15 nm gold) positive membranes do not contain internalized BSA–5 nm gold. Arrows point to compartments that contain the endocytic marker 10 min after internalization ( D ). Double labelling of rabaptin-5α (15 nm gold) and clathrin (10 nm gold). Some of the membranes within or associated with rabaptin-5α-positive membranes also stained for clathrin (arrows). Note that the nearby endosomal vacuole (E) has a normal morphology ( E ). G = Golgi complex, L = lysosome. Bar, 200 nm.

    Article Snippet: Rabaptin constructs were cloned in pcDNA3 and pcDNA3.1His (Invitrogen, Leek, The Netherlands).

    Techniques: Transfection, Marker, Staining

    Functional cell surface expression of CD1d1 on L cells transfected with cd1d1 cDNA from murine CD1 + hematopoietic tumor cells. ( A ) Murine L cell fibroblasts were transfected with the pcDNA3.1-neo vector alone or the vector containing the full-length cd1d1 cDNA generated from L5178Y-R, YAC-1, or 18.81 cells. The cells were stained with a PE-labeled anti-mouse CD1 mAb (filled histograms). A PE-conjugated rat IgG2b (open histograms) served as an isotype control. Analysis was by cytofluorography. The data are representative of two independent experiments. ( B ) L cells transfected with vector only or vector containing the WT cd1d1 cDNA (L-CD1d1WT) or that from L5178Y-R, YAC-1, or 18.81 cells were cocultured with the Vα14 + (canonical; DN32.D3; white bars) or Vα5 + (noncanonical; N37-1A12; black bars) NKT cell hybridomas for 24 h. Supernatants were harvested, and IL-2 production was measured by ELISA. The data shown are the mean of triplicate cultures ± SD.

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

    Article Title: Inhibition of glycolipid shedding rescues recognition of a CD1+ T cell lymphoma by natural killer T (NKT) cells

    doi: 10.1073/pnas.122636199

    Figure Lengend Snippet: Functional cell surface expression of CD1d1 on L cells transfected with cd1d1 cDNA from murine CD1 + hematopoietic tumor cells. ( A ) Murine L cell fibroblasts were transfected with the pcDNA3.1-neo vector alone or the vector containing the full-length cd1d1 cDNA generated from L5178Y-R, YAC-1, or 18.81 cells. The cells were stained with a PE-labeled anti-mouse CD1 mAb (filled histograms). A PE-conjugated rat IgG2b (open histograms) served as an isotype control. Analysis was by cytofluorography. The data are representative of two independent experiments. ( B ) L cells transfected with vector only or vector containing the WT cd1d1 cDNA (L-CD1d1WT) or that from L5178Y-R, YAC-1, or 18.81 cells were cocultured with the Vα14 + (canonical; DN32.D3; white bars) or Vα5 + (noncanonical; N37-1A12; black bars) NKT cell hybridomas for 24 h. Supernatants were harvested, and IL-2 production was measured by ELISA. The data shown are the mean of triplicate cultures ± SD.

    Article Snippet: In some experiments, L cells transfected with vector alone or the WT cd1d1 cDNA in pcDNA3.1-neo (Invitrogen), generated in our laboratory as above, were used.

    Techniques: Functional Assay, Expressing, Transfection, Plasmid Preparation, Generated, Staining, Labeling, Enzyme-linked Immunosorbent Assay

    Carnosic acid inhibits LX2 activation by inhibiting HMGB1. LX2 cells were randomly divided into three groups: pcDNA3.1-control, pcDNA3.1-control + CA (20 μM), and pcDNA3.1-HMGB1 + CA (20 μM). After transfection with the plasmid for 24 h, the cells were treated with CA for 12 h, and protein was then extracted. The protein expression levels of α-SMA, HMGB1, TLR4 and nuclear NF-κB p65 in LX2 cells were detected by western blot ( n = 3). The data are presented as the means ± SD. ∗∗ P

