dna fragmentation  (Millipore)

 
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    Name:
    DNA Fragmentation Imaging Kit
    Description:
    The DNA Fragmentation Imaging Kit is a simple and rapid TUNEL assay for detecting apoptosis induction in mammalian cells DNA fragmentation detected using terminal deoxynucleotidyl transferase and fluorescein labeled dUTP is measured by fluorescence microscopy or an automated imaging platform such as the Cellavista System The kit uses a dye to stain the nuclei of living and dead cells for quantifying total and apoptotic cell numbers and calculating the percentage of apoptotic cells
    Catalog Number:
    06432344001
    Price:
    None
    Applications:
    Programmed cell death (apoptosis) is a key pathway in mammalian cells during tissue homeostasis. Cell death malfunction has been implicated in pathology. Quantification of caspase-triggered DNA fragmentation is one of the principal techniques used to detect apoptosis induction. The DNA Fragmentation Imaging Kit performs the TUNEL assay for accurate and fast quantitative fluorescence detection using terminal deoxynucleotidyl transferase and fluorescein-labeled dUTP. The kit is ideal for measuring apoptosis in medium to high throughput cellular workflows.. Quickly determine apoptosis induction for cell-based workflows in life science research.. Reliably perform screening assays in product development, e.g., cancer research, pre-clinical safety.. Accurately measure malignant cell sensitivity in cancer research.
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    Structured Review

    Millipore dna fragmentation
    DNA Fragmentation Imaging Kit
    The DNA Fragmentation Imaging Kit is a simple and rapid TUNEL assay for detecting apoptosis induction in mammalian cells DNA fragmentation detected using terminal deoxynucleotidyl transferase and fluorescein labeled dUTP is measured by fluorescence microscopy or an automated imaging platform such as the Cellavista System The kit uses a dye to stain the nuclei of living and dead cells for quantifying total and apoptotic cell numbers and calculating the percentage of apoptotic cells
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    Images

    1) Product Images from "Phloridzin docosahexaenoate, a novel flavonoid derivative, suppresses growth and induces apoptosis in T-cell acute lymphoblastic leukemia cells"

    Article Title: Phloridzin docosahexaenoate, a novel flavonoid derivative, suppresses growth and induces apoptosis in T-cell acute lymphoblastic leukemia cells

    Journal: American Journal of Cancer Research

    doi:

    PZ-DHA-induced apoptosis is associated with caspase activation and DNA fragmentation in Jurkat cells. A. Jurkat and K562 cells were treated with vehicle, test compounds (50 µM), or 2.5 µM staurosporine, STS (positive control) for 18 h and caspase activity was detected using Caspase-Glo 3/7 assay. Luminescence units were recorded. B. Jurkat and K562 cells were treated with vehicle or test compounds (50 µM) for 24 h and DNA fragmentation was quantified by ELISA assay. Absorbance values were measured at 370 nm. Data represent mean ± SD (n=3). * P
    Figure Legend Snippet: PZ-DHA-induced apoptosis is associated with caspase activation and DNA fragmentation in Jurkat cells. A. Jurkat and K562 cells were treated with vehicle, test compounds (50 µM), or 2.5 µM staurosporine, STS (positive control) for 18 h and caspase activity was detected using Caspase-Glo 3/7 assay. Luminescence units were recorded. B. Jurkat and K562 cells were treated with vehicle or test compounds (50 µM) for 24 h and DNA fragmentation was quantified by ELISA assay. Absorbance values were measured at 370 nm. Data represent mean ± SD (n=3). * P

    Techniques Used: Activation Assay, Positive Control, Activity Assay, Caspase-Glo Assay, Enzyme-linked Immunosorbent Assay

    2) Product Images from "Trauma-Hemorrhagic Shock Mesenteric Lymph Induces Endothelial Apoptosis That Involves Both Caspase-Dependent and Caspase-Independent Mechanisms"

    Article Title: Trauma-Hemorrhagic Shock Mesenteric Lymph Induces Endothelial Apoptosis That Involves Both Caspase-Dependent and Caspase-Independent Mechanisms

    Journal: Annals of Surgery

    doi: 10.1097/01.sla.0000129341.94219.cf

    FIGURE 2. (A) T/HS lymph but not T/SS lymph or medium induced DNA fragmentation. HUVECs were incubated with lymph for 4 hours, after which genomic DNA was isolated, fractionated on a 1.5% agarose gel and stained with ethidium bromide. The hallmark DNA step-laddering pattern characteristic of apoptosis is present only in the HUVECS incubated with T/HS lymph. These results are representative of 3 independent studies (M, marker). (B) The number of free nucleosomes generated in HUVECs after 4-hour incubation with T/HS lymph was increased compared with HUVECs incubated in medium or T/SS lymph. Nuclear extracts were prepared using a Nucleosome ELISA kit (Oncogene Research). Optical density (OD) correlates with the number of free nucleosomes. Data expressed as mean ± SD. * P
    Figure Legend Snippet: FIGURE 2. (A) T/HS lymph but not T/SS lymph or medium induced DNA fragmentation. HUVECs were incubated with lymph for 4 hours, after which genomic DNA was isolated, fractionated on a 1.5% agarose gel and stained with ethidium bromide. The hallmark DNA step-laddering pattern characteristic of apoptosis is present only in the HUVECS incubated with T/HS lymph. These results are representative of 3 independent studies (M, marker). (B) The number of free nucleosomes generated in HUVECs after 4-hour incubation with T/HS lymph was increased compared with HUVECs incubated in medium or T/SS lymph. Nuclear extracts were prepared using a Nucleosome ELISA kit (Oncogene Research). Optical density (OD) correlates with the number of free nucleosomes. Data expressed as mean ± SD. * P

    Techniques Used: Incubation, Isolation, Agarose Gel Electrophoresis, Staining, Marker, Generated, Enzyme-linked Immunosorbent Assay

    3) Product Images from "Flavokawain B and Doxorubicin Work Synergistically to Impede the Propagation of Gastric Cancer Cells via ROS-Mediated Apoptosis and Autophagy Pathways"

    Article Title: Flavokawain B and Doxorubicin Work Synergistically to Impede the Propagation of Gastric Cancer Cells via ROS-Mediated Apoptosis and Autophagy Pathways

