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Addgene inc complementary dna cdna clones
Complementary Dna Cdna Clones, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/complementary dna cdna clones/product/Addgene inc
Average 90 stars, based on 1 article reviews
Price from $9.99 to $1999.99
complementary dna cdna clones - by Bioz Stars, 2020-05
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Clone Assay:

Article Title: EBV noncoding RNA EBER2 interacts with host RNA-binding proteins to regulate viral gene expression
Article Snippet: .. Complementary DNA (cDNA) clones were obtained from Addgene or Open Biosystems (SFPQ: ID 46320; HNRNPM: ID 2900532; NONO: ID 35379; RBM14: ID 2819856; HNRNPK: ID 2964383; MATR3: ID 32880) and coding sequences were cloned into vector pcDNA-FLAG. .. HEK 293T cells were transfected with EBER2 expression plasmid (pBS-5×EBER2) together with each of the FLAG expression plasmids using Effectene (Qiagen).

Plasmid Preparation:

Article Title: EBV noncoding RNA EBER2 interacts with host RNA-binding proteins to regulate viral gene expression
Article Snippet: .. Complementary DNA (cDNA) clones were obtained from Addgene or Open Biosystems (SFPQ: ID 46320; HNRNPM: ID 2900532; NONO: ID 35379; RBM14: ID 2819856; HNRNPK: ID 2964383; MATR3: ID 32880) and coding sequences were cloned into vector pcDNA-FLAG. .. HEK 293T cells were transfected with EBER2 expression plasmid (pBS-5×EBER2) together with each of the FLAG expression plasmids using Effectene (Qiagen).