    Journal: Frontiers in Pharmacology

    Article Title: Carnosic Acid Alleviates BDL-Induced Liver Fibrosis through miR-29b-3p-Mediated Inhibition of the High-Mobility Group Box 1/Toll-Like Receptor 4 Signaling Pathway in Rats

    doi: 10.3389/fphar.2017.00976

    Figure Lengend Snippet: Carnosic acid inhibits LX2 activation by inhibiting HMGB1. LX2 cells were randomly divided into three groups: pcDNA3.1-control, pcDNA3.1-control + CA (20 μM), and pcDNA3.1-HMGB1 + CA (20 μM). After transfection with the plasmid for 24 h, the cells were treated with CA for 12 h, and protein was then extracted. The protein expression levels of α-SMA, HMGB1, TLR4 and nuclear NF-κB p65 in LX2 cells were detected by western blot ( n = 3). The data are presented as the means ± SD. ∗∗ P

    Article Snippet: Transfected experiments were performed using 2 μg pcDNA3.1/HMGB1, 50 nM mimic-miR-29b-3p, 50 nM mimic-miR-300 or 50 nM antagomiR-29b-3p (GenePharma) and Lipofectamine 3000 (Invitrogen, United States) according to the manufacturer’s instructions. pcDNA3.1 (GenePharma) and a random RNA duplex (GenePharma) was used as negative control.

    Techniques: Activation Assay, Transfection, Plasmid Preparation, Expressing, Western Blot

    PRRX1 promotes myoblast proliferation. (A,C) The overexpression efficiency of the pcDNA3.1 with PRRX1 in CPMs and QM-7 cells. (B,D) The interference efficiency of PRRX1 SiRNA in CPMs and QM-7 cells. (E,G) Cell cycle after overexpression of PRRX1 in CPMs and QM-7 cells. (F,H) Cell cycle after interference of PRRX1 in CPMs and QM-7 cells. (I–L) Cell growth curves were measured following the transfection of PRRX1 overexpression vector and SiRNA in CPMs and QM-7 cells. (M,O) Evaluation of the proliferation of PRRX1 -transfected CPMs and QM-7 cells by EdU incorporation, EdU-stained cell proportions were counted. (N,P) Evaluation of the proliferation of PRRX1 SiRNA-transfected CPMs and QM-7 cells by EdU incorporation, EdU-stained cell proportions were counted. The results of all groups are shown as mean ± S.E.M., and the data represent three independent assessment methods. Statistical significance of the mean difference was assessed using an unpaired two-sample t -tests ( ∗ p

    Journal: Frontiers in Genetics

    Article Title: gga-mir-133a-3p Regulates Myoblasts Proliferation and Differentiation by Targeting PRRX1

    doi: 10.3389/fgene.2018.00577

    Figure Lengend Snippet: PRRX1 promotes myoblast proliferation. (A,C) The overexpression efficiency of the pcDNA3.1 with PRRX1 in CPMs and QM-7 cells. (B,D) The interference efficiency of PRRX1 SiRNA in CPMs and QM-7 cells. (E,G) Cell cycle after overexpression of PRRX1 in CPMs and QM-7 cells. (F,H) Cell cycle after interference of PRRX1 in CPMs and QM-7 cells. (I–L) Cell growth curves were measured following the transfection of PRRX1 overexpression vector and SiRNA in CPMs and QM-7 cells. (M,O) Evaluation of the proliferation of PRRX1 -transfected CPMs and QM-7 cells by EdU incorporation, EdU-stained cell proportions were counted. (N,P) Evaluation of the proliferation of PRRX1 SiRNA-transfected CPMs and QM-7 cells by EdU incorporation, EdU-stained cell proportions were counted. The results of all groups are shown as mean ± S.E.M., and the data represent three independent assessment methods. Statistical significance of the mean difference was assessed using an unpaired two-sample t -tests ( ∗ p

    Article Snippet: To evaluate the roles of PRRX1 in the biological action of gga-mir-133a-3p, we conducted a recovery validation experiment of gga-mir-133a-3p function by co-transfecting with: gga-mir-133a-3p mimic and pcDNA3.1, mimic NC and pcDNA3.1, gga-mir-133a-3p mimic and pcDNA3.1+ PRRX1 to test their effects on myoblast proliferation and differentiation.

