antibody h2ax  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antibody h2ax
    ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone <t>(γ-H2AX)</t> was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.
    Antibody H2ax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibody h2ax/product/Cell Signaling Technology Inc
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibody h2ax - by Bioz Stars, 2023-10
    96/100 stars

    Images

    1) Product Images from "D-Serine reduces the expression of the cytopathic genotoxin colibactin"

    Article Title: D-Serine reduces the expression of the cytopathic genotoxin colibactin

    Journal: Microbial Cell

    doi: 10.15698/mic2023.03.793

    ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone (γ-H2AX) was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.
    Figure Legend Snippet: ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone (γ-H2AX) was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.

    Techniques Used: Cell Culture, Plasmid Preparation, Activity Assay, Electrophoresis, Migration, Marker, Infection, Western Blot, Software

    HeLa cells were infected for 4 h with E. coli Nissle 1917 or DH10B hosting BAC- pks (MOI = 400). Infections were performed with and without the addition of 1 mM D-Serine to the growth media. At 8 h post infection, cells were washed, fixed, and stained with anti-γ-H2AX antibody. (A) Cells were examined by confocal microscopy for DNA in cyan and phosphorylated histone H2AX protein in magenta. Images of uninfected, and pks + infected cells are shown, scale bar = 50 μm. (B) Intracellular levels of phosphorylated histone H2AX were measured by flow cytometry 8 h after infection. Dot plots reveal the percentage of viable cells fluorescing in the γ-H2AX channel, 100k events were analysed for each sample.
    Figure Legend Snippet: HeLa cells were infected for 4 h with E. coli Nissle 1917 or DH10B hosting BAC- pks (MOI = 400). Infections were performed with and without the addition of 1 mM D-Serine to the growth media. At 8 h post infection, cells were washed, fixed, and stained with anti-γ-H2AX antibody. (A) Cells were examined by confocal microscopy for DNA in cyan and phosphorylated histone H2AX protein in magenta. Images of uninfected, and pks + infected cells are shown, scale bar = 50 μm. (B) Intracellular levels of phosphorylated histone H2AX were measured by flow cytometry 8 h after infection. Dot plots reveal the percentage of viable cells fluorescing in the γ-H2AX channel, 100k events were analysed for each sample.

    Techniques Used: Infection, Staining, Confocal Microscopy, Flow Cytometry

    Generation of an isogenic mutant, Nissle Δ dsdC, revealed that D-Serine-associated repression of colibactin activity occurred independently of the D-Serine tolerance locus in pks + E. coli strains. (A) Heat map showing the EdgeR calculated log 2 relative fold changes for each gene in the pks island with corresponding colour key adjacent. False discovery rate-corrected P values can be found in Table S1. (B) The genotoxic activity of Nissle Δ dsdC was assessed by infecting HeLa cells as discussed above. Proteins were extracted and the level of H2AX phosphorylation was determined. Immunoblot analysis of cell lysates extracted 4 h post-infection is shown. Anti-γ-H2AX antibody was used as an indicator of double stranded DNA breaks and β-Tubulin was used as a loading control for cell lysates. (C) Signal intensities of bands were measured as described in the methods using LI-COR Image Studio. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, * indicating P < 0.05.
    Figure Legend Snippet: Generation of an isogenic mutant, Nissle Δ dsdC, revealed that D-Serine-associated repression of colibactin activity occurred independently of the D-Serine tolerance locus in pks + E. coli strains. (A) Heat map showing the EdgeR calculated log 2 relative fold changes for each gene in the pks island with corresponding colour key adjacent. False discovery rate-corrected P values can be found in Table S1. (B) The genotoxic activity of Nissle Δ dsdC was assessed by infecting HeLa cells as discussed above. Proteins were extracted and the level of H2AX phosphorylation was determined. Immunoblot analysis of cell lysates extracted 4 h post-infection is shown. Anti-γ-H2AX antibody was used as an indicator of double stranded DNA breaks and β-Tubulin was used as a loading control for cell lysates. (C) Signal intensities of bands were measured as described in the methods using LI-COR Image Studio. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, * indicating P < 0.05.