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  • 92
    Addgene inc full length human pvt1 cdna
    Wnt/β-catenin signaling pathway is involved in <t>PVT1-</t> mediated SCCHN progression. Specific inhibitor iCRT14 (20μmol/L) was used to impede Wnt/β-catenin signaling pathway in FaDu cells infected with PVT1 <t>cDNA</t> and empty vector, and then: (A) western blotting assays were used to check alterations of Wnt/β-catenin signaling molecules. (B) Cell proliferation was assayed by CCK8. (C) Transwell migration and (D) invasion assays were used to examine the changes of migration and invasion. (E) E-cadherin and (F) Vimentin mRNAs were examined by qPCR.
    Full Length Human Pvt1 Cdna, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/full length human pvt1 cdna/product/Addgene inc
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    85
    Addgene inc mdpy 30 cdna
    Colocalization analyses between internalized β1 integrin and EGFP-Rab4b or EGFP-Rab11 recycling GTPases in <t>mDpy-30</t> knockdown cells. HeLa cells were transfected with 20 nM siRNAs for 48 hr and/or <t>cDNA</t> for 24 hr before analysis. (A) Impact of depleting mDpy-30 on the endosomal trafficking of β1 integrin. An anti-β1 integrin antibody was employed to label surface β1 integrin (0°C, 1 hr). After labeling, cells were returned to 37°C for various periods of time before imaging analysis. A brief acid wash was conducted as described in “ Materials and Methods ” before fixation to remove surface-bound antibody and permit the better visualization of internalized β1 integrin. The enrichment of internalized β1 integrin near cell protrusions was scored as described in Fig. 2 . The experiments were performed six times (n = 6) with more than 500 cells scored in each experiment. (B) The fraction of total internalized β1 integrin that appears at cell protrusions was determined from confocal images of cells treated with either a non-targeting control siRNA or mDpy-30 siRNA. Only cells exhibiting internalized β1 integrin at cell protrusions were assayed from both conditions. At least 50 cells from each condition were used for the quantification. The average number of protrusions per cell did not vary significantly in the two conditions (1.2 for control and 1.3 for mDpy-30 siRNA); p-value determined by Student's T-test (C–D) Colocalization analyses of internalized β1 integrin and either EGFP-Rab4b (C) or EGFP-Rab11 (D) using confocal microscopy. An anti-β1 integrin antibody was added to the culture medium (37°C, 45 min) to allow the labeling and internalization of β1 integrin. The graphs at the right indicate the signal intensity of each pixel measured in the single representative Z-section images that appear to the left. The X-axis is the intensity of EGFP-Rab4b or EGFP-Rab11 signal and the Y-axis corresponds to that of internalized β1 integrin. The color on the graph corresponds the relative frequency with which a specific combination of X and Y values is found in all the pixels analyzed, with blue indicating lower frequencies and red higher frequencies. (E–F) Quantification of colocalization between internalized β1 integrin and either EGFP-Rab4b or EGFP-Rab11 in the entire cell (E) or the protrusions (F) of cells depleted of mDpy-30. The Pearson's correlations were determined as described in Fig. 3C and 3D . Error bars: standard deviation; scale bars: 10 µm.
    Mdpy 30 Cdna, supplied by Addgene inc, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mdpy 30 cdna/product/Addgene inc
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    93
    Addgene inc human bcl xl cdna
    B, Retroviral vectors containing human <t>Bcl-2</t> or Bcl-xL <t>cDNA,</t> GFP, and an IRES element to couple translation. GFP coexpression allowed for efficient identification of selective growth or survival of transduced populations. GFP indicates green fluorescent protein; IRES, internal ribosome entry site; LTR, long terminal repeat; TCR, T-cell receptor.
    Human Bcl Xl Cdna, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Addgene inc full length zfp64 cdna
    <t>ZFP64</t> employs a C-terminal transactivation domain to maintain MLL expression and leukemia growth. (A) Experimental strategy used to map the trans-activation domain (TAD) of ZFP64 using GAL4 fusion reporter assays. (B) A series of GAL4-ZFP64 fusion proteins tested in the luciferase assay. FL: full length, ZF: Zinc finger. Number Z1-Z11 describes the number of Zinc finger contained in the construct. Transactivation activity of different ZFP64 mutant by luciferase assay is plotted. Renilla luciferase internal control normalized. (n=3) (C) Western blot confirming detectable protein levels of GAL4-ZFP64 fusion proteins after transfected into 293T cells. (D) RT-qPCR analysis of MLL expression in MOLM-13 cells transduced with various combination of sgRNAs or CRISPR-resistant ZFP64 <t>cDNA.</t> Results were normalized to GAPDH . (n=3) (E) Competition-based proliferation assay in MOLM-13 after transduction with various combination of sgRNAs or CRISPR-resistant ZFP64 cDNA. (n=3) (F) Western blot confirming detectable protein levels of CRISPR resistant ZFP64 cDNA (ZFP64 WT ) and C-terminal deleted ZFP64 mutant (ZFP64 ΔTAD ) in MOLM-13. (G) Domain structure of ZFP64. All bar graphs represent the mean ± SEM. * denotes unpaired T test, p
    Full Length Zfp64 Cdna, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Wnt/β-catenin signaling pathway is involved in PVT1- mediated SCCHN progression. Specific inhibitor iCRT14 (20μmol/L) was used to impede Wnt/β-catenin signaling pathway in FaDu cells infected with PVT1 cDNA and empty vector, and then: (A) western blotting assays were used to check alterations of Wnt/β-catenin signaling molecules. (B) Cell proliferation was assayed by CCK8. (C) Transwell migration and (D) invasion assays were used to examine the changes of migration and invasion. (E) E-cadherin and (F) Vimentin mRNAs were examined by qPCR.

    Journal: Journal of Cancer

    Article Title: LncRNA PVT1 promotes malignant progression in squamous cell carcinoma of the head and neck

    doi: 10.7150/jca.26465

    Figure Lengend Snippet: Wnt/β-catenin signaling pathway is involved in PVT1- mediated SCCHN progression. Specific inhibitor iCRT14 (20μmol/L) was used to impede Wnt/β-catenin signaling pathway in FaDu cells infected with PVT1 cDNA and empty vector, and then: (A) western blotting assays were used to check alterations of Wnt/β-catenin signaling molecules. (B) Cell proliferation was assayed by CCK8. (C) Transwell migration and (D) invasion assays were used to examine the changes of migration and invasion. (E) E-cadherin and (F) Vimentin mRNAs were examined by qPCR.

    Article Snippet: Overexpression or knockdown of PVT1 For PVT1 overexpression, full-length human PVT1 cDNA was amplified by PCR and then cloned into pLV lentiviral plasmid (Addgene).