    Techniques: Over Expression, Transfection, Plasmid Preparation, Staining

    Elevated expression of PLD1 suppresses DNA damage-induced increases in the level of p53 in cells where PLD provides survival signals. (A) 3Y1 c-Src and 3Y1 c-Src ). (B) 3Y1 and 3Y1-P1 cells were treated with CPT, ADR, and PonA, and p53 levels were determined as described above. (C) MCF-7 cells stably transfected with pcDNA3.1(−)-PLD2 or the parental pcDNA3.1(−) vector were treated with either CPT or ADR, and p53 levels were determined as described above. (D) The relative levels of PLD2 protein determined by Western blot and PLD activity in the MCF-7 cells stably expressing PLD2 and transfected with the parental empty vector are shown. The data shown are representative of results obtained at least three times.

    Journal: Molecular and Cellular Biology

    Article Title: Phospholipase D Elevates the Level of MDM2 and Suppresses DNA Damage-Induced Increases in p53

    doi: 10.1128/MCB.24.13.5677-5686.2004

    Figure Lengend Snippet: Elevated expression of PLD1 suppresses DNA damage-induced increases in the level of p53 in cells where PLD provides survival signals. (A) 3Y1 c-Src and 3Y1 c-Src ). (B) 3Y1 and 3Y1-P1 cells were treated with CPT, ADR, and PonA, and p53 levels were determined as described above. (C) MCF-7 cells stably transfected with pcDNA3.1(−)-PLD2 or the parental pcDNA3.1(−) vector were treated with either CPT or ADR, and p53 levels were determined as described above. (D) The relative levels of PLD2 protein determined by Western blot and PLD activity in the MCF-7 cells stably expressing PLD2 and transfected with the parental empty vector are shown. The data shown are representative of results obtained at least three times.

    Article Snippet: The human PLD2 gene ( ) was excised from pBluescript-SK-hPLD2 ( ) with NotI and HindIII and was ligated into the polylinker region of the pcDNA3.1() expression plasmid (Stratagene) which was cut with NotI and HindIII.

    Techniques: Expressing, Cycling Probe Technology, Stable Transfection, Transfection, Plasmid Preparation, Western Blot, Activity Assay

    Effects of transfection on Sirtuin 1 (Sirt1) expression. BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or shRNA against Sirt1 respectively, and then the transfection efficiency was tested by RT-PCR ( A ) and Western blot analysis ( B ). GAPDH was used as an internal control. * p

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Sirtuin 1 (Sirt1) Overexpression in BaF3 Cells Contributes to Cell Proliferation Promotion, Apoptosis Resistance and Pro-Inflammatory Cytokine Production

    doi: 10.12659/MSM.900754

    Figure Lengend Snippet: Effects of transfection on Sirtuin 1 (Sirt1) expression. BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or shRNA against Sirt1 respectively, and then the transfection efficiency was tested by RT-PCR ( A ) and Western blot analysis ( B ). GAPDH was used as an internal control. * p

    Article Snippet: Effects of transfection on Sirt1 expression BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or shRNA against Sirt1 respectively, and then the transfection efficiency was tested by RT-PCR and Western blot analysis ( ).

    Techniques: Transfection, Expressing, shRNA, Reverse Transcription Polymerase Chain Reaction, Western Blot

    Nuclear factor-kappa B (NF-κB) pathway was involved in the effects of Sirtuin 1 (Sirt1) on NaF3 cells. After BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or Sirt1-shRNA, the protein expressions of p/t-inhibitory subunit of NF-κB (IκBα), p/t-p65, and B-Cell CLL/Lymphoma 3 (Bcl-3) were detected by Western blot analysis ( A, B ). GAPDH was used as an internal control. * p

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Sirtuin 1 (Sirt1) Overexpression in BaF3 Cells Contributes to Cell Proliferation Promotion, Apoptosis Resistance and Pro-Inflammatory Cytokine Production

    doi: 10.12659/MSM.900754

    Figure Lengend Snippet: Nuclear factor-kappa B (NF-κB) pathway was involved in the effects of Sirtuin 1 (Sirt1) on NaF3 cells. After BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or Sirt1-shRNA, the protein expressions of p/t-inhibitory subunit of NF-κB (IκBα), p/t-p65, and B-Cell CLL/Lymphoma 3 (Bcl-3) were detected by Western blot analysis ( A, B ). GAPDH was used as an internal control. * p

    Article Snippet: Effects of transfection on Sirt1 expression BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or shRNA against Sirt1 respectively, and then the transfection efficiency was tested by RT-PCR and Western blot analysis ( ).