    Journal: Cancers

    doi: 10.3390/cancers12092475

    The synergistic effects of flavokawain B (FKB) and co-treatment with doxorubicin induced apoptosis of AGS cells in human gastric cancer. Cells have been exposed to FKB (0–2.5 μg/mL), doxorubicin (0.5 μg/mL), and a 24-h mixture of them. ( A ) Microscopy of phase-contrast (200 scale magnification) was used to investigate structural changes. ( B ) A TUNEL assay was conducted to determine the fragmentation of apoptotic DNA. The green florescence indicates the number of TUNEL-positive cells from three separate samples in the microscopic fields (Bar, 50 micron). ( C ) Western blot study of the protein content of caspase-3. It shows typical results of three independent experiments. On SDS-PAGE, the protein (50 μg) was resolved from each sample, and Western blot was performed. β-actin was used as an internal control of loads. Densitometric analysis calculated relative changes in protein bands with the control as 1.0-fold, as shown just below the gel results ( Figure S1 ). Values were expressed as mean ± SD ( n = 3). Significant at *** p
    Figure Legend Snippet: The synergistic effects of flavokawain B (FKB) and co-treatment with doxorubicin induced apoptosis of AGS cells in human gastric cancer. Cells have been exposed to FKB (0–2.5 μg/mL), doxorubicin (0.5 μg/mL), and a 24-h mixture of them. ( A ) Microscopy of phase-contrast (200 scale magnification) was used to investigate structural changes. ( B ) A TUNEL assay was conducted to determine the fragmentation of apoptotic DNA. The green florescence indicates the number of TUNEL-positive cells from three separate samples in the microscopic fields (Bar, 50 micron). ( C ) Western blot study of the protein content of caspase-3. It shows typical results of three independent experiments. On SDS-PAGE, the protein (50 μg) was resolved from each sample, and Western blot was performed. β-actin was used as an internal control of loads. Densitometric analysis calculated relative changes in protein bands with the control as 1.0-fold, as shown just below the gel results ( Figure S1 ). Values were expressed as mean ± SD ( n = 3). Significant at *** p

    Techniques Used: Microscopy, TUNEL Assay, Western Blot, SDS Page

    FKB exacerbates apoptotic cell death in AGS cells caused by doxorubicin. Cells were treated for 1 h with the apoptosis inhibitor (Z-VAD-FMK, 20 μM) prior to co-treatment with FKB (2.5 μg/mL) and doxorubicin (0.5 μg/mL) for 24 h. ( A ) Morphological changes were examined under a phase-contrast microscope and the MTT assay was performed on the viability of the cells. ( B , C ) A TUNEL assay was conducted to determine the fragmentation of apoptotic DNA. The green florescence shows the number of TUNEL-positive cells from three separate samples in the microscopic fields (Bar, 50 μM). Values were expressed as mean ± SD ( n = 3). Significant at *** p
    Figure Legend Snippet: FKB exacerbates apoptotic cell death in AGS cells caused by doxorubicin. Cells were treated for 1 h with the apoptosis inhibitor (Z-VAD-FMK, 20 μM) prior to co-treatment with FKB (2.5 μg/mL) and doxorubicin (0.5 μg/mL) for 24 h. ( A ) Morphological changes were examined under a phase-contrast microscope and the MTT assay was performed on the viability of the cells. ( B , C ) A TUNEL assay was conducted to determine the fragmentation of apoptotic DNA. The green florescence shows the number of TUNEL-positive cells from three separate samples in the microscopic fields (Bar, 50 μM). Values were expressed as mean ± SD ( n = 3). Significant at *** p

    Techniques Used: Microscopy, MTT Assay, TUNEL Assay

    4) Product Images from "Concomitant epigenetic targeting of LSD1 and HDAC synergistically induces mitochondrial apoptosis in rhabdomyosarcoma cells"

    Article Title: Concomitant epigenetic targeting of LSD1 and HDAC synergistically induces mitochondrial apoptosis in rhabdomyosarcoma cells

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2017.239

    BMF, BIM and NOXA contribute to GSK690/JNJ-26481585-induced apoptosis. RD and RH30 were transiently transfected for 24 h with non-silencing siRNA or siRNA targeting BMF, BIM or NOXA mRNA. ( a, c,e ), BMF mRNA levels were assessed by qRT-PCR ( a ), BIM ( c ) and NOXA ( e ) protein levels were detected by Western blotting; β-Actin was used as loading control. ( b, d,f ), Cells were treated 24 h after transfection with 1 μ M GSK690 (RD cells) or 5 μ M GSK690 (RH30 cells) and/or 10 nM JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). In ( b, d,f ), mean and SD of three independent experiments performed in triplicate are shown; * P
    Figure Legend Snippet: BMF, BIM and NOXA contribute to GSK690/JNJ-26481585-induced apoptosis. RD and RH30 were transiently transfected for 24 h with non-silencing siRNA or siRNA targeting BMF, BIM or NOXA mRNA. ( a, c,e ), BMF mRNA levels were assessed by qRT-PCR ( a ), BIM ( c ) and NOXA ( e ) protein levels were detected by Western blotting; β-Actin was used as loading control. ( b, d,f ), Cells were treated 24 h after transfection with 1 μ M GSK690 (RD cells) or 5 μ M GSK690 (RH30 cells) and/or 10 nM JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). In ( b, d,f ), mean and SD of three independent experiments performed in triplicate are shown; * P

    Techniques Used: Transfection, Quantitative RT-PCR, Western Blot, Flow Cytometry, Staining, Fluorescence, Microscopy, Double Staining

    BAK contributes to GSK690/JNJ-26481585-induced apoptosis. RD and RH30 were transiently transfected for 48 h with non-silencing siRNA or siRNA targeting BAK. ( a ) Knockdown of BAK protein was detected by Western blotting, GAPDH served as loading control. ( b ) Cells were treated 48 h after transfection with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 72 h and cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). Mean and S.D. of three independent experiments performed in triplicate are shown; * P
    Figure Legend Snippet: BAK contributes to GSK690/JNJ-26481585-induced apoptosis. RD and RH30 were transiently transfected for 48 h with non-silencing siRNA or siRNA targeting BAK. ( a ) Knockdown of BAK protein was detected by Western blotting, GAPDH served as loading control. ( b ) Cells were treated 48 h after transfection with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 72 h and cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). Mean and S.D. of three independent experiments performed in triplicate are shown; * P

