double stranded calf thymus dna  (MedChemExpress)

Journal: iScience

Article Title: Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite

doi: 10.1016/j.isci.2023.106637

Figure Lengend Snippet: Pf CoSP exhibits DNA and RNA binding ability (A i) Schematic representation of predicted domains and motifs of Pf CoSP. (A ii) Multiple sequence alignment of Pf CoSP with its homologs in Escherichia coli , Homo sapiens and plants ( Capsicum annuum , Hibiscus syriacus , Manihot esculenta ). Residues marked with yellow are predicted residues involved in DNA binding and those highlighted in green and marked with red are predicted to be involved in RNA binding. (A iii) Phylogenetic analysis of Pf CoSP with its homologs in other species showing evolutionary distances among them. (B) SDS-PAGE showing recombinant purified Pf CoSP tagged with 6x-Histidine stained with Coomassie Brilliant Blue (CBB). (C) Pf CoSP-DNA interaction using pull down assay. Pf CoSP and negative control BSA were incubated with single stranded (ss) DNA oligomer/double stranded (ds) DNA immobilized cellulose beads in a pull down assay. Elutes and washes from the assay were loaded on 15% SDS-PAGE as depicted. (D) Gel retardation assay showing Pf CoSP-nucleic acid interaction. Left panel: Agarose gel (1%) showing Pf CoSP-DNA binding. Right panel: Agarose gel (1%) showing Pf CoSP- Pf RNA binding. Samples are depicted with + and – above each lane. (E and F) Interaction studies of Pf CoSP with Pf gDNA (E) and Pf RNA (F) using Microscale Thermophoresis (MST). Purified recombinant Pf CoSP was labeled with RED-NHS Lysine dye followed by titration with varying concentrations of Pf g DNA and Pf RNA. Dose-response curves generated K d of 0.137 nM and 8.88 nM for Pf CoSP-gDNA interactions, respectively.

Article Snippet: Deoxyribonucleic acid-cellulose double-stranded from calf Thymus DNA , Sigma-Aldrich , Cat #D8515.

Techniques: RNA Binding Assay, Sequencing, Binding Assay, SDS Page, Recombinant, Purification, Staining, Pull Down Assay, Negative Control, Incubation, Electrophoretic Mobility Shift Assay, Agarose Gel Electrophoresis, Microscale Thermophoresis, Labeling, Titration, Generated

Journal: iScience

Article Title: Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite

doi: 10.1016/j.isci.2023.106637

Figure Lengend Snippet: Interaction of Pf CoSP with α and β tubulin and complex formation of Pf CoSP with ssDNA and tubulin (A) Semi-quantitative ELISA. Concentration-dependent binding curves of Pf CoSP with α and β tubulin where y-axis represents absorbance at 490 nm and x-axis denotes amount of Pf CoSP. Error bars represent standard deviation among three replicates. Blue and red line depicts Pf CoSP-α tubulin and Pf CoSP-β tubulin binding, respectively whereas green depicts BSA as negative control. (B and C) Interaction studies of Pf CoSP with α tubulin (B) and β tubulin (C) using MST. Labeled P. falciparum α and β tubulins were titrated against varying concentrations of Pf CoSP. Dose-response curves were generated that resulted in K d values of 210 nM and 6.49 μM for Pf CoSP-α tubulin and Pf CoSP- β tubulin interactions respectively. (D) Co-immunoprecipitation assay. Pf CoSP (D i, iii), α tubulin (D ii) and β tubulin specific antisera (iv) were coupled to aminolink plus coupling resin, and used to pull down α/β tubulin (D i, iii) and Pf CoSP (D ii, iv), respectively from parasite culture. Preimmune antisera (PI) was used as a control in each pull down assay. Protein bands are marked with ‘∗’. (E) Pf CoSP promotes microtubule assembly. Graph represents the turbidimetry plot of tubulin assembly in the absence or presence of Pf CoSP (10 μM). Purified Pf α and Pf β tubulins were incubated with Pf CoSP and the absorbance at 340 nm was monitored as an indicator of tubulin polymerisation. (F) Complex binding assays depicting complex formation of Pf CoSP with ssDNA and α tubulin. Recombinant Pf CoSP was incubated with the cellulose beads with immobilized single stranded calf thymus DNA and post washing allowed to bind with α tubulin. Elutes from the assay were analyzed by western blot analysis using specific polyclonal antisera against Pf CoSP and α tubulin simultaneously. Samples are depicted with + and – above each lane. Elute from single-stranded DNA oligomer immobilized cellulose beads incubated with Pf CoSP were loaded as a positive control. Elutes from beads incubated with α tubulin and elutes from beads incubated with BSA followed by α tubulin were loaded as negative control. Protein bands are marked with ‘∗’.

