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Thermo Fisher pcdna 4
Pcdna 4, 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
https://www.bioz.com/result/pcdna 4/product/Thermo Fisher
Average 85 stars, based on 3 article reviews
Price from $9.99 to $1999.99
pcdna 4 - by Bioz Stars, 2020-09
85/100 stars

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Stable Transfection:

Article Title: Live-cell p53 single-molecule binding is modulated by C-terminal acetylation and correlates with transcriptional activity
Article Snippet: .. Stable cell lines generation The plasmids encoding for HaloTag-p53wt and HaloTag-p53mSB under the control of a Tet-dependent promoter were generated by digestion of the CMVd1-HaloTag-p53 and CMVd1-HaloTag-p53mSB plasmids with HindIII and XbaI restriction enzymes, and subsequent ligation into the pCDNA-4/TO vector (Invitrogen, Thermo-Fisher, Waltham, MA, USA). .. Each of the plasmids was co-transfected with the pCDNA-6 plasmid (Thermo-Fisher) (responsible for the constitutive expression of the Tet-repressor) into lung carcinoma H1299 cells (ATCC, LGC Standards S.r.l., Milan, Italy) using Lipofectamine LTX (Thermo-Fisher) according to the manufacturer’s instructions.

Ligation:

Article Title: Live-cell p53 single-molecule binding is modulated by C-terminal acetylation and correlates with transcriptional activity
Article Snippet: .. Stable cell lines generation The plasmids encoding for HaloTag-p53wt and HaloTag-p53mSB under the control of a Tet-dependent promoter were generated by digestion of the CMVd1-HaloTag-p53 and CMVd1-HaloTag-p53mSB plasmids with HindIII and XbaI restriction enzymes, and subsequent ligation into the pCDNA-4/TO vector (Invitrogen, Thermo-Fisher, Waltham, MA, USA). .. Each of the plasmids was co-transfected with the pCDNA-6 plasmid (Thermo-Fisher) (responsible for the constitutive expression of the Tet-repressor) into lung carcinoma H1299 cells (ATCC, LGC Standards S.r.l., Milan, Italy) using Lipofectamine LTX (Thermo-Fisher) according to the manufacturer’s instructions.

Construct:

Article Title: Chemokine Signaling Specificity: Essential Role for the N-Terminal Domain of Chemokine Receptors †
Article Snippet: .. Finally, these constructs were subcloned into the pcDNA-4/TO expression plasmid (Invitrogen, Carlsbad, CA). .. All constructs were verified by nucleotide sequencing (UTMB Protein Chemistry Core Facility).

Generated:

Article Title: Live-cell p53 single-molecule binding is modulated by C-terminal acetylation and correlates with transcriptional activity
Article Snippet: .. Stable cell lines generation The plasmids encoding for HaloTag-p53wt and HaloTag-p53mSB under the control of a Tet-dependent promoter were generated by digestion of the CMVd1-HaloTag-p53 and CMVd1-HaloTag-p53mSB plasmids with HindIII and XbaI restriction enzymes, and subsequent ligation into the pCDNA-4/TO vector (Invitrogen, Thermo-Fisher, Waltham, MA, USA). .. Each of the plasmids was co-transfected with the pCDNA-6 plasmid (Thermo-Fisher) (responsible for the constitutive expression of the Tet-repressor) into lung carcinoma H1299 cells (ATCC, LGC Standards S.r.l., Milan, Italy) using Lipofectamine LTX (Thermo-Fisher) according to the manufacturer’s instructions.

Article Title: Identification of a MAD2-binding protein, CMT2, and its role in mitosis
Article Snippet: .. HeLa T-Rex cells that express CMT2 protein were generated by transfecting them with pcDNA 4 (Invitrogen) plasmid carrying CMT2 gene. .. Zeocin-resistant foci were selected and purified using the dilution method.

Expressing:

Article Title: Chemokine Signaling Specificity: Essential Role for the N-Terminal Domain of Chemokine Receptors †
Article Snippet: .. Finally, these constructs were subcloned into the pcDNA-4/TO expression plasmid (Invitrogen, Carlsbad, CA). .. All constructs were verified by nucleotide sequencing (UTMB Protein Chemistry Core Facility).