    Techniques Used: Transfection, Western Blot, Flow Cytometry, Staining, Fluorescence, Microscopy, Double Staining

    GSK690/JNJ-26481585 cotreatment induces caspase-dependent cell death. ( a ) Cells were treated for indicated times with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585. Caspase-3 and caspase-9 cleavage was detected by Western blotting, cleavage products are indicated by arrows. GAPDH was used as loading control. Cells were treated with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 21 h (RD cells) or 15 h (RH30 cells). PARP cleavage was detected by Western blotting, the cleavage product is indicated by arrow; β-Actin was used as loading control. ( b ) Cells were treated for 72 h with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 in the presence or absence of 50 μ M zVAD.fmk. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei. Mean and SD of three independent experiments performed in triplicate are shown; * P
    Figure Legend Snippet: GSK690/JNJ-26481585 cotreatment induces caspase-dependent cell death. ( a ) Cells were treated for indicated times with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585. Caspase-3 and caspase-9 cleavage was detected by Western blotting, cleavage products are indicated by arrows. GAPDH was used as loading control. Cells were treated with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 21 h (RD cells) or 15 h (RH30 cells). PARP cleavage was detected by Western blotting, the cleavage product is indicated by arrow; β-Actin was used as loading control. ( b ) Cells were treated for 72 h with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 in the presence or absence of 50 μ M zVAD.fmk. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei. Mean and SD of three independent experiments performed in triplicate are shown; * P

    Techniques Used: Western Blot, Flow Cytometry, Staining

    LSD1 and HDAC inhibitors synergize to induce cell death in RMS cells. ( a ) Cells were treated with indicated concentrations of GSK690 and/or JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei. ( b ) Cells were treated with 1 μ M GSK690 and 15 nM JNJ-26481585 (RD) or 10 μ M GSK690 and 5 nM JNJ-26481585 (RH30) for 72 h. Cell viability was assessed by MTT assay. ( c ) Cells were treated with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for indicated time points. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei. In ( a-c ) mean and S.D. of three independent experiments performed in triplicate are shown; * P
    Figure Legend Snippet: LSD1 and HDAC inhibitors synergize to induce cell death in RMS cells. ( a ) Cells were treated with indicated concentrations of GSK690 and/or JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei. ( b ) Cells were treated with 1 μ M GSK690 and 15 nM JNJ-26481585 (RD) or 10 μ M GSK690 and 5 nM JNJ-26481585 (RH30) for 72 h. Cell viability was assessed by MTT assay. ( c ) Cells were treated with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for indicated time points. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei. In ( a-c ) mean and S.D. of three independent experiments performed in triplicate are shown; * P

    Techniques Used: Flow Cytometry, Staining, MTT Assay

    Overexpression of BCL-2 or MCL-1 reduces GSK690/JNJ-26481585-induced apoptosis. ( a ) RD and RH30 were transfected with empty vector (EV) or a vector containing a murine BCL-2 construct (mBCL-2). Expression of BCL-2 was assessed by Western blotting, asterisks indicate empty lanes. GAPDH was used as loading control. ( b ) Cells were treated with 1 μ M GSK690 (RD cells) or 5 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). ( c ) Cells were treated with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 36 h (RD) or 24 h (RH30). Cell viability was assessed with MTT assay. ( d ) Cells were transfected with EV, wild-type MCL-1 (WT) or phospho-mutant MCL-1 (4A) constructs. Ectopic expression of MCL-1 constructs was detected by Western blotting, β-Actin served as loading control. ( e ) Transfected cells were treated with 1 μ M GSK690 (RD cells) or 5 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). In ( b,c,e ) mean and S.D. of three independent experiments performed in triplicate are shown; * P
    Figure Legend Snippet: Overexpression of BCL-2 or MCL-1 reduces GSK690/JNJ-26481585-induced apoptosis. ( a ) RD and RH30 were transfected with empty vector (EV) or a vector containing a murine BCL-2 construct (mBCL-2). Expression of BCL-2 was assessed by Western blotting, asterisks indicate empty lanes. GAPDH was used as loading control. ( b ) Cells were treated with 1 μ M GSK690 (RD cells) or 5 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). ( c ) Cells were treated with 1 μ M GSK690 (RD cells) or 10 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 36 h (RD) or 24 h (RH30). Cell viability was assessed with MTT assay. ( d ) Cells were transfected with EV, wild-type MCL-1 (WT) or phospho-mutant MCL-1 (4A) constructs. Ectopic expression of MCL-1 constructs was detected by Western blotting, β-Actin served as loading control. ( e ) Transfected cells were treated with 1 μ M GSK690 (RD cells) or 5 μ M GSK690 (RH30 cells) and/or 15 nM JNJ-26481585 for 72 h. Cell death was determined by flow cytometric analysis of DNA fragmentation of PI-stained nuclei (RD cells) or fluorescence-based microscope analysis of PI uptake using Hoechst 33342 and PI double staining (RH30 cells). In ( b,c,e ) mean and S.D. of three independent experiments performed in triplicate are shown; * P

    Techniques Used: Over Expression, Transfection, Plasmid Preparation, Construct, Expressing, Western Blot, Flow Cytometry, Staining, Fluorescence, Microscopy, Double Staining, MTT Assay, Mutagenesis

    5) Product Images from "Epstein-Barr Virus (EBV) Latent Membrane Protein 2A Regulates B-Cell Receptor-Induced Apoptosis and EBV Reactivation through Tyrosine Phosphorylation"

    Article Title: Epstein-Barr Virus (EBV) Latent Membrane Protein 2A Regulates B-Cell Receptor-Induced Apoptosis and EBV Reactivation through Tyrosine Phosphorylation

    Journal: Journal of Virology

    doi: 10.1128/JVI.79.13.8655-8660.2005

    LMP2A or genistein inhibits BCR-induced tyrosine phosphorylation, DNA fragmentation, and cleavage PARP in Ramos cells. (A) Parental (P), vector control (V), and LMP2A-expressing (2A) Ramos cells (1 × 10 6 /ml) were treated without (control [−])
    Figure Legend Snippet: LMP2A or genistein inhibits BCR-induced tyrosine phosphorylation, DNA fragmentation, and cleavage PARP in Ramos cells. (A) Parental (P), vector control (V), and LMP2A-expressing (2A) Ramos cells (1 × 10 6 /ml) were treated without (control [−])

    Techniques Used: Plasmid Preparation, Expressing

    LMP2A inhibits BCR-induced DNA fragmentation and cleavage of PARP in Ramos cells. (A) Cells were seeded at 3 × 10 5 cells/ml, and cells were treated without (control) or with 35 μg/ml anti-IgM antibody (αIgAb) for 24 h or 48 h.
    Figure Legend Snippet: LMP2A inhibits BCR-induced DNA fragmentation and cleavage of PARP in Ramos cells. (A) Cells were seeded at 3 × 10 5 cells/ml, and cells were treated without (control) or with 35 μg/ml anti-IgM antibody (αIgAb) for 24 h or 48 h.

