aspergillus oryzae  (ATCC)


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    ATCC aspergillus oryzae
    Aspergillus Oryzae, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    aspergillus oryzae  (ATCC)


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    ATCC aspergillus oryzae
    Aspergillus Oryzae, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    e faecalis pcm 1861 strain  (ATCC)


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    ATCC e faecalis pcm 1861 strain
    E Faecalis Pcm 1861 Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    e faecalis pcm 1861  (ATCC)


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    ATCC e faecalis pcm 1861
    E Faecalis Pcm 1861, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bacillus subtilis 168  (ATCC)


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    ATCC bacillus subtilis 168
    Bacillus Subtilis 168, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cho em9 cells  (ATCC)


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    ATCC cho em9 cells
    Cho Em9 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    repair deficient em9 mutant  (ATCC)


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    ATCC repair deficient em9 mutant
    Repair Deficient Em9 Mutant, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cho em9 cells  (ATCC)


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    ATCC cho em9 cells
    Recruitment of XRCC1-YFP and deletion mutants to micro-irradiated regions after kinase inhibitor treatment. ( a ) Untreated, freely cycling cells stably expressing XRCC1-YFP 1 s and 100 s after 405 nm micro-irradiation in a selected region (marked with arrow). Bars 5 µM. ( b–e ) Average fold increase in mIF intensities of XRCC1-YFP in HeLa cells treated with either 0.25% DMSO (mock, black lines) or kinase inhibitors (red lines). Mean ± SEM is shown. ( b ) 25 µM CK2 inhibitor TBB. Mock n = 4, TBB n = 9. (c) 25 µM PI3K inhibitor LY294002. Mock n = 16, LY294002 n = 7. ( d ) 25 µM p38 MAPK inhibitor SB203580. Mock n = 12, SB203580 n = 12. ( e ) 25 µM p38 MAPK inhibitor BIRB0796. Mock n = 11, BIRB0796 n = 16 ( f ) Schematic overview of full length XRCC1 and deletion mutants. ( g ) Average fold increase in mIF intensities of full-length XRCC1-YFP (left panel), YFP-MD (middle panel) and YFP-BLB (right panel) deletion mutants in <t>CHO</t> <t>EM9</t> cells in absence (black line) and presence of 25 µM SB203580 (red line). The graphs representing the mutants in absence of SB203580 have previously been published . XRCC1: Mock n = 15, SB203580 n = 11. MD: Mock n = 15. SB203580 n = 16. BLB: Mock n = 20, SB203580 n = 17.
    Cho Em9 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "p38 MAPK signaling and phosphorylations in the BRCT1 domain regulate XRCC1 recruitment to sites of DNA damage"

    Article Title: p38 MAPK signaling and phosphorylations in the BRCT1 domain regulate XRCC1 recruitment to sites of DNA damage

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-06770-3

    Recruitment of XRCC1-YFP and deletion mutants to micro-irradiated regions after kinase inhibitor treatment. ( a ) Untreated, freely cycling cells stably expressing XRCC1-YFP 1 s and 100 s after 405 nm micro-irradiation in a selected region (marked with arrow). Bars 5 µM. ( b–e ) Average fold increase in mIF intensities of XRCC1-YFP in HeLa cells treated with either 0.25% DMSO (mock, black lines) or kinase inhibitors (red lines). Mean ± SEM is shown. ( b ) 25 µM CK2 inhibitor TBB. Mock n = 4, TBB n = 9. (c) 25 µM PI3K inhibitor LY294002. Mock n = 16, LY294002 n = 7. ( d ) 25 µM p38 MAPK inhibitor SB203580. Mock n = 12, SB203580 n = 12. ( e ) 25 µM p38 MAPK inhibitor BIRB0796. Mock n = 11, BIRB0796 n = 16 ( f ) Schematic overview of full length XRCC1 and deletion mutants. ( g ) Average fold increase in mIF intensities of full-length XRCC1-YFP (left panel), YFP-MD (middle panel) and YFP-BLB (right panel) deletion mutants in CHO EM9 cells in absence (black line) and presence of 25 µM SB203580 (red line). The graphs representing the mutants in absence of SB203580 have previously been published . XRCC1: Mock n = 15, SB203580 n = 11. MD: Mock n = 15. SB203580 n = 16. BLB: Mock n = 20, SB203580 n = 17.
    Figure Legend Snippet: Recruitment of XRCC1-YFP and deletion mutants to micro-irradiated regions after kinase inhibitor treatment. ( a ) Untreated, freely cycling cells stably expressing XRCC1-YFP 1 s and 100 s after 405 nm micro-irradiation in a selected region (marked with arrow). Bars 5 µM. ( b–e ) Average fold increase in mIF intensities of XRCC1-YFP in HeLa cells treated with either 0.25% DMSO (mock, black lines) or kinase inhibitors (red lines). Mean ± SEM is shown. ( b ) 25 µM CK2 inhibitor TBB. Mock n = 4, TBB n = 9. (c) 25 µM PI3K inhibitor LY294002. Mock n = 16, LY294002 n = 7. ( d ) 25 µM p38 MAPK inhibitor SB203580. Mock n = 12, SB203580 n = 12. ( e ) 25 µM p38 MAPK inhibitor BIRB0796. Mock n = 11, BIRB0796 n = 16 ( f ) Schematic overview of full length XRCC1 and deletion mutants. ( g ) Average fold increase in mIF intensities of full-length XRCC1-YFP (left panel), YFP-MD (middle panel) and YFP-BLB (right panel) deletion mutants in CHO EM9 cells in absence (black line) and presence of 25 µM SB203580 (red line). The graphs representing the mutants in absence of SB203580 have previously been published . XRCC1: Mock n = 15, SB203580 n = 11. MD: Mock n = 15. SB203580 n = 16. BLB: Mock n = 20, SB203580 n = 17.