    Techniques: Infection, Plasmid Preparation, Western Blot, Migration, Real-time Polymerase Chain Reaction

    Colocalization analyses between internalized β1 integrin and EGFP-Rab4b or EGFP-Rab11 recycling GTPases in mDpy-30 knockdown cells. HeLa cells were transfected with 20 nM siRNAs for 48 hr and/or cDNA for 24 hr before analysis. (A) Impact of depleting mDpy-30 on the endosomal trafficking of β1 integrin. An anti-β1 integrin antibody was employed to label surface β1 integrin (0°C, 1 hr). After labeling, cells were returned to 37°C for various periods of time before imaging analysis. A brief acid wash was conducted as described in “ Materials and Methods ” before fixation to remove surface-bound antibody and permit the better visualization of internalized β1 integrin. The enrichment of internalized β1 integrin near cell protrusions was scored as described in Fig. 2 . The experiments were performed six times (n = 6) with more than 500 cells scored in each experiment. (B) The fraction of total internalized β1 integrin that appears at cell protrusions was determined from confocal images of cells treated with either a non-targeting control siRNA or mDpy-30 siRNA. Only cells exhibiting internalized β1 integrin at cell protrusions were assayed from both conditions. At least 50 cells from each condition were used for the quantification. The average number of protrusions per cell did not vary significantly in the two conditions (1.2 for control and 1.3 for mDpy-30 siRNA); p-value determined by Student's T-test (C–D) Colocalization analyses of internalized β1 integrin and either EGFP-Rab4b (C) or EGFP-Rab11 (D) using confocal microscopy. An anti-β1 integrin antibody was added to the culture medium (37°C, 45 min) to allow the labeling and internalization of β1 integrin. The graphs at the right indicate the signal intensity of each pixel measured in the single representative Z-section images that appear to the left. The X-axis is the intensity of EGFP-Rab4b or EGFP-Rab11 signal and the Y-axis corresponds to that of internalized β1 integrin. The color on the graph corresponds the relative frequency with which a specific combination of X and Y values is found in all the pixels analyzed, with blue indicating lower frequencies and red higher frequencies. (E–F) Quantification of colocalization between internalized β1 integrin and either EGFP-Rab4b or EGFP-Rab11 in the entire cell (E) or the protrusions (F) of cells depleted of mDpy-30. The Pearson's correlations were determined as described in Fig. 3C and 3D . Error bars: standard deviation; scale bars: 10 µm.

    Journal: PLoS ONE

    Article Title: Modulation of Cell Adhesion and Migration by the Histone Methyltransferase Subunit mDpy-30 and Its Interacting Proteins

    doi: 10.1371/journal.pone.0011771

    Figure Lengend Snippet: Colocalization analyses between internalized β1 integrin and EGFP-Rab4b or EGFP-Rab11 recycling GTPases in mDpy-30 knockdown cells. HeLa cells were transfected with 20 nM siRNAs for 48 hr and/or cDNA for 24 hr before analysis. (A) Impact of depleting mDpy-30 on the endosomal trafficking of β1 integrin. An anti-β1 integrin antibody was employed to label surface β1 integrin (0°C, 1 hr). After labeling, cells were returned to 37°C for various periods of time before imaging analysis. A brief acid wash was conducted as described in “ Materials and Methods ” before fixation to remove surface-bound antibody and permit the better visualization of internalized β1 integrin. The enrichment of internalized β1 integrin near cell protrusions was scored as described in Fig. 2 . The experiments were performed six times (n = 6) with more than 500 cells scored in each experiment. (B) The fraction of total internalized β1 integrin that appears at cell protrusions was determined from confocal images of cells treated with either a non-targeting control siRNA or mDpy-30 siRNA. Only cells exhibiting internalized β1 integrin at cell protrusions were assayed from both conditions. At least 50 cells from each condition were used for the quantification. The average number of protrusions per cell did not vary significantly in the two conditions (1.2 for control and 1.3 for mDpy-30 siRNA); p-value determined by Student's T-test (C–D) Colocalization analyses of internalized β1 integrin and either EGFP-Rab4b (C) or EGFP-Rab11 (D) using confocal microscopy. An anti-β1 integrin antibody was added to the culture medium (37°C, 45 min) to allow the labeling and internalization of β1 integrin. The graphs at the right indicate the signal intensity of each pixel measured in the single representative Z-section images that appear to the left. The X-axis is the intensity of EGFP-Rab4b or EGFP-Rab11 signal and the Y-axis corresponds to that of internalized β1 integrin. The color on the graph corresponds the relative frequency with which a specific combination of X and Y values is found in all the pixels analyzed, with blue indicating lower frequencies and red higher frequencies. (E–F) Quantification of colocalization between internalized β1 integrin and either EGFP-Rab4b or EGFP-Rab11 in the entire cell (E) or the protrusions (F) of cells depleted of mDpy-30. The Pearson's correlations were determined as described in Fig. 3C and 3D . Error bars: standard deviation; scale bars: 10 µm.