    Techniques Used:

    LMP2A or genistein blocks BCR-induced DNA fragmentation, cleavage of PARP, and EBV reactivation. (A) DNA fragmentation and evaluation of cleavage of PARP. Parental (P), vector control (V), and LMP2A-expressing (2A) Akata cells (5 × 10 5 /ml) were
    Figure Legend Snippet: LMP2A or genistein blocks BCR-induced DNA fragmentation, cleavage of PARP, and EBV reactivation. (A) DNA fragmentation and evaluation of cleavage of PARP. Parental (P), vector control (V), and LMP2A-expressing (2A) Akata cells (5 × 10 5 /ml) were

    Techniques Used: Plasmid Preparation, Expressing

    6) Product Images from "Epstein-Barr Virus (EBV) Latent Membrane Protein 2A Regulates B-Cell Receptor-Induced Apoptosis and EBV Reactivation through Tyrosine Phosphorylation"

    Article Title: Epstein-Barr Virus (EBV) Latent Membrane Protein 2A Regulates B-Cell Receptor-Induced Apoptosis and EBV Reactivation through Tyrosine Phosphorylation

    Journal: Journal of Virology

    doi: 10.1128/JVI.79.13.8655-8660.2005

    LMP2A or genistein inhibits BCR-induced tyrosine phosphorylation, DNA fragmentation, and cleavage PARP in Ramos cells. (A) Parental (P), vector control (V), and LMP2A-expressing (2A) Ramos cells (1 × 10 6 /ml) were treated without (control [−])
    Figure Legend Snippet: LMP2A or genistein inhibits BCR-induced tyrosine phosphorylation, DNA fragmentation, and cleavage PARP in Ramos cells. (A) Parental (P), vector control (V), and LMP2A-expressing (2A) Ramos cells (1 × 10 6 /ml) were treated without (control [−])

    Techniques Used: Plasmid Preparation, Expressing

    LMP2A inhibits BCR-induced DNA fragmentation and cleavage of PARP in Ramos cells. (A) Cells were seeded at 3 × 10 5 cells/ml, and cells were treated without (control) or with 35 μg/ml anti-IgM antibody (αIgAb) for 24 h or 48 h.
    Figure Legend Snippet: LMP2A inhibits BCR-induced DNA fragmentation and cleavage of PARP in Ramos cells. (A) Cells were seeded at 3 × 10 5 cells/ml, and cells were treated without (control) or with 35 μg/ml anti-IgM antibody (αIgAb) for 24 h or 48 h.

    Techniques Used:

    LMP2A or genistein blocks BCR-induced DNA fragmentation, cleavage of PARP, and EBV reactivation. (A) DNA fragmentation and evaluation of cleavage of PARP. Parental (P), vector control (V), and LMP2A-expressing (2A) Akata cells (5 × 10 5 /ml) were
    Figure Legend Snippet: LMP2A or genistein blocks BCR-induced DNA fragmentation, cleavage of PARP, and EBV reactivation. (A) DNA fragmentation and evaluation of cleavage of PARP. Parental (P), vector control (V), and LMP2A-expressing (2A) Akata cells (5 × 10 5 /ml) were

    Techniques Used: Plasmid Preparation, Expressing

    7) Product Images from "TNF-α and IFN-γ Together Up-Regulates Par-4 Expression and Induce Apoptosis in Human Neuroblastomas"

    Article Title: TNF-α and IFN-γ Together Up-Regulates Par-4 Expression and Induce Apoptosis in Human Neuroblastomas

    Journal: Biomedicines

    doi: 10.3390/biomedicines6010004

    Combination of IFN-γ (interferon gamma) and TNF-α (tumor necrosis factor-alpha) enhances apoptosis in SK-N-MC cells. Cells were treated with IFN-γ (10 ng/mL) and TNF-α 20 ng/mL) alone and in combination for 48 h, and analyzed for apoptosis: ( A ) hypodiploid population by flow-cytometry; ( B ) DNA fragmentation; ( C ) Poly (ADP-ribose)polymerase (PARP) cleavage by immunoblotting; and ( D ) Casapase-8 activity assay. The figures are representative of 2 similar experiments.
    Figure Legend Snippet: Combination of IFN-γ (interferon gamma) and TNF-α (tumor necrosis factor-alpha) enhances apoptosis in SK-N-MC cells. Cells were treated with IFN-γ (10 ng/mL) and TNF-α 20 ng/mL) alone and in combination for 48 h, and analyzed for apoptosis: ( A ) hypodiploid population by flow-cytometry; ( B ) DNA fragmentation; ( C ) Poly (ADP-ribose)polymerase (PARP) cleavage by immunoblotting; and ( D ) Casapase-8 activity assay. The figures are representative of 2 similar experiments.