    Techniques Used: Mutagenesis, Activity Assay, Western Blot, Infection

    rabbit monoclonal anti phospho histone h2ax antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti phospho histone h2ax antibody
    Requirement of Klotho in the reduction of IR-induced DNA damage. (A) Representative images of <t>γ-H2AX</t> foci in HK-2 cells at 0.5 hours after IR. Immunofluorescence staining was performed using anti-γ-H2AX antibodies. Scale bar: 10 μm. γ-H2AX, red. DAPI (DNA), blue. (B) Number of γ-H2AX foci in HK-2 cells at 0.5, 2.0, 8.0 and 24 hours after 1 Gy of IR. (C) Representative images of γ-H2AX foci in parental and KL-GFP-expressing 293 cells at 0.5 hours. Immunofluorescence staining was performed using anti-γ-H2AX antibodies. Scale bar: 10 μm. γ-H2AX, red. DAPI (DNA), blue. (D) Numbers of γ-H2AX foci in parental or KL-GFP-expressing 293 cells at 0.5, 2.0, 8.0 and 24 hours after 1 Gy of IR. Data are shown as mean ± SE of three independent experiments. ** P < 0.01 ( t -test). (E) Representative comet assay images of HK-2 cells with or without X-ray exposure. DNA was stained by SYBR GOLD. (F) The tail moments of HK-2 cells detected by a neutral comet assay after 15 Gy of IR. After IR, the cells were immediately placed on ice, and then 406 cells were analyzed in each experiment. Data are shown as mean ± SE of three independent experiments. ** P < 0.01, *** P < 0.001 ( t -test).
    Rabbit Monoclonal Anti Phospho Histone H2ax Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Klotho protects chromosomal DNA from radiation-induced damage"

    Article Title: Klotho protects chromosomal DNA from radiation-induced damage

    Journal: Journal of Biochemistry

    doi: 10.1093/jb/mvad001

    Requirement of Klotho in the reduction of IR-induced DNA damage. (A) Representative images of γ-H2AX foci in HK-2 cells at 0.5 hours after IR. Immunofluorescence staining was performed using anti-γ-H2AX antibodies. Scale bar: 10 μm. γ-H2AX, red. DAPI (DNA), blue. (B) Number of γ-H2AX foci in HK-2 cells at 0.5, 2.0, 8.0 and 24 hours after 1 Gy of IR. (C) Representative images of γ-H2AX foci in parental and KL-GFP-expressing 293 cells at 0.5 hours. Immunofluorescence staining was performed using anti-γ-H2AX antibodies. Scale bar: 10 μm. γ-H2AX, red. DAPI (DNA), blue. (D) Numbers of γ-H2AX foci in parental or KL-GFP-expressing 293 cells at 0.5, 2.0, 8.0 and 24 hours after 1 Gy of IR. Data are shown as mean ± SE of three independent experiments. ** P < 0.01 ( t -test). (E) Representative comet assay images of HK-2 cells with or without X-ray exposure. DNA was stained by SYBR GOLD. (F) The tail moments of HK-2 cells detected by a neutral comet assay after 15 Gy of IR. After IR, the cells were immediately placed on ice, and then 406 cells were analyzed in each experiment. Data are shown as mean ± SE of three independent experiments. ** P < 0.01, *** P < 0.001 ( t -test).
    Figure Legend Snippet: Requirement of Klotho in the reduction of IR-induced DNA damage. (A) Representative images of γ-H2AX foci in HK-2 cells at 0.5 hours after IR. Immunofluorescence staining was performed using anti-γ-H2AX antibodies. Scale bar: 10 μm. γ-H2AX, red. DAPI (DNA), blue. (B) Number of γ-H2AX foci in HK-2 cells at 0.5, 2.0, 8.0 and 24 hours after 1 Gy of IR. (C) Representative images of γ-H2AX foci in parental and KL-GFP-expressing 293 cells at 0.5 hours. Immunofluorescence staining was performed using anti-γ-H2AX antibodies. Scale bar: 10 μm. γ-H2AX, red. DAPI (DNA), blue. (D) Numbers of γ-H2AX foci in parental or KL-GFP-expressing 293 cells at 0.5, 2.0, 8.0 and 24 hours after 1 Gy of IR. Data are shown as mean ± SE of three independent experiments. ** P < 0.01 ( t -test). (E) Representative comet assay images of HK-2 cells with or without X-ray exposure. DNA was stained by SYBR GOLD. (F) The tail moments of HK-2 cells detected by a neutral comet assay after 15 Gy of IR. After IR, the cells were immediately placed on ice, and then 406 cells were analyzed in each experiment. Data are shown as mean ± SE of three independent experiments. ** P < 0.01, *** P < 0.001 ( t -test).