Plasmid Preparation:

Article Title: Live-cell p53 single-molecule binding is modulated by C-terminal acetylation and correlates with transcriptional activity
Article Snippet: .. Stable cell lines generation The plasmids encoding for HaloTag-p53wt and HaloTag-p53mSB under the control of a Tet-dependent promoter were generated by digestion of the CMVd1-HaloTag-p53 and CMVd1-HaloTag-p53mSB plasmids with HindIII and XbaI restriction enzymes, and subsequent ligation into the pCDNA-4/TO vector (Invitrogen, Thermo-Fisher, Waltham, MA, USA). .. Each of the plasmids was co-transfected with the pCDNA-6 plasmid (Thermo-Fisher) (responsible for the constitutive expression of the Tet-repressor) into lung carcinoma H1299 cells (ATCC, LGC Standards S.r.l., Milan, Italy) using Lipofectamine LTX (Thermo-Fisher) according to the manufacturer’s instructions.

Article Title: Chemokine Signaling Specificity: Essential Role for the N-Terminal Domain of Chemokine Receptors †
Article Snippet: .. Finally, these constructs were subcloned into the pcDNA-4/TO expression plasmid (Invitrogen, Carlsbad, CA). .. All constructs were verified by nucleotide sequencing (UTMB Protein Chemistry Core Facility).

Article Title: Identification of a MAD2-binding protein, CMT2, and its role in mitosis
Article Snippet: .. HeLa T-Rex cells that express CMT2 protein were generated by transfecting them with pcDNA 4 (Invitrogen) plasmid carrying CMT2 gene. .. Zeocin-resistant foci were selected and purified using the dilution method.

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  • 99
    Thermo Fisher t rex mammalian inducible vector pcdna4 to mychisc
    Cellular level of cyclin A1 influences paclitaxel response in ovarian cancer cells Growth inhibition of (A) TOV112D-CCNA1 cancer cells, (B) the parental TOV112D cell line, and (C) <t>TOV112D-pCDNA4</t> cells that harbor mock control vector, <t>pcDNA4/TO/mycHisC,</t> by paclitaxel as measured by MTT assay. Cells were either incubated in medium containing 1μg/ml tetracycline, or without any tetracycline, respectively. In (D), TOV112D-CCNA1 cells were induced by tetracycline incubation, transfected with either cyclin A1-specific siRNA, or control siRNA (luciferase-specific), respectively. After 48 hours of paclitaxel incubation, MTT assays were performed. All the data shown are averages of triplicates of data from three independent experiments.
    T Rex Mammalian Inducible Vector Pcdna4 To Mychisc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t rex mammalian inducible vector pcdna4 to mychisc/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    t rex mammalian inducible vector pcdna4 to mychisc - by Bioz Stars, 2020-09
    99/100 stars
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    92
    Thermo Fisher pcdna4 to
    Presence of PML-NBs leads to hyperSUMOylation of IE1. (A) HEK293T cells were co-transfected at a ratio of 1:1:1 with pCMV2N3T-HA-SUMO-1: pDEST-MYC-PML-I: <t>pcDNA4/TO</t> or pcDNA4/TO-IE1B plasmids. After 48h cells were collected and lysed in RIPA buffer. A portion (10%) of the lysate was used to monitor protein expression (input). The remaining portion of the lysate was used for IE1 immunoprecipitation. IE1-SUMO-1 conjugates were detected using anti-HA antibodies. In presence of PML, SUMOylation of IE1 is enhance and that is shown by the presence of a second IE1-SUMO-1 band. (B) Illustration representing possible SUMOylation states of protein. Once mature, a SUMO protein is charged on a E1 activating enzyme and then transferred to a E2 conjugating enzyme. The SUMO-E2 complex can directly SUMOylate a protein on its acceptor lysine (K). Following conjugation to E2, the SUMO-E2 complex can be bound by a E3 SUMO ligase that will facilitate the discharge of the SUMO protein on the acceptor site of a target. The presence of a E3 SUMO ligase can influence or help reach those different levels of SUMOylation where polySUMOylation is realized by the presence of SUMO-2/3 paralogues that possess SUMO acceptor sites. (C) Scheme illustrating major domains and modification sites of PML protein. Leucine at position 73 allows the attachment of monomers of PML to form a tetramer, essential for the formation of PML-NBs [ 44 ]. (D) IF images representing the different PML-I phenotypes after transfection of PML-I WT or PML-I RING domain mutant (PML-I:L73E) in U2OS PML -/- cells. PML RING mutant lost the ability to form nuclear bodies. (E) HEK293T cells were co-transfected at a ratio of 1:1:1 with pCMV2N3T-HA-SUMO-1/SUMO-2 or SUMO-3: pCMV-MYC-PML-I: pcDNA4/TO or pcDNA4/TO-IE1B plasmids. Cells were collected and processed as in (A). Enhancement of SUMOylation of IE1 is PML-I WT and SUMO-1 dependent. These results are the representation of three independent experiments (n = 3).
    Pcdna4 To, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pcdna4 to/product/Thermo Fisher
    Average 92 stars, based on 83 article reviews
    Price from $9.99 to $1999.99
    pcdna4 to - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    91
    Thermo Fisher pcdna capn4
    Overexpression of calpain small subunit 1 <t>(Capn4)</t> reversed the inhibitory effect of miR-124 on the Wnt/β-catenin signaling pathway. HONE1 and CNE2 cells were transfected with miR-124 or co-transfected with miR-124 and <t>pcDNA-Capn4</t> ( A and B ). Western blot analysis revealed that Capn4 overexpression reversed the decreased β-catenin, cyclin D1, and c-Myc protein levels caused by the overexpression of miR-124 in HONE1 and CNE2 cells. Data are shown as mean ± standard deviation (n=3). * P
    Pcdna Capn4, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pcdna capn4/product/Thermo Fisher
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pcdna capn4 - by Bioz Stars, 2020-09
    91/100 stars
      Buy from Supplier