    Techniques Used: Flow Cytometry, Cytometry, Activity Assay

    8) Product Images from "Divergent Effects of Dioxin- or Non-Dioxin-Like Polychlorinated Biphenyls on the Apoptosis of Primary Cell Culture from the Mouse Pituitary Gland"

    Article Title: Divergent Effects of Dioxin- or Non-Dioxin-Like Polychlorinated Biphenyls on the Apoptosis of Primary Cell Culture from the Mouse Pituitary Gland

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0146729

    Evaluation of apoptosis induced by ROS production. Quantitative ROS generation was measured using the oxidant-sensitive probe dichlorofluorescein (H2DCF-DA) assay (A), apoptosis was evaluated by ELISA DNA fragmentation assay (B), and caspase-3 activity was determined by fluorimetric assay (C), as described in the Materials and Methods. Pituitary primary cells were treated as described in the study design. 10 μM Hydrogen Peroxide (H 2 O 2 ) (A), 50 μM H 2 O 2 (B, C), or 32 μM Cisplatin (B,C) were used as positive controls. In all the assays, 1 mM Ascorbic Acid (vitamin C) was used as an antioxidant. ROS production was not influenced by non-dioxin-like PCB 180 or PCB 153, with or without the addition of vitamin C (A). Moreover, vitamin C had no effect on either apoptosis or caspase-3 activity of PCBs-treated pituitary cells (B, C), suggesting that ROS do not play a key role in PCBs-mediated apoptosis mechanism. Results represent the mean ± SD of five independent experiments, each performed in quadruplicate and expressed as arbitrary units (A.U.). The value of 1 was assigned to ROS production (A), DNA fragmentation (B) or caspase-3 activity (C) from vehicle-exposed cells. **, p
    Figure Legend Snippet: Evaluation of apoptosis induced by ROS production. Quantitative ROS generation was measured using the oxidant-sensitive probe dichlorofluorescein (H2DCF-DA) assay (A), apoptosis was evaluated by ELISA DNA fragmentation assay (B), and caspase-3 activity was determined by fluorimetric assay (C), as described in the Materials and Methods. Pituitary primary cells were treated as described in the study design. 10 μM Hydrogen Peroxide (H 2 O 2 ) (A), 50 μM H 2 O 2 (B, C), or 32 μM Cisplatin (B,C) were used as positive controls. In all the assays, 1 mM Ascorbic Acid (vitamin C) was used as an antioxidant. ROS production was not influenced by non-dioxin-like PCB 180 or PCB 153, with or without the addition of vitamin C (A). Moreover, vitamin C had no effect on either apoptosis or caspase-3 activity of PCBs-treated pituitary cells (B, C), suggesting that ROS do not play a key role in PCBs-mediated apoptosis mechanism. Results represent the mean ± SD of five independent experiments, each performed in quadruplicate and expressed as arbitrary units (A.U.). The value of 1 was assigned to ROS production (A), DNA fragmentation (B) or caspase-3 activity (C) from vehicle-exposed cells. **, p

    Techniques Used: Enzyme-linked Immunosorbent Assay, DNA Fragmentation Assay, Activity Assay, Fluorimetry Assay

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    Article Snippet: The secondary antibody binding was detected by ECL Plus chemiluminescent reagents and analyzed by Storm image analysis systems (GE Healthcare Biosciences, Piscataway, NJ). .. Apoptosis Apoptosis was determined by DNA fragmentation using ApoDirect TUNEL assay kit from Millipore (Billerica, MA) based on supplier’s instruction. .. Briefly, 106 Cells were incubated with increasing concentrations of rhArg for 36 h. Afterwards, DNA breaks were fluorescently labeled with fluorescein isothiocyanate, and cells were analyzed by FACScan flow cytometer (Becton Dickinson Biosciences, San Jose, CA) using Cell Quest Pro software.

    Article Title: Toll-like receptor 2 signaling is a mediator of apoptosis in herpes simplex virus-infected microglia
    Article Snippet: .. TUNEL staining Wild type and TLR2-/- microglial cells were infected with HSV (MOI = 2) and DNA fragmentation was determined by terminal deoxynucleotidyl transferase (TdT)-mediated dUTP-X nick end labeling (TUNEL) using the ApopTag ® peroxidasein situ apoptosis detection kit (Millipore, Temecula, CA). .. Microglial cells were cultured on Lab-Tek chamber slides at a density of 2 × 105 cells per well.

    Article Title: Protective Actions of Ovarian Hormones In the Serotonin System of Macaques
    Article Snippet: .. For the in situ analysis of DNA fragmentation, the TUNEL staining was performed on sections from perfused brains that were mounted, dried and stored at −80C using a commercial kit (Apopka Kit-S7100, Chemicon, Temecula, CA) according to the directions of the manufacturer. ..

    In Situ:

    Article Title: Ovarian Steroids Decrease DNA Fragmentation In Serotonin Neurons of Non-injured Rhesus Macaques
    Article Snippet: Sections (25 μm) were cut on a sliding microtome, mounted on Super Frost plus slides (Fisher Scientific, Pittsburgh, PA), dehydrated under vacuum and then frozen at −80°C until processing for TUNEL assay. .. TUNEL assay For the in situ analysis of DNA fragmentation, the TUNEL staining was performed using a commercial kit (ApopTag Kit-S7100, Chemicon, Temecula, CA). .. Briefly, frozen sections were post-fixed with 1% paraformaldehyde for 15 min followed by a cold solution of ethanol: acetic acid (2:1) for 5 min. Then the slides were washed 2 times with 50 mM phosphate buffer saline (PBS), immersed in 0.5% triton for 15 min, washed 2 times, digested with proteinase K (20 μg/ml) for 15 min and endogenous peroxidase was quenched with 3% H2 O2 for 20 min. After 2 washings, the sections were incubated with TdT enzyme at 37°C for 90 min.

    Article Title: Protective Actions of Ovarian Hormones In the Serotonin System of Macaques
    Article Snippet: .. For the in situ analysis of DNA fragmentation, the TUNEL staining was performed on sections from perfused brains that were mounted, dried and stored at −80C using a commercial kit (Apopka Kit-S7100, Chemicon, Temecula, CA) according to the directions of the manufacturer. ..

    Staining:

    Article Title: Ovarian Steroids Decrease DNA Fragmentation In Serotonin Neurons of Non-injured Rhesus Macaques
    Article Snippet: Sections (25 μm) were cut on a sliding microtome, mounted on Super Frost plus slides (Fisher Scientific, Pittsburgh, PA), dehydrated under vacuum and then frozen at −80°C until processing for TUNEL assay. .. TUNEL assay For the in situ analysis of DNA fragmentation, the TUNEL staining was performed using a commercial kit (ApopTag Kit-S7100, Chemicon, Temecula, CA). .. Briefly, frozen sections were post-fixed with 1% paraformaldehyde for 15 min followed by a cold solution of ethanol: acetic acid (2:1) for 5 min. Then the slides were washed 2 times with 50 mM phosphate buffer saline (PBS), immersed in 0.5% triton for 15 min, washed 2 times, digested with proteinase K (20 μg/ml) for 15 min and endogenous peroxidase was quenched with 3% H2 O2 for 20 min. After 2 washings, the sections were incubated with TdT enzyme at 37°C for 90 min.