    Techniques: Transfection, shRNA, Western Blot

    Overexpression of Sirtuin 1 (Sirt1) upregulated the expression of inflammatory cytokines and downregulated the expression of p53. Cells were first transfected with empty pcDNA3.1 or pc-Sirt1, and then the mRNA level expressions of pro-inflammatory cytokines ( A ) and p53 ( B ) in transfected cells were determined by RT-PCR. * p

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Sirtuin 1 (Sirt1) Overexpression in BaF3 Cells Contributes to Cell Proliferation Promotion, Apoptosis Resistance and Pro-Inflammatory Cytokine Production

    doi: 10.12659/MSM.900754

    Figure Lengend Snippet: Overexpression of Sirtuin 1 (Sirt1) upregulated the expression of inflammatory cytokines and downregulated the expression of p53. Cells were first transfected with empty pcDNA3.1 or pc-Sirt1, and then the mRNA level expressions of pro-inflammatory cytokines ( A ) and p53 ( B ) in transfected cells were determined by RT-PCR. * p

    Article Snippet: Effects of transfection on Sirt1 expression BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or shRNA against Sirt1 respectively, and then the transfection efficiency was tested by RT-PCR and Western blot analysis ( ).

    Techniques: Over Expression, Expressing, Transfection, Reverse Transcription Polymerase Chain Reaction

    Overexpression of Sirtuin 1 (Sirt1) increased cell viability and suppressed apoptosis. After BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or Sirt1-shRNA, cell viability was measured by MTT ( A ) and apoptosis was determined by flow cytometry ( B ). * p

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Sirtuin 1 (Sirt1) Overexpression in BaF3 Cells Contributes to Cell Proliferation Promotion, Apoptosis Resistance and Pro-Inflammatory Cytokine Production

    doi: 10.12659/MSM.900754

    Figure Lengend Snippet: Overexpression of Sirtuin 1 (Sirt1) increased cell viability and suppressed apoptosis. After BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or Sirt1-shRNA, cell viability was measured by MTT ( A ) and apoptosis was determined by flow cytometry ( B ). * p

    Article Snippet: Effects of transfection on Sirt1 expression BaF3 cells were transfected with empty pcDNA3.1, pc-Sirt1, scrambled shRNA, or shRNA against Sirt1 respectively, and then the transfection efficiency was tested by RT-PCR and Western blot analysis ( ).

    Techniques: Over Expression, Transfection, shRNA, MTT Assay, Flow Cytometry, Cytometry

    Reciprocal proliferation effects of GLI1 and FOXS1; FOXS1 inhibits GLI1 activity. EdU incorporation assay of Rh36 cells (A) and Daoy cells (B) following transfection with siRNA combinations of siControl + siControl, siControl + siGLI1, siControl + siFOXS1, or siGLI1 + siFOXS1. Data from one representative experiment are shown in the histogram. EdU incorporation assay of Daoy cells (C) following transfection/transduction with siControl + Ad‐Vector, siControl + Ad‐GLI1, siFOXS1 + Ad‐Vector, or siFOXS1 + Ad‐GLI1. Adenoviruses were added 6 h after siRNA transfection. Data from one representative experiment are shown in the histogram. (D) A schematic diagram of the proposed model for the FOXS1/GLI1 feedback loop. The transcription factor GLI1 positively regulates the expression of the FOXS1 transcription factor, while FOXS1 negatively regulates GLI1. GLI1 promotes cell proliferation, whereas FOXS1 inhibits cell proliferation. (E) FOXS1 expression reduces GLI1 transcriptional activity. HEK293A cells were co‐transfected with pcDNA3.1 vector (pcDNA), pGL3 basic luciferase empty vector (pGL3), pCMV‐GLI1‐flag (pGLI1), or pcDNA3.1‐FOXS1 (pFOXS1), together with the reporter plasmid 12xGLIBS and the control plasmid Renilla. Data from one representative experiment are shown. Error bars indicate standard deviation. Statistical significant, ## P