Article Snippet: Deoxyribonucleic acid-cellulose double-stranded from calf Thymus DNA , Sigma-Aldrich , Cat #D8515.

Techniques: Enzyme-linked Immunosorbent Assay, Concentration Assay, Binding Assay, Standard Deviation, Negative Control, Labeling, Generated, Co-Immunoprecipitation Assay, Pull Down Assay, Purification, Incubation, Recombinant, Western Blot, Positive Control

Journal: iScience

Article Title: Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite

doi: 10.1016/j.isci.2023.106637

Figure Lengend Snippet: Expression and localization analysis of Pf CoSP at asexual and gametocyte stages of parasite life cycle and effect of LI71 on native Pf CoSP to bind with DNA and α/β tubulin (A) Immunofluorescence images showing the localization of Pf CoSP at asexual and gametocyte stages of parasite life cycle. Smears of methanol-fixed Pf 3D7-infected erythrocytes were stained with anti- Pf CoSP antibodies (1:250) followed by incubation with Alexa Fluor-conjugated secondary antibodies (Alexa Fluor 488, green). DIC: differential interference contrast image, DAPI: nuclear staining 40, 6-diamidino-2-phenylindole (blue); Pf CoSP: mouse anti- Pf CoSP (green); merge: overlay of Pf CoSP with DAPI (Scale bar: 2 μm). (B) Co-localization of Pf CoSP with Pf NapL. Smears of methanol-fixed Pf 3D7-infected erythrocytes were stained with anti- Pf CoSP (1:250) and anti- Pf NapL antibodies (1:250), followed by incubation with Alexa Fluor-conjugated secondary antibodies (Alexa Fluor 488, green; Alexa Fluor 594, red). DIC: differential interference contrast image, DAPI: nuclear staining 40, 6-diamidino-2-phenylindole (blue); Pf CoSP: mouse anti- Pf CoSP (green); Pf NapL: anti- Pf NapL antibody (red); merge: overlay of Pf CoSP with Pf NapL (Scale bar: 2 μm). (C) Co-localization of Pf CoSP with tubulin. Smears of methanol-fixed Pf 3D7-infected erythrocytes were stained with anti- Pf CoSP (1:250) and anti-tubulin antibodies (1:250), followed by incubation with Alexa Fluor-conjugated secondary antibodies (Alexa Fluor 488, green; Alexa Fluor 594, red). DIC: differential interference contrast image, DAPI: nuclear staining 40, 6-diamidino-2-phenylindole (blue); Pf CoSP: mouse anti- Pf CoSP (green); Pf tubulin-: anti- Pf tubulin antibody (red); merge: overlay of Pf CoSP with Pf tubulin (Scale bar: 2 μm). (D) Bead based Pf CoSP-DNA pull down assay in the presence of LI71. Cellulose beads with immobilized single and double stranded calf thymus DNA (as mentioned on the blot) were incubated with parasite lysate treated with and without LI71 (as depicted by + and - sign on the blot) at 25°C and 37°C (mentioned below the blot). Post washing bead pellet was boiled in 1X SDS-PAGE sample loading dye followed by western blotting. Protein bands are marked with ‘∗’. (E) Co-immunoprecipitation assay with parasite lysate to evaluate the interaction of native Pf CoSP with α/β tubulin in the presence and absence of LI71. Pf CoSP specific antisera was coupled to aminolink plus coupling resin, and used to pull down α (i) and β tubulin (ii) from parasite culture treated with and without LI71 (as depicted by + and - sign on the blot) at 25°C and 37°C (mentioned below the blot). Elutes from the assay were probed by western blot analysis using anti-α (i) and anti-β (ii) tubulin antibodies. Protein bands are marked with ‘∗’.

Article Snippet: Deoxyribonucleic acid-cellulose double-stranded from calf Thymus DNA , Sigma-Aldrich , Cat #D8515.