    Article Title: Toll-like receptor 2 signaling is a mediator of apoptosis in herpes simplex virus-infected microglia
    Article Snippet: .. TUNEL staining Wild type and TLR2-/- microglial cells were infected with HSV (MOI = 2) and DNA fragmentation was determined by terminal deoxynucleotidyl transferase (TdT)-mediated dUTP-X nick end labeling (TUNEL) using the ApopTag ® peroxidasein situ apoptosis detection kit (Millipore, Temecula, CA). .. Microglial cells were cultured on Lab-Tek chamber slides at a density of 2 × 105 cells per well.

    Article Title: Protective Actions of Ovarian Hormones In the Serotonin System of Macaques
    Article Snippet: .. For the in situ analysis of DNA fragmentation, the TUNEL staining was performed on sections from perfused brains that were mounted, dried and stored at −80C using a commercial kit (Apopka Kit-S7100, Chemicon, Temecula, CA) according to the directions of the manufacturer. ..

    Isolation:

    Article Title: TNF-α and IFN-γ Together Up-Regulates Par-4 Expression and Induce Apoptosis in Human Neuroblastomas
    Article Snippet: DNA Fragmentation Assay DNA fragmentation assays were performed to determine the apoptosis on combination treatment. .. SK-N-MC cells (5 × 106 ) were treated with combination of TNF-α (20 ng/mL) and IFN-γ (10 ng/mL) for 48 h. DNA was isolated, and DNA fragmentation was assessed (Suicide-Track™ DNA Ladder Isolation Kit Cat # AM41, Calbiochem, San Diego, CA, USA) and loaded on a 1.5% agarose gels. .. The gels were stained with 0.5 μg/mL ethidium bromides for 15 min and visualized using a gel-documentation system.

    Ligation:

    Article Title: Epstein-Barr Virus (EBV) Latent Membrane Protein 2A Regulates B-Cell Receptor-Induced Apoptosis and EBV Reactivation through Tyrosine Phosphorylation
    Article Snippet: .. To verify the DNA fragmentation and cleavage of PARP by BCR ligation were dependent on caspase activity in Ramos cells, cells were pretreated with zVAD-fmk (Calbiochem, La Jolla, CA), a broad caspase inhibitor and, as expected, DNA fragmentation and PARP cleavage were blocked by the addition of zVAD-fmk (Fig. and ). .. We next examined the mechanism of inhibition of BCR-induced apoptosis by LMP2A.

    Activity Assay:

    Article Title: Epstein-Barr Virus (EBV) Latent Membrane Protein 2A Regulates B-Cell Receptor-Induced Apoptosis and EBV Reactivation through Tyrosine Phosphorylation
    Article Snippet: .. To verify the DNA fragmentation and cleavage of PARP by BCR ligation were dependent on caspase activity in Ramos cells, cells were pretreated with zVAD-fmk (Calbiochem, La Jolla, CA), a broad caspase inhibitor and, as expected, DNA fragmentation and PARP cleavage were blocked by the addition of zVAD-fmk (Fig. and ). .. We next examined the mechanism of inhibition of BCR-induced apoptosis by LMP2A.

    Infection:

    Article Title: Toll-like receptor 2 signaling is a mediator of apoptosis in herpes simplex virus-infected microglia
    Article Snippet: .. TUNEL staining Wild type and TLR2-/- microglial cells were infected with HSV (MOI = 2) and DNA fragmentation was determined by terminal deoxynucleotidyl transferase (TdT)-mediated dUTP-X nick end labeling (TUNEL) using the ApopTag ® peroxidasein situ apoptosis detection kit (Millipore, Temecula, CA). .. Microglial cells were cultured on Lab-Tek chamber slides at a density of 2 × 105 cells per well.

    End Labeling:

    Article Title: Toll-like receptor 2 signaling is a mediator of apoptosis in herpes simplex virus-infected microglia
    Article Snippet: .. TUNEL staining Wild type and TLR2-/- microglial cells were infected with HSV (MOI = 2) and DNA fragmentation was determined by terminal deoxynucleotidyl transferase (TdT)-mediated dUTP-X nick end labeling (TUNEL) using the ApopTag ® peroxidasein situ apoptosis detection kit (Millipore, Temecula, CA). .. Microglial cells were cultured on Lab-Tek chamber slides at a density of 2 × 105 cells per well.

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  • 99
    Millipore dna fragment
    PCR and Southern blot experiments showed that group II <t>intron-based</t> vectors efficiently targeted the Clostridium cellulolyticum mdh and ldh genes in pure cultures . (A) Primers MdhF/intronR1 (5' junction) and intronF1/MdhR (3' junction) produced bands from the Ccel_0137 mutant cells (lanes 1 and 2) but not from wild-type (lanes 4 and 5). Primers MdhF/MdhR amplified a single band from the mutant (lane 3) that is 915 bp larger than the wild-type (lane 6). (B) Primers LdhF/intronR1 (5' junction) and intronF1/LdhR (3' junction) produced bands in the Ccel_2485 mutant cells (lanes 1 and 2) but not in the wild-type (lanes 4 and 5). Primers LdhF/LdhR, amplified a single band from the mutant (lane 3), which is 915 bp larger than the wild-type (lane 6). (C) Amplifications using plasmid-specific primers pWH199F2 and pintronR1 confirmed plasmid curing. Lane 1, positive control (plasmid); lane 2, Ccel_0137 mutant; lane 3, Ccel_2485 mutant; lane 4, negative control. (D) Amplification from wild-type <t>DNA</t> using primers LdhF-R (lane 1) and MdhF-R (lane 2) produced low molecular weight products. Genes containing insertions were amplified from the ldh mutant using primers LdhF-R (lane 3) and from the mdh mutant using primers MdhF-R (lane 4), producing larger products. The same size PCR products were obtained in amplifications from ldh mdh mutant DNA using primers LdhF-R (lane 5) and MdhF-R (lane 6). (E) A Southern blot using an intron-specific probe confirmed the intron insertions in DNA digested with Eco RI. No band was detected in the chromosomal DNA of wild-type cells (lane 1), while two bands in the ldh mdh mutant (lane 2) correspond to bands in the ldh mutant (lane 3) and the mdh mutant (lane 4). No band corresponding to the plasmid (lane 5) was identified in any of the plasmid-cured strains.
    Dna Fragment, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore dna fragmentation
    HSV infection induces apoptosis in murine microglial cells. Wild-type and <t>TLR2</t> -/- C57BL/6 microglial cells were infected with HSV at a MOI of 2. (A) The cells were examined for apoptotic <t>DNA</t> fragmentation using an oligonucleosomal ELISA at 8 and 24 h p.i. Data are presented as optical density (OD) per 10 4 cells and are representative of three independent experiments using cells isolated from different brain specimens. (B) TUNEL staining of wild-type and TLR2 -/- microglia at 24 h p.i. After fixing and staining the wells, TUNEL positive cells from at least five fields were counted for each well. Data presented were representative of three independent experiments.
    Dna Fragmentation, supplied by Millipore, 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/dna fragmentation/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dna fragmentation - by Bioz Stars, 2021-04
    99/100 stars
      Buy from Supplier