    Techniques Used: Irradiation, Stable Transfection, Expressing

    Mutation of XRCC1 phosphorylation sites and recruitment to DNA damage. ( a ) Map of XRCC1: known domains, deletion mutants, predicted MAPK docking motif, PAR-binding region, predicted p38 MAPK and known phosphorylation residues. Phosphorylation residues identified in this publication is marked in green. ( b ) Average fold increase in mIF intensities of wild type YFP-MD (WT, green lines) and mutant YFP-MD T367A (MUT, black lines) in mock and p38i (SB203580, 25 µM) treated CHO EM9 cells using 1x laser dose. WT: Mock n = 19, p38i n = 12. MUT (T367A): Mock n = 17, p38i n = 16. Mean ± SEM. ( c ) Comet analysis: Dot plot of CHO EM9 cells expressing XRCC1-YFP wild type, XRCC1-YFP T367A and YFP treated with H 2 O 2 (62 µM) for 10 min. 0, 10 and 20 min recovery. Averages of n = 100 ± SEM. One out of three similar experiments is shown. Asterisks represent Student’s t-test p-values from cells with mutated or no XRCC1 vs. the corresponding XRCC1 wild type sample, where **p < 0.001. ( d ) Sequence of the XRCC1 BRCT1 domain. The phosphorylated peptide detected on MS (green box) and the phosphate-binding pocket (red) are indicated. ( e , f ) Average mIF intensities of wild type YFP-MD (WT, green lines) and YFP-MD T357A ( e ) and T358A ( f ) mutants (MUT, black lines) in mock and p38i (SB203580, 25 µM) treated HeLa cells using 1x laser dose. WT: Mock n = 16, p38i n = 10. S357A: Mock n = 16, p38i n = 11. T358A: Mock n = 8, p38i n = 4. Mean ± SEM.
    Figure Legend Snippet: Mutation of XRCC1 phosphorylation sites and recruitment to DNA damage. ( a ) Map of XRCC1: known domains, deletion mutants, predicted MAPK docking motif, PAR-binding region, predicted p38 MAPK and known phosphorylation residues. Phosphorylation residues identified in this publication is marked in green. ( b ) Average fold increase in mIF intensities of wild type YFP-MD (WT, green lines) and mutant YFP-MD T367A (MUT, black lines) in mock and p38i (SB203580, 25 µM) treated CHO EM9 cells using 1x laser dose. WT: Mock n = 19, p38i n = 12. MUT (T367A): Mock n = 17, p38i n = 16. Mean ± SEM. ( c ) Comet analysis: Dot plot of CHO EM9 cells expressing XRCC1-YFP wild type, XRCC1-YFP T367A and YFP treated with H 2 O 2 (62 µM) for 10 min. 0, 10 and 20 min recovery. Averages of n = 100 ± SEM. One out of three similar experiments is shown. Asterisks represent Student’s t-test p-values from cells with mutated or no XRCC1 vs. the corresponding XRCC1 wild type sample, where **p < 0.001. ( d ) Sequence of the XRCC1 BRCT1 domain. The phosphorylated peptide detected on MS (green box) and the phosphate-binding pocket (red) are indicated. ( e , f ) Average mIF intensities of wild type YFP-MD (WT, green lines) and YFP-MD T357A ( e ) and T358A ( f ) mutants (MUT, black lines) in mock and p38i (SB203580, 25 µM) treated HeLa cells using 1x laser dose. WT: Mock n = 16, p38i n = 10. S357A: Mock n = 16, p38i n = 11. T358A: Mock n = 8, p38i n = 4. Mean ± SEM.