    Image Search Results


    Cellular level of cyclin A1 influences paclitaxel response in ovarian cancer cells Growth inhibition of (A) TOV112D-CCNA1 cancer cells, (B) the parental TOV112D cell line, and (C) TOV112D-pCDNA4 cells that harbor mock control vector, pcDNA4/TO/mycHisC, by paclitaxel as measured by MTT assay. Cells were either incubated in medium containing 1μg/ml tetracycline, or without any tetracycline, respectively. In (D), TOV112D-CCNA1 cells were induced by tetracycline incubation, transfected with either cyclin A1-specific siRNA, or control siRNA (luciferase-specific), respectively. After 48 hours of paclitaxel incubation, MTT assays were performed. All the data shown are averages of triplicates of data from three independent experiments.

    Journal: European journal of cancer (Oxford, England : 1990)

    Article Title: CyclinA1 Expression and Paclitaxel Resistance in Human Ovarian Cancer Cells

    doi: 10.1016/j.ejca.2016.08.007

    Figure Lengend Snippet: Cellular level of cyclin A1 influences paclitaxel response in ovarian cancer cells Growth inhibition of (A) TOV112D-CCNA1 cancer cells, (B) the parental TOV112D cell line, and (C) TOV112D-pCDNA4 cells that harbor mock control vector, pcDNA4/TO/mycHisC, by paclitaxel as measured by MTT assay. Cells were either incubated in medium containing 1μg/ml tetracycline, or without any tetracycline, respectively. In (D), TOV112D-CCNA1 cells were induced by tetracycline incubation, transfected with either cyclin A1-specific siRNA, or control siRNA (luciferase-specific), respectively. After 48 hours of paclitaxel incubation, MTT assays were performed. All the data shown are averages of triplicates of data from three independent experiments.

    Article Snippet: The cDNA was then restricted from the vector by Eco RI digestion and cloned into T-REx mammalian inducible vector pcDNA4/TO/mycHisC (Thermo Fisher Scientific, MA, USA) at the Eco RI site.

    Techniques: Inhibition, Plasmid Preparation, MTT Assay, Incubation, Transfection, Luciferase