    Techniques Used: Immunofluorescence, Staining, Expressing, Single Cell Gel Electrophoresis, Neutral Comet Assay

    γ-H2AX in Klotho knockout mice after IR. (A) Klotho immunohistochemical staining of kidney tissues of wild-type (+/+), hetero- ( kl /+) or homo- ( kl/kl ) Klotho knockout mice irradiated by 2 Gy of X-rays. Scale bar: 100 μm. (B) Klotho expression in wild-type (+/+), hetero- ( kl /+) and homo- ( kl/kl ) Klotho knockout mice was quantified by an immunoblotting analysis using anti-Klotho antibodies. The extracts of kidney tissue from the three types of mice were analyzed ( n = 3). (C) Quantification of the Klotho expression shown in (B). The amounts of Klotho were normalized to GAPDH. ** P < 0.01 ( t -test), ( n = 3). (D) γ-H2AX immunohistochemical staining of kidney tissues of wild-type (+/+), hetero- ( kl /+) or homo- ( kl/kl ) Klotho knockout mice after 2 Gy irradiation. Scale bar: 50 μm. (E). Immunoblotting analysis of γ-H2AX using kidney tissue extracts from wild-type (+/+), hetero- ( kl /+) or homo- ( kl/kl ) Klotho knockout mice after 2 Gy irradiation, using anti-γ-H2AX antibodies. Histone H3 was used as a loading control ( n = 3). (F). Quantification of the γ-H2AX shown in (E). The amounts of Klotho were normalized to histone H3. The three types of mice were analyzed ( n = 3).
    Figure Legend Snippet: γ-H2AX in Klotho knockout mice after IR. (A) Klotho immunohistochemical staining of kidney tissues of wild-type (+/+), hetero- ( kl /+) or homo- ( kl/kl ) Klotho knockout mice irradiated by 2 Gy of X-rays. Scale bar: 100 μm. (B) Klotho expression in wild-type (+/+), hetero- ( kl /+) and homo- ( kl/kl ) Klotho knockout mice was quantified by an immunoblotting analysis using anti-Klotho antibodies. The extracts of kidney tissue from the three types of mice were analyzed ( n = 3). (C) Quantification of the Klotho expression shown in (B). The amounts of Klotho were normalized to GAPDH. ** P < 0.01 ( t -test), ( n = 3). (D) γ-H2AX immunohistochemical staining of kidney tissues of wild-type (+/+), hetero- ( kl /+) or homo- ( kl/kl ) Klotho knockout mice after 2 Gy irradiation. Scale bar: 50 μm. (E). Immunoblotting analysis of γ-H2AX using kidney tissue extracts from wild-type (+/+), hetero- ( kl /+) or homo- ( kl/kl ) Klotho knockout mice after 2 Gy irradiation, using anti-γ-H2AX antibodies. Histone H3 was used as a loading control ( n = 3). (F). Quantification of the γ-H2AX shown in (E). The amounts of Klotho were normalized to histone H3. The three types of mice were analyzed ( n = 3).

    Techniques Used: Knock-Out, Immunohistochemical staining, Staining, Irradiation, Expressing, Western Blot

    antibody h2ax  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antibody h2ax
    ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone <t>(γ-H2AX)</t> was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.
    Antibody H2ax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibody h2ax/product/Cell Signaling Technology Inc
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibody h2ax - by Bioz Stars, 2023-10
    96/100 stars

    Images

    1) Product Images from "D-Serine reduces the expression of the cytopathic genotoxin colibactin"

    Article Title: D-Serine reduces the expression of the cytopathic genotoxin colibactin

    Journal: Microbial Cell

    doi: 10.15698/mic2023.03.793

    ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone (γ-H2AX) was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.
    Figure Legend Snippet: ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone (γ-H2AX) was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.

    Techniques Used: Cell Culture, Plasmid Preparation, Activity Assay, Electrophoresis, Migration, Marker, Infection, Western Blot, Software

    HeLa cells were infected for 4 h with E. coli Nissle 1917 or DH10B hosting BAC- pks (MOI = 400). Infections were performed with and without the addition of 1 mM D-Serine to the growth media. At 8 h post infection, cells were washed, fixed, and stained with anti-γ-H2AX antibody. (A) Cells were examined by confocal microscopy for DNA in cyan and phosphorylated histone H2AX protein in magenta. Images of uninfected, and pks + infected cells are shown, scale bar = 50 μm. (B) Intracellular levels of phosphorylated histone H2AX were measured by flow cytometry 8 h after infection. Dot plots reveal the percentage of viable cells fluorescing in the γ-H2AX channel, 100k events were analysed for each sample.
    Figure Legend Snippet: HeLa cells were infected for 4 h with E. coli Nissle 1917 or DH10B hosting BAC- pks (MOI = 400). Infections were performed with and without the addition of 1 mM D-Serine to the growth media. At 8 h post infection, cells were washed, fixed, and stained with anti-γ-H2AX antibody. (A) Cells were examined by confocal microscopy for DNA in cyan and phosphorylated histone H2AX protein in magenta. Images of uninfected, and pks + infected cells are shown, scale bar = 50 μm. (B) Intracellular levels of phosphorylated histone H2AX were measured by flow cytometry 8 h after infection. Dot plots reveal the percentage of viable cells fluorescing in the γ-H2AX channel, 100k events were analysed for each sample.