    Article Snippet: DNA constructs and reagents For lentivirus-mediated overexpression of mDpy-30, mDpy-30 cDNA was cloned into pWPI (Addgene).

    Techniques: Transfection, Labeling, Imaging, Confocal Microscopy, Standard Deviation

    Colocalization analyses between internalized CD8-CIMPR and EGFP-Rab4b or EGFP-Rab11 recycling GTPases in mDpy-30 knockdown cells. HeLa cells were transfected with 20 nM siRNAs for 48 hr and/or cDNA for 24 hr before analysis. (A–B) Colocalization analyses of internalized CD8-CIMPR and EGFP-Rab4b (A) or EGFP-Rab11 (B) in HeLa CD8-CIMPR stable cells treated with an mDpy-30 siRNA. A monoclonal anti-CD8 antibody was added to the culture media (37°C, 45 min) to allow the labeling and internalization of surface CD8-CIMPR [5] , and the localizations of internalized receptors and both Rab GTPases were examined using a confocal microscope. (C–D) Quantification of colocalization between internalized CD8-CIMPR and either EGFP-Rab4b or EGFP-Rab11 in the entire cell (C) or the protrusions (D) of HeLa CD8-CIMPR cells depleted of mDpy-30. The Pearson's correlations between the signals in single 0.5 µm Z-sections of confocal images were calculated. At least 20 cells were measured for each condition. (E–F) Colocalization analyses between VPS26 and internalized CD8-CIMPR (F) or EGFP-Rab4b (F) using a conventional microscope. Error bars: standard deviation; scale bars: 10 µm. Asterisks indicate a p-value of ≤0.05 (*) or ≤0.01(**) as determined by Student's T-test.

    Journal: PLoS ONE

    Article Title: Modulation of Cell Adhesion and Migration by the Histone Methyltransferase Subunit mDpy-30 and Its Interacting Proteins

    doi: 10.1371/journal.pone.0011771

    Figure Lengend Snippet: Colocalization analyses between internalized CD8-CIMPR and EGFP-Rab4b or EGFP-Rab11 recycling GTPases in mDpy-30 knockdown cells. HeLa cells were transfected with 20 nM siRNAs for 48 hr and/or cDNA for 24 hr before analysis. (A–B) Colocalization analyses of internalized CD8-CIMPR and EGFP-Rab4b (A) or EGFP-Rab11 (B) in HeLa CD8-CIMPR stable cells treated with an mDpy-30 siRNA. A monoclonal anti-CD8 antibody was added to the culture media (37°C, 45 min) to allow the labeling and internalization of surface CD8-CIMPR [5] , and the localizations of internalized receptors and both Rab GTPases were examined using a confocal microscope. (C–D) Quantification of colocalization between internalized CD8-CIMPR and either EGFP-Rab4b or EGFP-Rab11 in the entire cell (C) or the protrusions (D) of HeLa CD8-CIMPR cells depleted of mDpy-30. The Pearson's correlations between the signals in single 0.5 µm Z-sections of confocal images were calculated. At least 20 cells were measured for each condition. (E–F) Colocalization analyses between VPS26 and internalized CD8-CIMPR (F) or EGFP-Rab4b (F) using a conventional microscope. Error bars: standard deviation; scale bars: 10 µm. Asterisks indicate a p-value of ≤0.05 (*) or ≤0.01(**) as determined by Student's T-test.

    Article Snippet: DNA constructs and reagents For lentivirus-mediated overexpression of mDpy-30, mDpy-30 cDNA was cloned into pWPI (Addgene).