    Journal: Molecular Oncology

    Article Title: Identification of novel GLI1 target genes and regulatory circuits in human cancer cells

    doi: 10.1002/1878-0261.12366

    Figure Lengend Snippet: Reciprocal proliferation effects of GLI1 and FOXS1; FOXS1 inhibits GLI1 activity. EdU incorporation assay of Rh36 cells (A) and Daoy cells (B) following transfection with siRNA combinations of siControl + siControl, siControl + siGLI1, siControl + siFOXS1, or siGLI1 + siFOXS1. Data from one representative experiment are shown in the histogram. EdU incorporation assay of Daoy cells (C) following transfection/transduction with siControl + Ad‐Vector, siControl + Ad‐GLI1, siFOXS1 + Ad‐Vector, or siFOXS1 + Ad‐GLI1. Adenoviruses were added 6 h after siRNA transfection. Data from one representative experiment are shown in the histogram. (D) A schematic diagram of the proposed model for the FOXS1/GLI1 feedback loop. The transcription factor GLI1 positively regulates the expression of the FOXS1 transcription factor, while FOXS1 negatively regulates GLI1. GLI1 promotes cell proliferation, whereas FOXS1 inhibits cell proliferation. (E) FOXS1 expression reduces GLI1 transcriptional activity. HEK293A cells were co‐transfected with pcDNA3.1 vector (pcDNA), pGL3 basic luciferase empty vector (pGL3), pCMV‐GLI1‐flag (pGLI1), or pcDNA3.1‐FOXS1 (pFOXS1), together with the reporter plasmid 12xGLIBS and the control plasmid Renilla. Data from one representative experiment are shown. Error bars indicate standard deviation. Statistical significant, ## P

    Article Snippet: HEK293A cells were seeded in 24‐well plates and transfected with 200 ng of 12xGLI binding site luciferase reporter plasmid (12xGLIBS) (Mao et al ., ) and 10 ng of Renilla control reporter plasmid, together with pcDNA3.1 vector, pGL3 basic luciferase empty vector, the pCMV‐GLI1‐flag expression construct (pGLI1), and/or pcDNA3.1‐FOXS1 ( ; GeneScript, Piscatway, NJ, USA) using Lipofectamine 3000 (Invitrogen).

    Techniques: Activity Assay, Transfection, Transduction, Plasmid Preparation, Expressing, Luciferase, Standard Deviation

    Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the pcDNA3.1 expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is

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

    Article Title: The molecular dynamics of long noncoding RNA control of transcription in PTEN and its pseudogene

    doi: 10.1073/pnas.1621490114

    Figure Lengend Snippet: Characterization of the PTENpg1 asRNA F4R1 variant functional domain. ( A ) Various truncations of F4R1 were developed and cloned into the pcDNA3.1 expression vector and screened for binding to the PTEN promoter. M-Fold analysis of the predicted RNAs is

    Article Snippet: Various truncated versions of PTEN alpha exon 1 ( ) and mutants of F4R1 ( ) were generated to be expressed from the CMV promoter in the context of pcDNA3.1 (Genewiz).

    Techniques: Variant Assay, Functional Assay, Clone Assay, Expressing, Plasmid Preparation, Binding Assay

    Involvement of matrix metalloproteinases (MMPs) and E-cadherin in Src-promoted keratinocyte migration. (A and B) Western blot analysis of MMP-2, MMP-9 and E-cadherin expression in keratinocytes following transfection with overexpressing Src [pcDNA3.1(+)-Src] or silencing Src (Src-siRNA), or the corresponding controls. Controls used were untransfected cells (control) and pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA. Actin was used as a loading control. Bars represent the means ± SEM of n=4 tissue samples. * P

    Journal: International Journal of Molecular Medicine

    Article Title: Src promotes cutaneous wound healing by regulating MMP-2 through the ERK pathway

    doi: 10.3892/ijmm.2016.2472

    Figure Lengend Snippet: Involvement of matrix metalloproteinases (MMPs) and E-cadherin in Src-promoted keratinocyte migration. (A and B) Western blot analysis of MMP-2, MMP-9 and E-cadherin expression in keratinocytes following transfection with overexpressing Src [pcDNA3.1(+)-Src] or silencing Src (Src-siRNA), or the corresponding controls. Controls used were untransfected cells (control) and pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA. Actin was used as a loading control. Bars represent the means ± SEM of n=4 tissue samples. * P

    Article Snippet: Primary keratinocytes were divided into the following groups: control, pcDNA3.1(+), pcDNA3.1(+)-Src, mock and also the Src-siRNA transfected groups.