    Techniques Used: Infection, Staining, Confocal Microscopy, Flow Cytometry

    Generation of an isogenic mutant, Nissle Δ dsdC, revealed that D-Serine-associated repression of colibactin activity occurred independently of the D-Serine tolerance locus in pks + E. coli strains. (A) Heat map showing the EdgeR calculated log 2 relative fold changes for each gene in the pks island with corresponding colour key adjacent. False discovery rate-corrected P values can be found in Table S1. (B) The genotoxic activity of Nissle Δ dsdC was assessed by infecting HeLa cells as discussed above. Proteins were extracted and the level of H2AX phosphorylation was determined. Immunoblot analysis of cell lysates extracted 4 h post-infection is shown. Anti-γ-H2AX antibody was used as an indicator of double stranded DNA breaks and β-Tubulin was used as a loading control for cell lysates. (C) Signal intensities of bands were measured as described in the methods using LI-COR Image Studio. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, * indicating P < 0.05.
    Figure Legend Snippet: Generation of an isogenic mutant, Nissle Δ dsdC, revealed that D-Serine-associated repression of colibactin activity occurred independently of the D-Serine tolerance locus in pks + E. coli strains. (A) Heat map showing the EdgeR calculated log 2 relative fold changes for each gene in the pks island with corresponding colour key adjacent. False discovery rate-corrected P values can be found in Table S1. (B) The genotoxic activity of Nissle Δ dsdC was assessed by infecting HeLa cells as discussed above. Proteins were extracted and the level of H2AX phosphorylation was determined. Immunoblot analysis of cell lysates extracted 4 h post-infection is shown. Anti-γ-H2AX antibody was used as an indicator of double stranded DNA breaks and β-Tubulin was used as a loading control for cell lysates. (C) Signal intensities of bands were measured as described in the methods using LI-COR Image Studio. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, * indicating P < 0.05.

    Techniques Used: Mutagenesis, Activity Assay, Western Blot, Infection

    anti bodies  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti bodies
    Anti Bodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti bodies/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti bodies - by Bioz Stars, 2023-10
    94/100 stars

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    anti γ h2ax primary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti γ h2ax primary antibody
    ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone <t>(γ-H2AX)</t> was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.
    Anti γ H2ax Primary Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "D-Serine reduces the expression of the cytopathic genotoxin colibactin"

    Article Title: D-Serine reduces the expression of the cytopathic genotoxin colibactin

    Journal: Microbial Cell

    doi: 10.15698/mic2023.03.793

    ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone (γ-H2AX) was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.
    Figure Legend Snippet: ( A and B ) Nissle 1917 and CFT073 were cultured for 5 h in M9 minimal media alone (-) or in media supplemented with 1 mM D-Serine (+) before 1.5 × 10 6 CFU was exposed to linearized plasmid DNA for 40 min. The DNA was extracted, and cross-linking activity was determined by electrophoresis in denaturing conditions. (A) DNA cross-link formation of linearized plasmid DNA exposed to Nissle 1917 and CFT073 was visualized after migration under alkaline denaturing conditions. M, DNA size marker (1 kB plus DNA ladder, Invitrogen). (B) The percentage of the DNA signal in the upper, cross-linked band (indicated by the arrow in panel A) relative to the total DNA signal. Signal intensities were quantified using ImageJ for three independent experiments and statistical significance was assessed by unpaired Student's t -test with, * indicating P = < 0.01. ( C and D ) HeLa cells were infected for 4 h with live pks + and pks - E. coli with a multiplicity of infection (MOI) of 400 bacteria per cell or left uninfected. Infections were performed in wells containing MEM-HEPES alone (-) or with media supplemented with 1 mM D-Serine (+). (C) Immunoblot analysis of cell lysates extracted 4 h post infection. Phosphorylated histone (γ-H2AX) was used as an indicator of double stranded DNA breaks and total histone (H2AX) was used as an internal control. β-Tubulin was used as a loading control for cell lysates. DH10B pBAC -pks and DC10B were used as positive and negative controls, respectively. (D) Signal intensities of bands were measured using LI-COR Image Studio software. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the eight samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, ** and *** indicating P < 0.01 and 0.001, respectively.