    Techniques: Transfection, Labeling, Microscopy, Standard Deviation

    B, Retroviral vectors containing human Bcl-2 or Bcl-xL cDNA, GFP, and an IRES element to couple translation. GFP coexpression allowed for efficient identification of selective growth or survival of transduced populations. GFP indicates green fluorescent protein; IRES, internal ribosome entry site; LTR, long terminal repeat; TCR, T-cell receptor.

    Journal: Journal of immunotherapy (Hagerstown, Md. : 1997)

    Article Title: Prevention of Interleukin-2 Withdrawal-Induced Apoptosis in Lymphocytes Retrovirally Cotransduced With Genes Encoding an Antitumor T-cell Receptor and an Antiapoptotic Protein

    doi: 10.1097/CJI.0b013e3181e475cd

    Figure Lengend Snippet: B, Retroviral vectors containing human Bcl-2 or Bcl-xL cDNA, GFP, and an IRES element to couple translation. GFP coexpression allowed for efficient identification of selective growth or survival of transduced populations. GFP indicates green fluorescent protein; IRES, internal ribosome entry site; LTR, long terminal repeat; TCR, T-cell receptor.

    Article Snippet: Human Bcl-xL cDNA followed by internal ribosome entry site (IRES) and green fluorescent protein (GFP) (Bcl-xL.GFP) were cloned into the pMSGV from pMIG-Bcl-xL (Addgene plasmid 8790) as well.

    Techniques:

    ZFP64 employs a C-terminal transactivation domain to maintain MLL expression and leukemia growth. (A) Experimental strategy used to map the trans-activation domain (TAD) of ZFP64 using GAL4 fusion reporter assays. (B) A series of GAL4-ZFP64 fusion proteins tested in the luciferase assay. FL: full length, ZF: Zinc finger. Number Z1-Z11 describes the number of Zinc finger contained in the construct. Transactivation activity of different ZFP64 mutant by luciferase assay is plotted. Renilla luciferase internal control normalized. (n=3) (C) Western blot confirming detectable protein levels of GAL4-ZFP64 fusion proteins after transfected into 293T cells. (D) RT-qPCR analysis of MLL expression in MOLM-13 cells transduced with various combination of sgRNAs or CRISPR-resistant ZFP64 cDNA. Results were normalized to GAPDH . (n=3) (E) Competition-based proliferation assay in MOLM-13 after transduction with various combination of sgRNAs or CRISPR-resistant ZFP64 cDNA. (n=3) (F) Western blot confirming detectable protein levels of CRISPR resistant ZFP64 cDNA (ZFP64 WT ) and C-terminal deleted ZFP64 mutant (ZFP64 ΔTAD ) in MOLM-13. (G) Domain structure of ZFP64. All bar graphs represent the mean ± SEM. * denotes unpaired T test, p

    Journal: Cancer cell

    Article Title: A transcription factor addiction in leukemia imposed by theMLL promoter sequence

    doi: 10.1016/j.ccell.2018.10.015

    Figure Lengend Snippet: ZFP64 employs a C-terminal transactivation domain to maintain MLL expression and leukemia growth. (A) Experimental strategy used to map the trans-activation domain (TAD) of ZFP64 using GAL4 fusion reporter assays. (B) A series of GAL4-ZFP64 fusion proteins tested in the luciferase assay. FL: full length, ZF: Zinc finger. Number Z1-Z11 describes the number of Zinc finger contained in the construct. Transactivation activity of different ZFP64 mutant by luciferase assay is plotted. Renilla luciferase internal control normalized. (n=3) (C) Western blot confirming detectable protein levels of GAL4-ZFP64 fusion proteins after transfected into 293T cells. (D) RT-qPCR analysis of MLL expression in MOLM-13 cells transduced with various combination of sgRNAs or CRISPR-resistant ZFP64 cDNA. Results were normalized to GAPDH . (n=3) (E) Competition-based proliferation assay in MOLM-13 after transduction with various combination of sgRNAs or CRISPR-resistant ZFP64 cDNA. (n=3) (F) Western blot confirming detectable protein levels of CRISPR resistant ZFP64 cDNA (ZFP64 WT ) and C-terminal deleted ZFP64 mutant (ZFP64 ΔTAD ) in MOLM-13. (G) Domain structure of ZFP64. All bar graphs represent the mean ± SEM. * denotes unpaired T test, p

    Article Snippet: For the cDNA overexpression experiments, a full length ZFP64 cDNA (DNASU, clone: HsCD00514448) was cloned into a lentiviral expression vector LentiV_Neo (Addgene: 108101).