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    PCR and Southern blot experiments showed that group II intron-based vectors efficiently targeted the Clostridium cellulolyticum mdh and ldh genes in pure cultures . (A) Primers MdhF/intronR1 (5' junction) and intronF1/MdhR (3' junction) produced bands from the Ccel_0137 mutant cells (lanes 1 and 2) but not from wild-type (lanes 4 and 5). Primers MdhF/MdhR amplified a single band from the mutant (lane 3) that is 915 bp larger than the wild-type (lane 6). (B) Primers LdhF/intronR1 (5' junction) and intronF1/LdhR (3' junction) produced bands in the Ccel_2485 mutant cells (lanes 1 and 2) but not in the wild-type (lanes 4 and 5). Primers LdhF/LdhR, amplified a single band from the mutant (lane 3), which is 915 bp larger than the wild-type (lane 6). (C) Amplifications using plasmid-specific primers pWH199F2 and pintronR1 confirmed plasmid curing. Lane 1, positive control (plasmid); lane 2, Ccel_0137 mutant; lane 3, Ccel_2485 mutant; lane 4, negative control. (D) Amplification from wild-type DNA using primers LdhF-R (lane 1) and MdhF-R (lane 2) produced low molecular weight products. Genes containing insertions were amplified from the ldh mutant using primers LdhF-R (lane 3) and from the mdh mutant using primers MdhF-R (lane 4), producing larger products. The same size PCR products were obtained in amplifications from ldh mdh mutant DNA using primers LdhF-R (lane 5) and MdhF-R (lane 6). (E) A Southern blot using an intron-specific probe confirmed the intron insertions in DNA digested with Eco RI. No band was detected in the chromosomal DNA of wild-type cells (lane 1), while two bands in the ldh mdh mutant (lane 2) correspond to bands in the ldh mutant (lane 3) and the mdh mutant (lane 4). No band corresponding to the plasmid (lane 5) was identified in any of the plasmid-cured strains.

    Journal: Biotechnology for Biofuels

    Article Title: Combined inactivation of the Clostridium cellulolyticum lactate and malate dehydrogenase genes substantially increases ethanol yield from cellulose and switchgrass fermentations

    doi: 10.1186/1754-6834-5-2

    Figure Lengend Snippet: PCR and Southern blot experiments showed that group II intron-based vectors efficiently targeted the Clostridium cellulolyticum mdh and ldh genes in pure cultures . (A) Primers MdhF/intronR1 (5' junction) and intronF1/MdhR (3' junction) produced bands from the Ccel_0137 mutant cells (lanes 1 and 2) but not from wild-type (lanes 4 and 5). Primers MdhF/MdhR amplified a single band from the mutant (lane 3) that is 915 bp larger than the wild-type (lane 6). (B) Primers LdhF/intronR1 (5' junction) and intronF1/LdhR (3' junction) produced bands in the Ccel_2485 mutant cells (lanes 1 and 2) but not in the wild-type (lanes 4 and 5). Primers LdhF/LdhR, amplified a single band from the mutant (lane 3), which is 915 bp larger than the wild-type (lane 6). (C) Amplifications using plasmid-specific primers pWH199F2 and pintronR1 confirmed plasmid curing. Lane 1, positive control (plasmid); lane 2, Ccel_0137 mutant; lane 3, Ccel_2485 mutant; lane 4, negative control. (D) Amplification from wild-type DNA using primers LdhF-R (lane 1) and MdhF-R (lane 2) produced low molecular weight products. Genes containing insertions were amplified from the ldh mutant using primers LdhF-R (lane 3) and from the mdh mutant using primers MdhF-R (lane 4), producing larger products. The same size PCR products were obtained in amplifications from ldh mdh mutant DNA using primers LdhF-R (lane 5) and MdhF-R (lane 6). (E) A Southern blot using an intron-specific probe confirmed the intron insertions in DNA digested with Eco RI. No band was detected in the chromosomal DNA of wild-type cells (lane 1), while two bands in the ldh mdh mutant (lane 2) correspond to bands in the ldh mutant (lane 3) and the mdh mutant (lane 4). No band corresponding to the plasmid (lane 5) was identified in any of the plasmid-cured strains.

    Article Snippet: To insert the intron into pWH199 downstream of a Clostridium pasteurianum ferredoxin (Fd) promoter [ ], a DNA fragment containing the intron and ltrA was amplified from pJIR750ai (Sigma-Aldrich, St. Louis, MO) by PCR using primers pJIR750aiXmaIF and pJIR750aiXhoIR (Additional file ).

    Techniques: Polymerase Chain Reaction, Southern Blot, Produced, Mutagenesis, Amplification, Plasmid Preparation, Positive Control, Negative Control, Molecular Weight

    DNA cleavage by SfiI. ( A ) Successive time-lapse images of a SfiI-DNA reaction obtained at 2.0 fps in the presence of Mg 2+ . The elapsed time is indicated in each image. The image is cropped from the original scan size of 600 nm × 450 nm.