Techniques: Expressing, Immunofluorescence, Infection, Staining, Incubation, Pull Down Assay, SDS Page, Western Blot, Co-Immunoprecipitation Assay

Journal: iScience

Article Title: Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite

doi: 10.1016/j.isci.2023.106637

Figure Lengend Snippet:

Article Snippet: Deoxyribonucleic acid-cellulose double-stranded from calf Thymus DNA , Sigma-Aldrich , Cat #D8515.

Techniques: Recombinant, SYBR Green Assay, Labeling, Software

Journal: iScience

Article Title: Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite

doi: 10.1016/j.isci.2023.106637

Figure Lengend Snippet: Pf CoSP exhibits DNA and RNA binding ability (A i) Schematic representation of predicted domains and motifs of Pf CoSP. (A ii) Multiple sequence alignment of Pf CoSP with its homologs in Escherichia coli , Homo sapiens and plants ( Capsicum annuum , Hibiscus syriacus , Manihot esculenta ). Residues marked with yellow are predicted residues involved in DNA binding and those highlighted in green and marked with red are predicted to be involved in RNA binding. (A iii) Phylogenetic analysis of Pf CoSP with its homologs in other species showing evolutionary distances among them. (B) SDS-PAGE showing recombinant purified Pf CoSP tagged with 6x-Histidine stained with Coomassie Brilliant Blue (CBB). (C) Pf CoSP-DNA interaction using pull down assay. Pf CoSP and negative control BSA were incubated with single stranded (ss) DNA oligomer/double stranded (ds) DNA immobilized cellulose beads in a pull down assay. Elutes and washes from the assay were loaded on 15% SDS-PAGE as depicted. (D) Gel retardation assay showing Pf CoSP-nucleic acid interaction. Left panel: Agarose gel (1%) showing Pf CoSP-DNA binding. Right panel: Agarose gel (1%) showing Pf CoSP- Pf RNA binding. Samples are depicted with + and – above each lane. (E and F) Interaction studies of Pf CoSP with Pf gDNA (E) and Pf RNA (F) using Microscale Thermophoresis (MST). Purified recombinant Pf CoSP was labeled with RED-NHS Lysine dye followed by titration with varying concentrations of Pf g DNA and Pf RNA. Dose-response curves generated K d of 0.137 nM and 8.88 nM for Pf CoSP-gDNA interactions, respectively.

Article Snippet: The nucleic acid binding property of protein was evaluated using cellulose beads with immobilized single and double stranded calf thymus DNA (Sigma Aldrich, USA).

Techniques: RNA Binding Assay, Sequencing, Binding Assay, SDS Page, Recombinant, Purification, Staining, Pull Down Assay, Negative Control, Incubation, Electrophoretic Mobility Shift Assay, Agarose Gel Electrophoresis, Microscale Thermophoresis, Labeling, Titration, Generated

Journal: iScience

Article Title: Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite

doi: 10.1016/j.isci.2023.106637

Figure Lengend Snippet: Interaction of Pf CoSP with α and β tubulin and complex formation of Pf CoSP with ssDNA and tubulin (A) Semi-quantitative ELISA. Concentration-dependent binding curves of Pf CoSP with α and β tubulin where y-axis represents absorbance at 490 nm and x-axis denotes amount of Pf CoSP. Error bars represent standard deviation among three replicates. Blue and red line depicts Pf CoSP-α tubulin and Pf CoSP-β tubulin binding, respectively whereas green depicts BSA as negative control. (B and C) Interaction studies of Pf CoSP with α tubulin (B) and β tubulin (C) using MST. Labeled P. falciparum α and β tubulins were titrated against varying concentrations of Pf CoSP. Dose-response curves were generated that resulted in K d values of 210 nM and 6.49 μM for Pf CoSP-α tubulin and Pf CoSP- β tubulin interactions respectively. (D) Co-immunoprecipitation assay. Pf CoSP (D i, iii), α tubulin (D ii) and β tubulin specific antisera (iv) were coupled to aminolink plus coupling resin, and used to pull down α/β tubulin (D i, iii) and Pf CoSP (D ii, iv), respectively from parasite culture. Preimmune antisera (PI) was used as a control in each pull down assay. Protein bands are marked with ‘∗’. (E) Pf CoSP promotes microtubule assembly. Graph represents the turbidimetry plot of tubulin assembly in the absence or presence of Pf CoSP (10 μM). Purified Pf α and Pf β tubulins were incubated with Pf CoSP and the absorbance at 340 nm was monitored as an indicator of tubulin polymerisation. (F) Complex binding assays depicting complex formation of Pf CoSP with ssDNA and α tubulin. Recombinant Pf CoSP was incubated with the cellulose beads with immobilized single stranded calf thymus DNA and post washing allowed to bind with α tubulin. Elutes from the assay were analyzed by western blot analysis using specific polyclonal antisera against Pf CoSP and α tubulin simultaneously. Samples are depicted with + and – above each lane. Elute from single-stranded DNA oligomer immobilized cellulose beads incubated with Pf CoSP were loaded as a positive control. Elutes from beads incubated with α tubulin and elutes from beads incubated with BSA followed by α tubulin were loaded as negative control. Protein bands are marked with ‘∗’.