    Techniques Used: Cell Culture, Plasmid Preparation, Activity Assay, Electrophoresis, Migration, Marker, Infection, Western Blot, Software

    HeLa cells were infected for 4 h with E. coli Nissle 1917 or DH10B hosting BAC- pks (MOI = 400). Infections were performed with and without the addition of 1 mM D-Serine to the growth media. At 8 h post infection, cells were washed, fixed, and stained with anti-γ-H2AX antibody. (A) Cells were examined by confocal microscopy for DNA in cyan and phosphorylated histone H2AX protein in magenta. Images of uninfected, and pks + infected cells are shown, scale bar = 50 μm. (B) Intracellular levels of phosphorylated histone H2AX were measured by flow cytometry 8 h after infection. Dot plots reveal the percentage of viable cells fluorescing in the γ-H2AX channel, 100k events were analysed for each sample.
    Figure Legend Snippet: HeLa cells were infected for 4 h with E. coli Nissle 1917 or DH10B hosting BAC- pks (MOI = 400). Infections were performed with and without the addition of 1 mM D-Serine to the growth media. At 8 h post infection, cells were washed, fixed, and stained with anti-γ-H2AX antibody. (A) Cells were examined by confocal microscopy for DNA in cyan and phosphorylated histone H2AX protein in magenta. Images of uninfected, and pks + infected cells are shown, scale bar = 50 μm. (B) Intracellular levels of phosphorylated histone H2AX were measured by flow cytometry 8 h after infection. Dot plots reveal the percentage of viable cells fluorescing in the γ-H2AX channel, 100k events were analysed for each sample.

    Techniques Used: Infection, Staining, Confocal Microscopy, Flow Cytometry

    Generation of an isogenic mutant, Nissle Δ dsdC, revealed that D-Serine-associated repression of colibactin activity occurred independently of the D-Serine tolerance locus in pks + E. coli strains. (A) Heat map showing the EdgeR calculated log 2 relative fold changes for each gene in the pks island with corresponding colour key adjacent. False discovery rate-corrected P values can be found in Table S1. (B) The genotoxic activity of Nissle Δ dsdC was assessed by infecting HeLa cells as discussed above. Proteins were extracted and the level of H2AX phosphorylation was determined. Immunoblot analysis of cell lysates extracted 4 h post-infection is shown. Anti-γ-H2AX antibody was used as an indicator of double stranded DNA breaks and β-Tubulin was used as a loading control for cell lysates. (C) Signal intensities of bands were measured as described in the methods using LI-COR Image Studio. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, * indicating P < 0.05.
    Figure Legend Snippet: Generation of an isogenic mutant, Nissle Δ dsdC, revealed that D-Serine-associated repression of colibactin activity occurred independently of the D-Serine tolerance locus in pks + E. coli strains. (A) Heat map showing the EdgeR calculated log 2 relative fold changes for each gene in the pks island with corresponding colour key adjacent. False discovery rate-corrected P values can be found in Table S1. (B) The genotoxic activity of Nissle Δ dsdC was assessed by infecting HeLa cells as discussed above. Proteins were extracted and the level of H2AX phosphorylation was determined. Immunoblot analysis of cell lysates extracted 4 h post-infection is shown. Anti-γ-H2AX antibody was used as an indicator of double stranded DNA breaks and β-Tubulin was used as a loading control for cell lysates. (C) Signal intensities of bands were measured as described in the methods using LI-COR Image Studio. γ-H2AX signals were corrected to account for any variation in loading using β-Tubulin signal intensity. Experimental signal was normalized so that the mean signal intensity of the samples was equivalent for each experiment. The experiment was carried out in triplicate. Columns represent mean +/- SEM with individual experimental observations indicated by data points. Statistical significance was assessed by unpaired Student's t -test with, * indicating P < 0.05.

    Techniques Used: Mutagenesis, Activity Assay, Western Blot, Infection

    primary antibody γ h2ax  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc primary antibody γ h2ax
    Primary Antibody γ H2ax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 98 stars, based on 1 article reviews
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    γ h2ax  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc γ h2ax
    In vitro antitumor efficacy of [Dbait-ADM@ZIF-8]OPM. (A) The effect of PBS, Dbait@ZIF-8, ADM@ZIF-8, Dbait-ADM@ZIF-8, and [Dbait-ADM@ZIF-8] OPM on the survival of SaOS-2 cells was detected by CCK-8 assay. (B) Under the condition of different doses of RT, the effect of each group on the proliferation of SaOS-2 cells was detected by colony formation assay. (C) The colony formation of SaOS-2 cells in different treatment groups under 2 Gy conditions. (D) PBS, Dbait@ZIF-8, ADM@ZIF-8, Dbait-ADM@ZIF-8, and [Dbait-ADM@ZIF-8] OPM induced apoptosis in SaOS-2 cells induced by 2 Gy RT. (E) Western blot analysis of <t>γ-H2AX</t> and PARP protein levels in SaOS-2 cells.
    γ H2ax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Integrated radiochemotherapy study of ZIF-8 coated with osteosarcoma-platelet hybrid membranes for the delivery of Dbait and Adriamycin"