    Techniques: Migration, Western Blot, Expressing, Transfection

    Western blot analysis of mitogen-activated protein kinase (MAPK) in keratinocytes after Src silencing or overexpression. Protein expression of (A) ERK, (B) JNK and (C) p38 after overexpressing Src [pcDNA3.1(+)-Src] or silencing Src expression (Src-siRNA). pcDNA3.1(+) and mock were used as negative controls; mock, cells transfected with scrambled siRNA. Bars represent the means ± SEM; n=4. ** P

    Journal: International Journal of Molecular Medicine

    Article Title: Src promotes cutaneous wound healing by regulating MMP-2 through the ERK pathway

    doi: 10.3892/ijmm.2016.2472

    Figure Lengend Snippet: Western blot analysis of mitogen-activated protein kinase (MAPK) in keratinocytes after Src silencing or overexpression. Protein expression of (A) ERK, (B) JNK and (C) p38 after overexpressing Src [pcDNA3.1(+)-Src] or silencing Src expression (Src-siRNA). pcDNA3.1(+) and mock were used as negative controls; mock, cells transfected with scrambled siRNA. Bars represent the means ± SEM; n=4. ** P

    Article Snippet: Primary keratinocytes were divided into the following groups: control, pcDNA3.1(+), pcDNA3.1(+)-Src, mock and also the Src-siRNA transfected groups.

    Techniques: Western Blot, Over Expression, Expressing, Transfection

    Effect of Src on keratinocyte migration in vitro . (A) Keratinocytes were transfected to overexpress Src [pcDNA3.1(+)-Src] or silence Src expression (Src-siRNA). Following 1 h of mitomycin C treatment, the cells were scratch-wounded with a micropipette tip (200 µ l). Black dotted lines indicate the wound borders at the beginning of the assay and were recorded at 0, 12 and 24 h post-scratching. Scale bar, 100 µ M. (B) Relative scratch gap was calculated as the ratio of the remaining scratch gap at the given time point and the original gap at 0 h. (C) Flow cytometric analysis showing the effect of Src on cell cycle distribution. Numbers of cells at G1, G2 and S phases were counted and the percentage was calculated. Controls used were untransfected cells (control), pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA sequence. Bars represent the means ± SEM; n=4 tissue samples. * P

    Journal: International Journal of Molecular Medicine

    Article Title: Src promotes cutaneous wound healing by regulating MMP-2 through the ERK pathway

    doi: 10.3892/ijmm.2016.2472

    Figure Lengend Snippet: Effect of Src on keratinocyte migration in vitro . (A) Keratinocytes were transfected to overexpress Src [pcDNA3.1(+)-Src] or silence Src expression (Src-siRNA). Following 1 h of mitomycin C treatment, the cells were scratch-wounded with a micropipette tip (200 µ l). Black dotted lines indicate the wound borders at the beginning of the assay and were recorded at 0, 12 and 24 h post-scratching. Scale bar, 100 µ M. (B) Relative scratch gap was calculated as the ratio of the remaining scratch gap at the given time point and the original gap at 0 h. (C) Flow cytometric analysis showing the effect of Src on cell cycle distribution. Numbers of cells at G1, G2 and S phases were counted and the percentage was calculated. Controls used were untransfected cells (control), pcDNA3.1(+) and mock; mock, cells transfected with scrambled siRNA sequence. Bars represent the means ± SEM; n=4 tissue samples. * P

    Article Snippet: Primary keratinocytes were divided into the following groups: control, pcDNA3.1(+), pcDNA3.1(+)-Src, mock and also the Src-siRNA transfected groups.