    Techniques: Expressing, Activation Assay, Luciferase, Construct, Activity Assay, Mutagenesis, Western Blot, Transfection, Quantitative RT-PCR, Transduction, CRISPR, Proliferation Assay

    MLL promoter activation is the critical function of ZFP64 underlying its role as a dependency in MLL -rearranged leukemia. (A) Experimental strategy for dual CRISPR-activation/mutagenesis. (B) RT-qPCR analysis of MLL after expressing the indicated sgRNAs targeting the MLL promoter in the CRISPR-activation experiment. (C) Western blotting of ZFP64 after transduction of sgRNAs targeting ZFP64 in MOLM-13 using S. aureus CRISPR indel mutagenesis. (D) Competition-based proliferation assay after SaCas9 based inactivation of ZFP64 and Sp_dCas9-based activation of MLL using sgRNA#11 or sgRNA#14. (n=3) (E) Western blotting and competition-based proliferation assay evaluating the effect of ZFP64 sgRNAs in human retroviral MLL-AF9/Nras G12D AML cells. sgRNA expression is linked to mCherry reporter in this experiment, since the cells were already GFP + . (n=3) (F) RNA-seq analysis of human retroviral MLL-AF9/Nras G12D AML cells after transduction with sgRNA targeting ZFP64 . To evaluate endogenous MLL , a custom transcript was inserted into the analysis representing the C-terminal portion of the gene (absent from the fusion cDNA). (G) Western blotting and competition-based proliferation assay evaluating the effect of Zfp64 sgRNAs in mouse MLL-AF9 knock-in AML cells. (n=3) (H) Western blotting and competition-based proliferation assay evaluating the effect of Zfp64 sgRNAs in mouse retroviral MLL-AF9/Nras G12D .

    Journal: Cancer cell

    Article Title: A transcription factor addiction in leukemia imposed by theMLL promoter sequence

    doi: 10.1016/j.ccell.2018.10.015

    Figure Lengend Snippet: MLL promoter activation is the critical function of ZFP64 underlying its role as a dependency in MLL -rearranged leukemia. (A) Experimental strategy for dual CRISPR-activation/mutagenesis. (B) RT-qPCR analysis of MLL after expressing the indicated sgRNAs targeting the MLL promoter in the CRISPR-activation experiment. (C) Western blotting of ZFP64 after transduction of sgRNAs targeting ZFP64 in MOLM-13 using S. aureus CRISPR indel mutagenesis. (D) Competition-based proliferation assay after SaCas9 based inactivation of ZFP64 and Sp_dCas9-based activation of MLL using sgRNA#11 or sgRNA#14. (n=3) (E) Western blotting and competition-based proliferation assay evaluating the effect of ZFP64 sgRNAs in human retroviral MLL-AF9/Nras G12D AML cells. sgRNA expression is linked to mCherry reporter in this experiment, since the cells were already GFP + . (n=3) (F) RNA-seq analysis of human retroviral MLL-AF9/Nras G12D AML cells after transduction with sgRNA targeting ZFP64 . To evaluate endogenous MLL , a custom transcript was inserted into the analysis representing the C-terminal portion of the gene (absent from the fusion cDNA). (G) Western blotting and competition-based proliferation assay evaluating the effect of Zfp64 sgRNAs in mouse MLL-AF9 knock-in AML cells. (n=3) (H) Western blotting and competition-based proliferation assay evaluating the effect of Zfp64 sgRNAs in mouse retroviral MLL-AF9/Nras G12D .

    Article Snippet: For the cDNA overexpression experiments, a full length ZFP64 cDNA (DNASU, clone: HsCD00514448) was cloned into a lentiviral expression vector LentiV_Neo (Addgene: 108101).

    Techniques: Activation Assay, CRISPR, Mutagenesis, Quantitative RT-PCR, Expressing, Western Blot, Transduction, Proliferation Assay, RNA Sequencing Assay, Knock-In