    Article Title: Integrated radiochemotherapy study of ZIF-8 coated with osteosarcoma-platelet hybrid membranes for the delivery of Dbait and Adriamycin

    Journal: Frontiers in Bioengineering and Biotechnology

    doi: 10.3389/fbioe.2023.1147064

    In vitro antitumor efficacy of [Dbait-ADM@ZIF-8]OPM. (A) The effect of PBS, Dbait@ZIF-8, ADM@ZIF-8, Dbait-ADM@ZIF-8, and [Dbait-ADM@ZIF-8] OPM on the survival of SaOS-2 cells was detected by CCK-8 assay. (B) Under the condition of different doses of RT, the effect of each group on the proliferation of SaOS-2 cells was detected by colony formation assay. (C) The colony formation of SaOS-2 cells in different treatment groups under 2 Gy conditions. (D) PBS, Dbait@ZIF-8, ADM@ZIF-8, Dbait-ADM@ZIF-8, and [Dbait-ADM@ZIF-8] OPM induced apoptosis in SaOS-2 cells induced by 2 Gy RT. (E) Western blot analysis of γ-H2AX and PARP protein levels in SaOS-2 cells.
    Figure Legend Snippet: In vitro antitumor efficacy of [Dbait-ADM@ZIF-8]OPM. (A) The effect of PBS, Dbait@ZIF-8, ADM@ZIF-8, Dbait-ADM@ZIF-8, and [Dbait-ADM@ZIF-8] OPM on the survival of SaOS-2 cells was detected by CCK-8 assay. (B) Under the condition of different doses of RT, the effect of each group on the proliferation of SaOS-2 cells was detected by colony formation assay. (C) The colony formation of SaOS-2 cells in different treatment groups under 2 Gy conditions. (D) PBS, Dbait@ZIF-8, ADM@ZIF-8, Dbait-ADM@ZIF-8, and [Dbait-ADM@ZIF-8] OPM induced apoptosis in SaOS-2 cells induced by 2 Gy RT. (E) Western blot analysis of γ-H2AX and PARP protein levels in SaOS-2 cells.

    Techniques Used: In Vitro, CCK-8 Assay, Colony Assay, Western Blot

    (A) Western blot analysis of γ-H2AX, PARP protein levels in OS organization.
    Figure Legend Snippet: (A) Western blot analysis of γ-H2AX, PARP protein levels in OS organization.

    Techniques Used: Western Blot

    antibody anti phospho h2ax s139  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
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    Cell Signaling Technology Inc antibody anti phospho h2ax s139
    ɣH2AX analysis for Caco-2 cells exposed to different doses of X rays (0, 1, 3 and 5 Gy), without (w/o) or with 1 U/mL EcAII (w/EcAII). Panels ( A , B ), illustrative fluorescence microscopy images for the different irradiation and treatment conditions obtained with Hoechst (blue for nuclear DNA, left) and ɣH2AX (red for DNA damage foci, right) of the sample fixed 30 min and 1 h after irradiation, respectively. Images were acquired using a 100× magnification. Cells pre-treated with EcAII for 72 h before radiation exposure. Panels ( C , D ), mean fluorescence intensity (MFI) per cell of the ɣH2AX signal (a.u.). ( E , F ) The count of <t>H2AX</t> foci/nucleus was obtained using open software ImageJ v 1.53 for the sample harvested 30 min and 1 h after irradiation, respectively. ( G ) Cells treated with EcAII after radiation exposure. Illustrative Western blot images of ɣH2AX <t>(S139)</t> and pan-H2AX. The densitometric analysis was performed by evaluating the p-H2AX/total H2AX ratio with changes expressed relative to the unirradiated and untreated control at each time point (% vs. CTRL NT). Samples in the absence of EcAII and with EcAII were harvested at 6 h ( H ), 24 h ( I ) and 48 h after irradiation ( J ). Data reported are mean ± SD, obtained from at least three independent experiments. Statistical significance (Student’s t -test) was calculated comparing the w/o and w/EcAII conditions for each dose and time point (Student’s t -test) and is as follows: * p < 0.05, ** p < 0.01, *** p < 0.001. In all charts black bars represent samples w/o EcAII and gray bars represent samples w/EcAII.
    Antibody Anti Phospho H2ax S139, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Asparagine and Glutamine Deprivation Alters Ionizing Radiation Response, Migration and Adhesion of a p53 null Colorectal Cancer Cell Line"

    Article Title: Asparagine and Glutamine Deprivation Alters Ionizing Radiation Response, Migration and Adhesion of a p53 null Colorectal Cancer Cell Line