    Presence of PML-NBs leads to hyperSUMOylation of IE1. (A) HEK293T cells were co-transfected at a ratio of 1:1:1 with pCMV2N3T-HA-SUMO-1: pDEST-MYC-PML-I: pcDNA4/TO or pcDNA4/TO-IE1B plasmids. After 48h cells were collected and lysed in RIPA buffer. A portion (10%) of the lysate was used to monitor protein expression (input). The remaining portion of the lysate was used for IE1 immunoprecipitation. IE1-SUMO-1 conjugates were detected using anti-HA antibodies. In presence of PML, SUMOylation of IE1 is enhance and that is shown by the presence of a second IE1-SUMO-1 band. (B) Illustration representing possible SUMOylation states of protein. Once mature, a SUMO protein is charged on a E1 activating enzyme and then transferred to a E2 conjugating enzyme. The SUMO-E2 complex can directly SUMOylate a protein on its acceptor lysine (K). Following conjugation to E2, the SUMO-E2 complex can be bound by a E3 SUMO ligase that will facilitate the discharge of the SUMO protein on the acceptor site of a target. The presence of a E3 SUMO ligase can influence or help reach those different levels of SUMOylation where polySUMOylation is realized by the presence of SUMO-2/3 paralogues that possess SUMO acceptor sites. (C) Scheme illustrating major domains and modification sites of PML protein. Leucine at position 73 allows the attachment of monomers of PML to form a tetramer, essential for the formation of PML-NBs [ 44 ]. (D) IF images representing the different PML-I phenotypes after transfection of PML-I WT or PML-I RING domain mutant (PML-I:L73E) in U2OS PML -/- cells. PML RING mutant lost the ability to form nuclear bodies. (E) HEK293T cells were co-transfected at a ratio of 1:1:1 with pCMV2N3T-HA-SUMO-1/SUMO-2 or SUMO-3: pCMV-MYC-PML-I: pcDNA4/TO or pcDNA4/TO-IE1B plasmids. Cells were collected and processed as in (A). Enhancement of SUMOylation of IE1 is PML-I WT and SUMO-1 dependent. These results are the representation of three independent experiments (n = 3).

    Journal: PLoS Pathogens

    Article Title: The Promyelocytic Leukemia Protein facilitates human herpesvirus 6B chromosomal integration, immediate-early 1 protein multiSUMOylation and its localization at telomeres

    doi: 10.1371/journal.ppat.1008683

    Figure Lengend Snippet: Presence of PML-NBs leads to hyperSUMOylation of IE1. (A) HEK293T cells were co-transfected at a ratio of 1:1:1 with pCMV2N3T-HA-SUMO-1: pDEST-MYC-PML-I: pcDNA4/TO or pcDNA4/TO-IE1B plasmids. After 48h cells were collected and lysed in RIPA buffer. A portion (10%) of the lysate was used to monitor protein expression (input). The remaining portion of the lysate was used for IE1 immunoprecipitation. IE1-SUMO-1 conjugates were detected using anti-HA antibodies. In presence of PML, SUMOylation of IE1 is enhance and that is shown by the presence of a second IE1-SUMO-1 band. (B) Illustration representing possible SUMOylation states of protein. Once mature, a SUMO protein is charged on a E1 activating enzyme and then transferred to a E2 conjugating enzyme. The SUMO-E2 complex can directly SUMOylate a protein on its acceptor lysine (K). Following conjugation to E2, the SUMO-E2 complex can be bound by a E3 SUMO ligase that will facilitate the discharge of the SUMO protein on the acceptor site of a target. The presence of a E3 SUMO ligase can influence or help reach those different levels of SUMOylation where polySUMOylation is realized by the presence of SUMO-2/3 paralogues that possess SUMO acceptor sites. (C) Scheme illustrating major domains and modification sites of PML protein. Leucine at position 73 allows the attachment of monomers of PML to form a tetramer, essential for the formation of PML-NBs [ 44 ]. (D) IF images representing the different PML-I phenotypes after transfection of PML-I WT or PML-I RING domain mutant (PML-I:L73E) in U2OS PML -/- cells. PML RING mutant lost the ability to form nuclear bodies. (E) HEK293T cells were co-transfected at a ratio of 1:1:1 with pCMV2N3T-HA-SUMO-1/SUMO-2 or SUMO-3: pCMV-MYC-PML-I: pcDNA4/TO or pcDNA4/TO-IE1B plasmids. Cells were collected and processed as in (A). Enhancement of SUMOylation of IE1 is PML-I WT and SUMO-1 dependent. These results are the representation of three independent experiments (n = 3).

    Article Snippet: Cells were transfected 24 hours post-seeding with 4 μg of pcDNA4/TO, or pcDNA4/TO-IE1B expression vector using Lipofectamine 2000 (Thermo Fischer Scientific).