Article Snippet: The nucleic acid binding property of protein was evaluated using cellulose beads with immobilized single and double stranded calf thymus DNA (Sigma Aldrich, USA).

Techniques: Enzyme-linked Immunosorbent Assay, Concentration Assay, Binding Assay, Standard Deviation, Negative Control, Labeling, Generated, Co-Immunoprecipitation Assay, Pull Down Assay, Purification, Incubation, Recombinant, Western Blot, Positive Control

Journal: iScience

Article Title: Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite

doi: 10.1016/j.isci.2023.106637

Figure Lengend Snippet: Expression and localization analysis of Pf CoSP at asexual and gametocyte stages of parasite life cycle and effect of LI71 on native Pf CoSP to bind with DNA and α/β tubulin (A) Immunofluorescence images showing the localization of Pf CoSP at asexual and gametocyte stages of parasite life cycle. Smears of methanol-fixed Pf 3D7-infected erythrocytes were stained with anti- Pf CoSP antibodies (1:250) followed by incubation with Alexa Fluor-conjugated secondary antibodies (Alexa Fluor 488, green). DIC: differential interference contrast image, DAPI: nuclear staining 40, 6-diamidino-2-phenylindole (blue); Pf CoSP: mouse anti- Pf CoSP (green); merge: overlay of Pf CoSP with DAPI (Scale bar: 2 μm). (B) Co-localization of Pf CoSP with Pf NapL. Smears of methanol-fixed Pf 3D7-infected erythrocytes were stained with anti- Pf CoSP (1:250) and anti- Pf NapL antibodies (1:250), followed by incubation with Alexa Fluor-conjugated secondary antibodies (Alexa Fluor 488, green; Alexa Fluor 594, red). DIC: differential interference contrast image, DAPI: nuclear staining 40, 6-diamidino-2-phenylindole (blue); Pf CoSP: mouse anti- Pf CoSP (green); Pf NapL: anti- Pf NapL antibody (red); merge: overlay of Pf CoSP with Pf NapL (Scale bar: 2 μm). (C) Co-localization of Pf CoSP with tubulin. Smears of methanol-fixed Pf 3D7-infected erythrocytes were stained with anti- Pf CoSP (1:250) and anti-tubulin antibodies (1:250), followed by incubation with Alexa Fluor-conjugated secondary antibodies (Alexa Fluor 488, green; Alexa Fluor 594, red). DIC: differential interference contrast image, DAPI: nuclear staining 40, 6-diamidino-2-phenylindole (blue); Pf CoSP: mouse anti- Pf CoSP (green); Pf tubulin-: anti- Pf tubulin antibody (red); merge: overlay of Pf CoSP with Pf tubulin (Scale bar: 2 μm). (D) Bead based Pf CoSP-DNA pull down assay in the presence of LI71. Cellulose beads with immobilized single and double stranded calf thymus DNA (as mentioned on the blot) were incubated with parasite lysate treated with and without LI71 (as depicted by + and - sign on the blot) at 25°C and 37°C (mentioned below the blot). Post washing bead pellet was boiled in 1X SDS-PAGE sample loading dye followed by western blotting. Protein bands are marked with ‘∗’. (E) Co-immunoprecipitation assay with parasite lysate to evaluate the interaction of native Pf CoSP with α/β tubulin in the presence and absence of LI71. Pf CoSP specific antisera was coupled to aminolink plus coupling resin, and used to pull down α (i) and β tubulin (ii) from parasite culture treated with and without LI71 (as depicted by + and - sign on the blot) at 25°C and 37°C (mentioned below the blot). Elutes from the assay were probed by western blot analysis using anti-α (i) and anti-β (ii) tubulin antibodies. Protein bands are marked with ‘∗’.