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms24032983

    ɣH2AX analysis for Caco-2 cells exposed to different doses of X rays (0, 1, 3 and 5 Gy), without (w/o) or with 1 U/mL EcAII (w/EcAII). Panels ( A , B ), illustrative fluorescence microscopy images for the different irradiation and treatment conditions obtained with Hoechst (blue for nuclear DNA, left) and ɣH2AX (red for DNA damage foci, right) of the sample fixed 30 min and 1 h after irradiation, respectively. Images were acquired using a 100× magnification. Cells pre-treated with EcAII for 72 h before radiation exposure. Panels ( C , D ), mean fluorescence intensity (MFI) per cell of the ɣH2AX signal (a.u.). ( E , F ) The count of H2AX foci/nucleus was obtained using open software ImageJ v 1.53 for the sample harvested 30 min and 1 h after irradiation, respectively. ( G ) Cells treated with EcAII after radiation exposure. Illustrative Western blot images of ɣH2AX (S139) and pan-H2AX. The densitometric analysis was performed by evaluating the p-H2AX/total H2AX ratio with changes expressed relative to the unirradiated and untreated control at each time point (% vs. CTRL NT). Samples in the absence of EcAII and with EcAII were harvested at 6 h ( H ), 24 h ( I ) and 48 h after irradiation ( J ). Data reported are mean ± SD, obtained from at least three independent experiments. Statistical significance (Student’s t -test) was calculated comparing the w/o and w/EcAII conditions for each dose and time point (Student’s t -test) and is as follows: * p < 0.05, ** p < 0.01, *** p < 0.001. In all charts black bars represent samples w/o EcAII and gray bars represent samples w/EcAII.
    Figure Legend Snippet: ɣH2AX analysis for Caco-2 cells exposed to different doses of X rays (0, 1, 3 and 5 Gy), without (w/o) or with 1 U/mL EcAII (w/EcAII). Panels ( A , B ), illustrative fluorescence microscopy images for the different irradiation and treatment conditions obtained with Hoechst (blue for nuclear DNA, left) and ɣH2AX (red for DNA damage foci, right) of the sample fixed 30 min and 1 h after irradiation, respectively. Images were acquired using a 100× magnification. Cells pre-treated with EcAII for 72 h before radiation exposure. Panels ( C , D ), mean fluorescence intensity (MFI) per cell of the ɣH2AX signal (a.u.). ( E , F ) The count of H2AX foci/nucleus was obtained using open software ImageJ v 1.53 for the sample harvested 30 min and 1 h after irradiation, respectively. ( G ) Cells treated with EcAII after radiation exposure. Illustrative Western blot images of ɣH2AX (S139) and pan-H2AX. The densitometric analysis was performed by evaluating the p-H2AX/total H2AX ratio with changes expressed relative to the unirradiated and untreated control at each time point (% vs. CTRL NT). Samples in the absence of EcAII and with EcAII were harvested at 6 h ( H ), 24 h ( I ) and 48 h after irradiation ( J ). Data reported are mean ± SD, obtained from at least three independent experiments. Statistical significance (Student’s t -test) was calculated comparing the w/o and w/EcAII conditions for each dose and time point (Student’s t -test) and is as follows: * p < 0.05, ** p < 0.01, *** p < 0.001. In all charts black bars represent samples w/o EcAII and gray bars represent samples w/EcAII.

    Techniques Used: Fluorescence, Microscopy, Irradiation, Software, Western Blot

    anti γ h2ax antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti γ h2ax antibody
    Therapeutic effect according to BRD overexpression in response to I-131 treatment. ( A ) Clonogenic survival assay in control, oNIS-, and oNIS+BRD-expressing cells. Cells were treated with 0, 0.56, 1.11, or 2.22 MBq of liquid I-131 for 7 h, washed, and incubated in 6-well plates for 10 days. ( B ) Quantification of the clonogenic survival assays in control, oNIS, and oNIS+BRD cells. ( C ) Representative fluorescence images of <t>γ-H2AX</t> foci. Cells were immunostained with anti-γ-H2AX (red) and DAPI (blue) after treatment with liquid I-131 (2.22 MBq) after a 7 h incubation. Scale bar = 30 μm. ( D ) Quantification of the γ-H2AX foci obtained from fluorescence confocal images. ( E ) DNA fragmentation assay with or without 2.22 MBq I-131 treatment. DNA isolated from cells was run on a 1% agarose gel at a current of 100 V for 30 min in TAE buffer. Values are means ± S.E.M. p < 0.001 (***), p < 0.05 (*).
    Anti γ H2ax Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Overexpression of Both Human Sodium Iodide Symporter (NIS) and BRG1-Bromodomain Synergistically Enhances Radioiodine Sensitivity by Stabilizing p53 through NPM1 Expression"