    Techniques: Transfection, Expressing, Immunoprecipitation, Conjugation Assay, Modification, Mutagenesis

    Localization of IE1 at telomeres is influenced by the presence of PML. (A) Deconvoluted confocal microscopy images representative of IE1/telomere staining of U2OS cells infected with HHV-6B for 48 hours. Telomeres were detected using a Cy5-labeled telomeric probe (aqua). Yellow squares represent IE1 colocalizing with telomeres in 3D. (B) Graph showing the percentage ± sd of IE1 (n = 8) foci colocalizing at telomeres throughout the z stacks, in HHV-6B infected U2OS cells. (C) Confocal microscopy images of U2OS PML +/+ and -/- cells transfected with pcDNA4/TO-IE1B or empty vector (EV). Yellow squares represent IE1 colocalizing with telomeres. (D) Graph showing the proportion (mean±sd) of IE1 foci localizing at telomeres throughout the z stacks, in U2OS PML +/+ (n = 46) and PML -/- (n = 42) cells. Each dot represents one IE1 + nucleus. Data were transformed to log values and the normal distributions analyzed using an unpaired t test with Welch's correction to compare frequency of IE1 at telomeres. ****P

    Journal: PLoS Pathogens

    Article Title: The Promyelocytic Leukemia Protein facilitates human herpesvirus 6B chromosomal integration, immediate-early 1 protein multiSUMOylation and its localization at telomeres

    doi: 10.1371/journal.ppat.1008683

    Figure Lengend Snippet: Localization of IE1 at telomeres is influenced by the presence of PML. (A) Deconvoluted confocal microscopy images representative of IE1/telomere staining of U2OS cells infected with HHV-6B for 48 hours. Telomeres were detected using a Cy5-labeled telomeric probe (aqua). Yellow squares represent IE1 colocalizing with telomeres in 3D. (B) Graph showing the percentage ± sd of IE1 (n = 8) foci colocalizing at telomeres throughout the z stacks, in HHV-6B infected U2OS cells. (C) Confocal microscopy images of U2OS PML +/+ and -/- cells transfected with pcDNA4/TO-IE1B or empty vector (EV). Yellow squares represent IE1 colocalizing with telomeres. (D) Graph showing the proportion (mean±sd) of IE1 foci localizing at telomeres throughout the z stacks, in U2OS PML +/+ (n = 46) and PML -/- (n = 42) cells. Each dot represents one IE1 + nucleus. Data were transformed to log values and the normal distributions analyzed using an unpaired t test with Welch's correction to compare frequency of IE1 at telomeres. ****P

    Article Snippet: Cells were transfected 24 hours post-seeding with 4 μg of pcDNA4/TO, or pcDNA4/TO-IE1B expression vector using Lipofectamine 2000 (Thermo Fischer Scientific).

    Techniques: Confocal Microscopy, Staining, Infection, Labeling, Transfection, Plasmid Preparation, Transformation Assay

    Putative IE1 Sumo-Interacting Motif site is important for multiSUMOylation in presence of PML. (A) Scheme and table of potential SUMO acceptor sites and SUMO-interacting motifs (SIM) of IE1 and the nomenclature of the generated mutants. (B) HEK293T cells were co-transfected with a ratio of 1:1:1 of pCMV2N3T-HA-SUMO-1: pcDNA4/TO-IE1B WT, mutants or control: no plasmid, expression vectors. Cells were collected and processed as in Fig 2A . The sequence motif at position 775 AAA 777 and the lysine at position 802 are essential for SUMOylation of IE1. (C) HEK293T cells were co-transfected with a ratio of 1:1:1 of pCMV2N3T-HA-SUMO-1: pcDNA4/TO-IE1B WT, mutants or control: PML, expression vectors. Cells were collected and processed as in Fig 2A . The sequence motif at position 775 AAA 777 and the lysine at position 802 are essential for higher SUMOylation state of IE1. (D) Western blot of WT and K802R SUMOylation of IE1 in HEK293T overexpressing or not PML-I. Cells were collected and processed as in Fig 2A .

    Journal: PLoS Pathogens

    Article Title: The Promyelocytic Leukemia Protein facilitates human herpesvirus 6B chromosomal integration, immediate-early 1 protein multiSUMOylation and its localization at telomeres

    doi: 10.1371/journal.ppat.1008683

    Figure Lengend Snippet: Putative IE1 Sumo-Interacting Motif site is important for multiSUMOylation in presence of PML. (A) Scheme and table of potential SUMO acceptor sites and SUMO-interacting motifs (SIM) of IE1 and the nomenclature of the generated mutants. (B) HEK293T cells were co-transfected with a ratio of 1:1:1 of pCMV2N3T-HA-SUMO-1: pcDNA4/TO-IE1B WT, mutants or control: no plasmid, expression vectors. Cells were collected and processed as in Fig 2A . The sequence motif at position 775 AAA 777 and the lysine at position 802 are essential for SUMOylation of IE1. (C) HEK293T cells were co-transfected with a ratio of 1:1:1 of pCMV2N3T-HA-SUMO-1: pcDNA4/TO-IE1B WT, mutants or control: PML, expression vectors. Cells were collected and processed as in Fig 2A . The sequence motif at position 775 AAA 777 and the lysine at position 802 are essential for higher SUMOylation state of IE1. (D) Western blot of WT and K802R SUMOylation of IE1 in HEK293T overexpressing or not PML-I. Cells were collected and processed as in Fig 2A .