    Techniques: Migration, In Vitro, Transfection, Expressing, Flow Cytometry, Sequencing

    Western blot analysis of Src expression in keratinocytes following transfection. (A) Keratinocytes were transfected with pcDNA3.1(+)-Src for overexpressing Src and (B) Src-siRNA was used for silencing Src. Controls used were untransfected cells (control), pcDNA3.1(+) and mock. Mock, cells transfected with scrambled siRNA. Bars represent the means ± SEM; n=4 tissue samples. ** P

    Journal: International Journal of Molecular Medicine

    Article Title: Src promotes cutaneous wound healing by regulating MMP-2 through the ERK pathway

    doi: 10.3892/ijmm.2016.2472

    Figure Lengend Snippet: Western blot analysis of Src expression in keratinocytes following transfection. (A) Keratinocytes were transfected with pcDNA3.1(+)-Src for overexpressing Src and (B) Src-siRNA was used for silencing Src. Controls used were untransfected cells (control), pcDNA3.1(+) and mock. Mock, cells transfected with scrambled siRNA. Bars represent the means ± SEM; n=4 tissue samples. ** P

    Article Snippet: Primary keratinocytes were divided into the following groups: control, pcDNA3.1(+), pcDNA3.1(+)-Src, mock and also the Src-siRNA transfected groups.

    Techniques: Western Blot, Expressing, Transfection

    Effect of Src on rat skin wound healing. (A) Full-thickness excision wounds were made on the back of SD rats at day(d) 0. The process of wound healing was digitally photographed on days 0, 7, 14 and 21 post-wounding in the control, pcDNA3.1(+), pcDNA3.1(+)-Src, mock and Src-siRNA transfected groups. Ruler notches, 1 mm. (B) The relative wound area was calculated as the ratio of the residual wound area at the given time-point and the original wound area on day 0. Control, saline; pcDNA3.1(+) and mock were used as negative controls; mock, cells transfected with scrambled siRNA. Bars represent the means ± SEM; n=10 rats/group. * P

    Journal: International Journal of Molecular Medicine

    Article Title: Src promotes cutaneous wound healing by regulating MMP-2 through the ERK pathway

    doi: 10.3892/ijmm.2016.2472

    Figure Lengend Snippet: Effect of Src on rat skin wound healing. (A) Full-thickness excision wounds were made on the back of SD rats at day(d) 0. The process of wound healing was digitally photographed on days 0, 7, 14 and 21 post-wounding in the control, pcDNA3.1(+), pcDNA3.1(+)-Src, mock and Src-siRNA transfected groups. Ruler notches, 1 mm. (B) The relative wound area was calculated as the ratio of the residual wound area at the given time-point and the original wound area on day 0. Control, saline; pcDNA3.1(+) and mock were used as negative controls; mock, cells transfected with scrambled siRNA. Bars represent the means ± SEM; n=10 rats/group. * P

    Article Snippet: Primary keratinocytes were divided into the following groups: control, pcDNA3.1(+), pcDNA3.1(+)-Src, mock and also the Src-siRNA transfected groups.

    Techniques: Transfection

    WDR5 bound to SMC-marker gene promoter loci. A , stable cell lines containing either empty or Myc-WDR5 expression plasmid had comparable differentiation potential to the original A404 cell line. Control stable , stable A404 cell line containing empty pcDNA3.1

    Journal: The Journal of Biological Chemistry

    Article Title: WD Repeat-containing Protein 5, a Ubiquitously Expressed Histone Methyltransferase Adaptor Protein, Regulates Smooth Muscle Cell-selective Gene Activation through Interaction with Pituitary Homeobox 2 *

    doi: 10.1074/jbc.M111.233098

    Figure Lengend Snippet: WDR5 bound to SMC-marker gene promoter loci. A , stable cell lines containing either empty or Myc-WDR5 expression plasmid had comparable differentiation potential to the original A404 cell line. Control stable , stable A404 cell line containing empty pcDNA3.1

    Article Snippet: An expression plasmid for Myc-tagged WDR5 was constructed by inserting WDR5 cDNA into pcDNA3.1-Myc/His (+) (Invitrogen).

    Techniques: Marker, Stable Transfection, Expressing, Plasmid Preparation