    Article Title: Overexpression of Both Human Sodium Iodide Symporter (NIS) and BRG1-Bromodomain Synergistically Enhances Radioiodine Sensitivity by Stabilizing p53 through NPM1 Expression

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms24032761

    Therapeutic effect according to BRD overexpression in response to I-131 treatment. ( A ) Clonogenic survival assay in control, oNIS-, and oNIS+BRD-expressing cells. Cells were treated with 0, 0.56, 1.11, or 2.22 MBq of liquid I-131 for 7 h, washed, and incubated in 6-well plates for 10 days. ( B ) Quantification of the clonogenic survival assays in control, oNIS, and oNIS+BRD cells. ( C ) Representative fluorescence images of γ-H2AX foci. Cells were immunostained with anti-γ-H2AX (red) and DAPI (blue) after treatment with liquid I-131 (2.22 MBq) after a 7 h incubation. Scale bar = 30 μm. ( D ) Quantification of the γ-H2AX foci obtained from fluorescence confocal images. ( E ) DNA fragmentation assay with or without 2.22 MBq I-131 treatment. DNA isolated from cells was run on a 1% agarose gel at a current of 100 V for 30 min in TAE buffer. Values are means ± S.E.M. p < 0.001 (***), p < 0.05 (*).
    Figure Legend Snippet: Therapeutic effect according to BRD overexpression in response to I-131 treatment. ( A ) Clonogenic survival assay in control, oNIS-, and oNIS+BRD-expressing cells. Cells were treated with 0, 0.56, 1.11, or 2.22 MBq of liquid I-131 for 7 h, washed, and incubated in 6-well plates for 10 days. ( B ) Quantification of the clonogenic survival assays in control, oNIS, and oNIS+BRD cells. ( C ) Representative fluorescence images of γ-H2AX foci. Cells were immunostained with anti-γ-H2AX (red) and DAPI (blue) after treatment with liquid I-131 (2.22 MBq) after a 7 h incubation. Scale bar = 30 μm. ( D ) Quantification of the γ-H2AX foci obtained from fluorescence confocal images. ( E ) DNA fragmentation assay with or without 2.22 MBq I-131 treatment. DNA isolated from cells was run on a 1% agarose gel at a current of 100 V for 30 min in TAE buffer. Values are means ± S.E.M. p < 0.001 (***), p < 0.05 (*).

    Techniques Used: Over Expression, Clonogenic Cell Survival Assay, Expressing, Incubation, Fluorescence, DNA Fragmentation Assay, Isolation, Agarose Gel Electrophoresis

    Radiation sensitization by BRD after low-dose (2.22 MBq) or high-dose (18.5 MBq) I-131 treatment. ( A ) Tumor volumes were measured with a caliper up to 10 days after treatment with 2.22 MBq or 18.5 MBq I-131. ( B , C ) A region of interest (ROI) was measured to quantify the luminescent signal from the tumors. The bioluminescence signal of the IVIS 100 correlated with the cell number after I-131 treatment. The scale bar represents the peak signal in photons/s/cm 2 /sr. ( D ) Tumor sections (4 μm in thickness) were stained with antibodies against myc-tag, ki67, and γ-H2AX. Scale bar for IHC = 50 μm. Scale bar for tissue = 2 mm. ( E ) Quantification of γ-H2AX or ki67 intensity in tumor tissues from D using TissueFAXS software. Values are means ± S.E.M. p < 0.001 (***), p < 0.05 (*).
    Figure Legend Snippet: Radiation sensitization by BRD after low-dose (2.22 MBq) or high-dose (18.5 MBq) I-131 treatment. ( A ) Tumor volumes were measured with a caliper up to 10 days after treatment with 2.22 MBq or 18.5 MBq I-131. ( B , C ) A region of interest (ROI) was measured to quantify the luminescent signal from the tumors. The bioluminescence signal of the IVIS 100 correlated with the cell number after I-131 treatment. The scale bar represents the peak signal in photons/s/cm 2 /sr. ( D ) Tumor sections (4 μm in thickness) were stained with antibodies against myc-tag, ki67, and γ-H2AX. Scale bar for IHC = 50 μm. Scale bar for tissue = 2 mm. ( E ) Quantification of γ-H2AX or ki67 intensity in tumor tissues from D using TissueFAXS software. Values are means ± S.E.M. p < 0.001 (***), p < 0.05 (*).

    Techniques Used: Staining, Software

    rabbit anti γ h2ax  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti γ h2ax
    Rabbit Anti γ H2ax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti phospho histone h2ax  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho histone h2ax
    Anti Phospho Histone H2ax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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