    Journal: Biophysical Journal

    Article Title: Visual Analysis of Concerted Cleavage by Type IIF Restriction Enzyme SfiI in Subsecond Time Region

    doi: 10.1016/j.bpj.2011.09.064

    Figure Lengend Snippet: DNA cleavage by SfiI. ( A ) Successive time-lapse images of a SfiI-DNA reaction obtained at 2.0 fps in the presence of Mg 2+ . The elapsed time is indicated in each image. The image is cropped from the original scan size of 600 nm × 450 nm.

    Article Snippet: Reaction mixtures contained 0.004 units of SfiI, 5 ng/ μ l DNA fragment (905 bp), 10 mM HEPES (pH 7.5), 5 mM CaCl2 , and 50 mM NaCl in a total volume of 10 μ l. After incubating at an ambient temperature for 15 min, the complexes were filtered through a Montage PCR column (Millipore, Bedford, MA) to remove bovine serum albumin, and unbound protein.

    Techniques:

    Looping and translocation by SfiI. Successive time-lapse images of a SfiI-DNA complex obtained at 1.0 fps in the presence of Ca 2+ . The elapsed time is shown in each image. The image is cropped from the original scan size of 600 nm × 450 nm.

    Journal: Biophysical Journal

    Article Title: Visual Analysis of Concerted Cleavage by Type IIF Restriction Enzyme SfiI in Subsecond Time Region

    doi: 10.1016/j.bpj.2011.09.064

    Figure Lengend Snippet: Looping and translocation by SfiI. Successive time-lapse images of a SfiI-DNA complex obtained at 1.0 fps in the presence of Ca 2+ . The elapsed time is shown in each image. The image is cropped from the original scan size of 600 nm × 450 nm.

    Article Snippet: Reaction mixtures contained 0.004 units of SfiI, 5 ng/ μ l DNA fragment (905 bp), 10 mM HEPES (pH 7.5), 5 mM CaCl2 , and 50 mM NaCl in a total volume of 10 μ l. After incubating at an ambient temperature for 15 min, the complexes were filtered through a Montage PCR column (Millipore, Bedford, MA) to remove bovine serum albumin, and unbound protein.

    Techniques: Translocation Assay

    DNA and protein movement on a mica surface. ( A . SfiI tetramers were indicated by yellow arrowheads. AFM imaging was performed in the presence of Ca 2+ . ( B ) Movement of DNA strands on a mica. The contours of four individual

    Journal: Biophysical Journal

    Article Title: Visual Analysis of Concerted Cleavage by Type IIF Restriction Enzyme SfiI in Subsecond Time Region

    doi: 10.1016/j.bpj.2011.09.064

    Figure Lengend Snippet: DNA and protein movement on a mica surface. ( A . SfiI tetramers were indicated by yellow arrowheads. AFM imaging was performed in the presence of Ca 2+ . ( B ) Movement of DNA strands on a mica. The contours of four individual

    Article Snippet: Reaction mixtures contained 0.004 units of SfiI, 5 ng/ μ l DNA fragment (905 bp), 10 mM HEPES (pH 7.5), 5 mM CaCl2 , and 50 mM NaCl in a total volume of 10 μ l. After incubating at an ambient temperature for 15 min, the complexes were filtered through a Montage PCR column (Millipore, Bedford, MA) to remove bovine serum albumin, and unbound protein.

    Techniques: Imaging

    Visualization of SfiI-DNA complex. ( A ) The locations of the two SfiI recognition sites along a 905 bp fragment are shown. ( B ) AFM image of SfiI-DNA complex obtained under a Ca 2+ -containing buffer. Loop and short arms are indicated by yellow and

    Journal: Biophysical Journal

    Article Title: Visual Analysis of Concerted Cleavage by Type IIF Restriction Enzyme SfiI in Subsecond Time Region

    doi: 10.1016/j.bpj.2011.09.064

    Figure Lengend Snippet: Visualization of SfiI-DNA complex. ( A ) The locations of the two SfiI recognition sites along a 905 bp fragment are shown. ( B ) AFM image of SfiI-DNA complex obtained under a Ca 2+ -containing buffer. Loop and short arms are indicated by yellow and

    Article Snippet: Reaction mixtures contained 0.004 units of SfiI, 5 ng/ μ l DNA fragment (905 bp), 10 mM HEPES (pH 7.5), 5 mM CaCl2 , and 50 mM NaCl in a total volume of 10 μ l. After incubating at an ambient temperature for 15 min, the complexes were filtered through a Montage PCR column (Millipore, Bedford, MA) to remove bovine serum albumin, and unbound protein.

    Techniques:

    HSV infection induces apoptosis in murine microglial cells. Wild-type and TLR2 -/- C57BL/6 microglial cells were infected with HSV at a MOI of 2. (A) The cells were examined for apoptotic DNA fragmentation using an oligonucleosomal ELISA at 8 and 24 h p.i. Data are presented as optical density (OD) per 10 4 cells and are representative of three independent experiments using cells isolated from different brain specimens. (B) TUNEL staining of wild-type and TLR2 -/- microglia at 24 h p.i. After fixing and staining the wells, TUNEL positive cells from at least five fields were counted for each well. Data presented were representative of three independent experiments.

    Journal: Journal of Neuroinflammation

    Article Title: Toll-like receptor 2 signaling is a mediator of apoptosis in herpes simplex virus-infected microglia

    doi: 10.1186/1742-2094-4-11

    Figure Lengend Snippet: HSV infection induces apoptosis in murine microglial cells. Wild-type and TLR2 -/- C57BL/6 microglial cells were infected with HSV at a MOI of 2. (A) The cells were examined for apoptotic DNA fragmentation using an oligonucleosomal ELISA at 8 and 24 h p.i. Data are presented as optical density (OD) per 10 4 cells and are representative of three independent experiments using cells isolated from different brain specimens. (B) TUNEL staining of wild-type and TLR2 -/- microglia at 24 h p.i. After fixing and staining the wells, TUNEL positive cells from at least five fields were counted for each well. Data presented were representative of three independent experiments.

    Article Snippet: TUNEL staining Wild type and TLR2-/- microglial cells were infected with HSV (MOI = 2) and DNA fragmentation was determined by terminal deoxynucleotidyl transferase (TdT)-mediated dUTP-X nick end labeling (TUNEL) using the ApopTag ® peroxidasein situ apoptosis detection kit (Millipore, Temecula, CA).

    Techniques: Infection, Enzyme-linked Immunosorbent Assay, Isolation, TUNEL Assay, Staining