    Techniques Used: Mutagenesis, Binding Assay, Expressing, Sequencing

    PAR-binding and recruitment to DNA damage of phosho-mimetic and phospho-defective T358 and T367 MD mutants. Average fold increase in mIF intensities of YFP-MD phospho-mimetic and phospho-defective mutants ( a ) T358 and ( b ) T367 using a 5x laser dose. Wild type YFP-MD (WT, green line): n = 10, T358A (grey dotted line): n = 8, T358D (black dotted line): n = 10, T367A (grey dotted line): n = 10, T367D (black dotted line): n = 8. Mean ± SEM. ( c ) Intracellular localization of wild type (WT), T358A/D, T367A/D YFP-MD in HeLa cells. ( d ) Intracellular localization of wild type YFP-MD and CFP-PCNA in CHO EM9 with and without PARPi (PJ34, 10 μM, 1 hour). ( e ) Co-immunoprecipitation of PARP1 and RNF146 with wild type, T358A/D and T367A/D YFP-MD with and without PARPi (PJ34, 10 μM, 1 hour) using 100 mM wash buffer. Cropped images of one out of five experiments with similar trends are depicted. ( f ) Co-immunoprecipitation of PARylated proteins with wild type, T358A/D and T367A/D YFP-MD using 1 M wash buffer. One out of three experiments with similar trend is depicted.
    Figure Legend Snippet: PAR-binding and recruitment to DNA damage of phosho-mimetic and phospho-defective T358 and T367 MD mutants. Average fold increase in mIF intensities of YFP-MD phospho-mimetic and phospho-defective mutants ( a ) T358 and ( b ) T367 using a 5x laser dose. Wild type YFP-MD (WT, green line): n = 10, T358A (grey dotted line): n = 8, T358D (black dotted line): n = 10, T367A (grey dotted line): n = 10, T367D (black dotted line): n = 8. Mean ± SEM. ( c ) Intracellular localization of wild type (WT), T358A/D, T367A/D YFP-MD in HeLa cells. ( d ) Intracellular localization of wild type YFP-MD and CFP-PCNA in CHO EM9 with and without PARPi (PJ34, 10 μM, 1 hour). ( e ) Co-immunoprecipitation of PARP1 and RNF146 with wild type, T358A/D and T367A/D YFP-MD with and without PARPi (PJ34, 10 μM, 1 hour) using 100 mM wash buffer. Cropped images of one out of five experiments with similar trends are depicted. ( f ) Co-immunoprecipitation of PARylated proteins with wild type, T358A/D and T367A/D YFP-MD using 1 M wash buffer. One out of three experiments with similar trend is depicted.

    Techniques Used: Binding Assay, Immunoprecipitation

    corynebacterium glutamicum iegm 1861  (ATCC)


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    ATCC corynebacterium glutamicum iegm 1861
    Corynebacterium Glutamicum Iegm 1861, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    corynebacterium glutamicum iegm 1861  (ATCC)


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    ATCC corynebacterium glutamicum iegm 1861
    Adhesion (%) of resting bacterial cells to polystyrene coated with biosurfactant at different concentrations
    Corynebacterium Glutamicum Iegm 1861, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Diverse effects of a biosurfactant from Rhodococcus ruber IEGM 231 on the adhesion of resting and growing bacteria to polystyrene"

    Article Title: Diverse effects of a biosurfactant from Rhodococcus ruber IEGM 231 on the adhesion of resting and growing bacteria to polystyrene

    Journal: AMB Express

    doi: 10.1186/s13568-016-0186-z

    Adhesion (%) of resting bacterial cells to polystyrene coated with biosurfactant at different concentrations
    Figure Legend Snippet: Adhesion (%) of resting bacterial cells to polystyrene coated with biosurfactant at different concentrations

    Techniques Used: Concentration Assay

    Adhesion (%) of growing bacterial cells to polystyrene coated with biosurfactant at different concentrations
    Figure Legend Snippet: Adhesion (%) of growing bacterial cells to polystyrene coated with biosurfactant at different concentrations

    Techniques Used: Concentration Assay

    Surface properties of bacterial strains depending on the growth phase
    Figure Legend Snippet: Surface properties of bacterial strains depending on the growth phase

    Techniques Used:

    hr esi ms m z 237 1861  (ATCC)


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    ATCC hr esi ms m z 237 1861
    Hr Esi Ms M Z 237 1861, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cho em9 cells  (ATCC)
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    repair deficient em9 mutant  (ATCC)
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    corynebacterium glutamicum iegm 1861  (ATCC)
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    ATCC corynebacterium glutamicum iegm 1861
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    hr esi ms m z 237 1861  (ATCC)
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