    Article Snippet: Cells were transfected 24 hours post-seeding with 4 μg of pcDNA4/TO, or pcDNA4/TO-IE1B expression vector using Lipofectamine 2000 (Thermo Fischer Scientific).

    Techniques: Generated, Transfection, Plasmid Preparation, Expressing, Sequencing, Western Blot

    Overexpression of calpain small subunit 1 (Capn4) reversed the inhibitory effect of miR-124 on the Wnt/β-catenin signaling pathway. HONE1 and CNE2 cells were transfected with miR-124 or co-transfected with miR-124 and pcDNA-Capn4 ( A and B ). Western blot analysis revealed that Capn4 overexpression reversed the decreased β-catenin, cyclin D1, and c-Myc protein levels caused by the overexpression of miR-124 in HONE1 and CNE2 cells. Data are shown as mean ± standard deviation (n=3). * P

    Journal: OncoTargets and therapy

    Article Title: miR-124 suppresses proliferation and invasion of nasopharyngeal carcinoma cells through the Wnt/β-catenin signaling pathway by targeting Capn4

    doi: 10.2147/OTT.S135563

    Figure Lengend Snippet: Overexpression of calpain small subunit 1 (Capn4) reversed the inhibitory effect of miR-124 on the Wnt/β-catenin signaling pathway. HONE1 and CNE2 cells were transfected with miR-124 or co-transfected with miR-124 and pcDNA-Capn4 ( A and B ). Western blot analysis revealed that Capn4 overexpression reversed the decreased β-catenin, cyclin D1, and c-Myc protein levels caused by the overexpression of miR-124 in HONE1 and CNE2 cells. Data are shown as mean ± standard deviation (n=3). * P

    Article Snippet: Cell transfection The pcDNA-Capn4 and pcDNA-control were purchased from Thermo Fisher Scientific.

    Techniques: Over Expression, Transfection, Western Blot, Standard Deviation

    MicroRNA-124 (miR-124) suppressed proliferation and invasion of NPC cells through the inhibition of Capn4 expression. HONE1 and CNE2 cells were transfected with miR-124 or in combination with pcDNA-Capn4. Notes: ( A ) MTT assay confirmed that restored Capn4 expression reversed the inhibitory effect of miR-124 on the cell viability of HONE1 and CNE2 cells at 24, 48, and 72 h after transfection. Data are shown as mean ± standard error of mean (n=3) ( B and C ) Transwell invasion assay suggested that transfection of pcDNA-Capn4 abolished miR-124-mediated inhibition of cell invasion in HONE1 and CNE2 cells. Data are shown as mean ± standard deviation (n=3). * P

    Journal: OncoTargets and therapy

    Article Title: miR-124 suppresses proliferation and invasion of nasopharyngeal carcinoma cells through the Wnt/β-catenin signaling pathway by targeting Capn4

    doi: 10.2147/OTT.S135563

    Figure Lengend Snippet: MicroRNA-124 (miR-124) suppressed proliferation and invasion of NPC cells through the inhibition of Capn4 expression. HONE1 and CNE2 cells were transfected with miR-124 or in combination with pcDNA-Capn4. Notes: ( A ) MTT assay confirmed that restored Capn4 expression reversed the inhibitory effect of miR-124 on the cell viability of HONE1 and CNE2 cells at 24, 48, and 72 h after transfection. Data are shown as mean ± standard error of mean (n=3) ( B and C ) Transwell invasion assay suggested that transfection of pcDNA-Capn4 abolished miR-124-mediated inhibition of cell invasion in HONE1 and CNE2 cells. Data are shown as mean ± standard deviation (n=3). * P

    Article Snippet: Cell transfection The pcDNA-Capn4 and pcDNA-control were purchased from Thermo Fisher Scientific.

    Techniques: Inhibition, Expressing, Transfection, MTT Assay, Transwell Invasion Assay, Standard Deviation