Article Snippet: The nucleic acid binding property of protein was evaluated using cellulose beads with immobilized single and double stranded calf thymus DNA (Sigma Aldrich, USA).

Techniques: Expressing, Immunofluorescence, Infection, Staining, Incubation, Pull Down Assay, SDS Page, Western Blot, Co-Immunoprecipitation Assay

Journal: PLoS ONE

Article Title: The Inhibition of Anti-DNA Binding to DNA by Nucleic Acid Binding Polymers

doi: 10.1371/journal.pone.0040862

Figure Lengend Snippet: The ability of polymers PAMAM, HDMBr, and CDP to inhibit binding of a murine monoclonal anti-DNA antibody QB1 to DNA was tested by ELISA. Binding of QB1 at 35 ng/ml final concentration was assayed by ELISA in the presence of PAMAM, HDMBr, or CDP at final concentrations from 10 ng/ml to 1,250 ng/ml. Control wells had buffer alone. Antibody was measured as described in Experimental Procedures. The OD 450 values of 3 wells of each polymer concentration or of 6 wells without polymer were averaged. Each point shown is 100% x average OD 450 with polymer/average OD 450 without polymer. Circles show data for PAMAM; squares show data for HDMBr; triangles show data for CDP.

Article Snippet: For the direct binding assay, wells of ELISA plates were coated with 5 µg/ml native double stranded calf thymus (CT) DNA (Worthington Biochemical, Lakewood, NJ) in 1 x SSC (150 mM NaCl, 15 mM Na citrate, pH 7) overnight at 4°C.

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Concentration Assay

Journal: PLoS ONE

Article Title: The Inhibition of Anti-DNA Binding to DNA by Nucleic Acid Binding Polymers

doi: 10.1371/journal.pone.0040862

Figure Lengend Snippet: The ability of polymers PAMAM, HDMBr, and CDP to inhibit DNA binding by anti-DNA antibodies in three SLE patient plasmas to DNA was tested by ELISA. Binding by antibodies in Plasma 1 (final dilution 1/1,000), Plasma 2 (final dilution 1/2,800), and Plasma 3 (final dilution 1/3,000) was assayed in the presence of PAMAM, HDMBr, or CDP at final concentrations ranging from 300 ng/ml to 10,000 ng/ml or with dilution buffer alone. Antibody levels were determined by ELISA as described in . The OD 450 values of 2 wells for each condition were averaged. Each point shown is 100% x average OD 450 with polymer/average OD 450 without polymer. Circles show data for Plasma 1; squares show data for Plasma 2; triangles show data for Plasma 3.

Article Snippet: For the direct binding assay, wells of ELISA plates were coated with 5 µg/ml native double stranded calf thymus (CT) DNA (Worthington Biochemical, Lakewood, NJ) in 1 x SSC (150 mM NaCl, 15 mM Na citrate, pH 7) overnight at 4°C.

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay

Journal: PLoS ONE

Article Title: The Inhibition of Anti-DNA Binding to DNA by Nucleic Acid Binding Polymers

doi: 10.1371/journal.pone.0040862

Figure Lengend Snippet: Native CT DNA was biotinylated and then captured in ELISA plate wells coated with streptavidin. The binding of Plasma 1 (final dilution 1/3,500), Plasma 2 (final dilution 1/8,000), and Plasma 3 (final dilution 1/4,500) was measured by ELISA in the presence of PAMAM, HDMBr, or CDP at final concentrations from 80 ng/ml to 10,000 ng/ml or with dilution buffer alone. The OD 450 values of 2 wells for each condition were averaged. Each point shown is 100% x average OD 450 with polymer/average OD 450 without polymer. Circles show data for Plasma 1; squares show data for Plasma 2; triangles show data for Plasma 3.

Article Snippet: For the direct binding assay, wells of ELISA plates were coated with 5 µg/ml native double stranded calf thymus (CT) DNA (Worthington Biochemical, Lakewood, NJ) in 1 x SSC (150 mM NaCl, 15 mM Na citrate, pH 7) overnight at 4°C.

Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay

Journal: PLoS ONE

Article Title: The Inhibition of Anti-DNA Binding to DNA by Nucleic Acid Binding Polymers

doi: 10.1371/journal.pone.0040862

Figure Lengend Snippet: In this assay, 50 µl/well of Plasma 1 diluted 1/1,700, Plasma 2 diluted 1/3,950, and Plasma 3 diluted 1/2,250 were incubated in wells of microtiter plates with biotinylated DNA bound to streptavidin. After 1 hour to allow the formation of immune complexes, 50 µl of dilutions of PAMAM, HDMBr, or CDP or 50 µl of dilution buffer alone were then added to produce concentrations of the polymers of 10,000 ng/ml, 2,500 ng/ml, 620 ng/ml, 160 ng/ml or 0 ng/ml. Antibody binding was then determined by ELISA. The OD 450 values of 2 wells for each condition were averaged. Each point shown is 100% x average OD 450 with polymer/average OD 450 without polymer. Circles show data for Plasma 1; squares show data for Plasma 2; triangles show data for Plasma 3.

Article Snippet: For the direct binding assay, wells of ELISA plates were coated with 5 µg/ml native double stranded calf thymus (CT) DNA (Worthington Biochemical, Lakewood, NJ) in 1 x SSC (150 mM NaCl, 15 mM Na citrate, pH 7) overnight at 4°C.

Techniques: Incubation, Binding Assay, Enzyme-linked Immunosorbent Assay

Journal: iScience

Article Title: Mixed-surface polyamidoamine polymer variants retain nucleic acid-scavenger ability with reduced toxicity

doi: 10.1016/j.isci.2022.105542

Figure Lengend Snippet: Mixed surface PAMAM variants capture double-stranded ctDNA (calf thymus DNA) at least as, if not more, effectively than the fully cationic PAMAM G3 molecule in “sandwich-type” ELISA assays (A) Plot of binding of ctDNA with data shown as mean ± standard error of the mean. (B) A two-way ANOVA with post hoc analysis via Tukey’s multiple comparison test demonstrates that the mixed polymers bind ctDNA more efficiently than G3 at 1 ng/mL and 3 ng/mL ctDNA concentrations.

Article Snippet: Blocking used 200 μL/well of 2% bovine serum albumin, 0.05% Tween-20 in PBS for 2 h. Calf thymus double stranded DNA (ctDNA) was sourced from Worthington Biochemical Corporation (cat# LS002105), resuspended in TE buffer (Tris 10 mM, EDTA 1 mM, pH 8.0), and extracted several times with phenol:chloroform:isoamyl alcohol (25:24:1; Millipore Sigma cat# 77617) and chloroform:isoamyl alcohol (24:1 Millipore Sigma cat# 25666). ctDNA was diluted in 1X SSC (150 mM NaCl, 15 mM Na citrate, pH 7).

Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay

Journal: Micromachines

Article Title: Low-Cost High-Resolution Potentiostat for Electrochemical Detection of Nucleic Acids and Biomolecular Interactions

doi: 10.3390/mi13101610

Figure Lengend Snippet: Effects of DNA concentrations on the electrochemical signal measured by the developed instrument and Autolab-PGSTAT-302. DPVs representing the guanine signals related to the different concentrations of ssDNA using ( A ) Autolab PGSTAT-302, and ( C ) the developed instrument, and the guanine signals related to the different concentrations of dsDNA using ( E ) Autolab PGSTAT-302, and ( G ) the developed instrument. ( B ) Line graph presenting average guanine signals ( n = 3) related to ssDNA-immobilized PGEs in the case of different ssDNA concentrations from 2 to 14 µg/mL with Autolab PGSTAT-302. ( D ) Line graph representing the average guanine signals ( n = 3) related to ssDNA-immobilized PGEs in the case of different ssDNA concentrations from 2 to 20 µg/mL with the developed instrument. ( F ) Line graph representing average guanine signals ( n = 3) related to dsDNA-immobilized PGEs in the case of different ssDNA concentrations from 2 to 18 µg/mL with Autolab PGSTAT-302. ( H ) Line graph representing average guanine signals ( n = 3) related to dsDNA-immobilized PGEs in the case of different dsDNA concentrations from 2 to 14 µg/mL with the developed instrument.

Article Snippet: Bovine serum albumin (BSA), calf thymus single-stranded DNA (ssDNA), and calf thymus double-stranded DNA (dsDNA) were purchased from Sigma-Aldrich.

Techniques: