topoisomerase  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95

    Structured Review

    New England Biolabs topoisomerase
    IAA influences the <t>topoisomerase</t> I activity. ( A ) and ( B ) Effect of 0.2, 1.0, and 3.0 mM IAA on the activity of 2.5 U mL −1 topoisomerase I from E. coli ( EcTopoI ). ( C ) and ( D ) Effect of 1.0 mM IAA on the activity of 0.1, 0.5, and 2.5 U mL −1 EcTopoI . To visualize the reaction products, the gels were stained post-electrophoresis with ethidium bromide and de-stained in deionized water. The relative intensity of each band in the gel was measured and used to calculate the amount of total DNA (the unprocessed DNA plus the distinct topoisomer species), and that of all individual reaction products. For each condition, the relaxation activity is expressed as a percentage of the produced topoisomers over the total DNA in each lane. Values are the means ± SD of three different biological replicates. The asterisks (*) indicate significant differences ( p
    Topoisomerase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/topoisomerase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    topoisomerase - by Bioz Stars, 2022-05
    95/100 stars

    Images

    1) Product Images from "New Insights into Structural and Functional Roles of Indole-3-acetic acid (IAA): Changes in DNA Topology and Gene Expression in Bacteria"

    Article Title: New Insights into Structural and Functional Roles of Indole-3-acetic acid (IAA): Changes in DNA Topology and Gene Expression in Bacteria

    Journal: Biomolecules

    doi: 10.3390/biom9100522

    IAA influences the topoisomerase I activity. ( A ) and ( B ) Effect of 0.2, 1.0, and 3.0 mM IAA on the activity of 2.5 U mL −1 topoisomerase I from E. coli ( EcTopoI ). ( C ) and ( D ) Effect of 1.0 mM IAA on the activity of 0.1, 0.5, and 2.5 U mL −1 EcTopoI . To visualize the reaction products, the gels were stained post-electrophoresis with ethidium bromide and de-stained in deionized water. The relative intensity of each band in the gel was measured and used to calculate the amount of total DNA (the unprocessed DNA plus the distinct topoisomer species), and that of all individual reaction products. For each condition, the relaxation activity is expressed as a percentage of the produced topoisomers over the total DNA in each lane. Values are the means ± SD of three different biological replicates. The asterisks (*) indicate significant differences ( p
    Figure Legend Snippet: IAA influences the topoisomerase I activity. ( A ) and ( B ) Effect of 0.2, 1.0, and 3.0 mM IAA on the activity of 2.5 U mL −1 topoisomerase I from E. coli ( EcTopoI ). ( C ) and ( D ) Effect of 1.0 mM IAA on the activity of 0.1, 0.5, and 2.5 U mL −1 EcTopoI . To visualize the reaction products, the gels were stained post-electrophoresis with ethidium bromide and de-stained in deionized water. The relative intensity of each band in the gel was measured and used to calculate the amount of total DNA (the unprocessed DNA plus the distinct topoisomer species), and that of all individual reaction products. For each condition, the relaxation activity is expressed as a percentage of the produced topoisomers over the total DNA in each lane. Values are the means ± SD of three different biological replicates. The asterisks (*) indicate significant differences ( p

    Techniques Used: Activity Assay, Staining, Electrophoresis, Produced

    2) Product Images from "Polymyxin B causes DNA damage in HK-2 cells and mice"

    Article Title: Polymyxin B causes DNA damage in HK-2 cells and mice

    Journal: Archives of toxicology

    doi: 10.1007/s00204-018-2192-1

    PMB had high affinity for DNA and inhibited electrophoretic migration of plasmid at higher concentrations. ( A ) 60 ng of pBlueScript II DNA incubated with PMB (12.5–500 μM) in a topoisomerase I buffer for 2 h at 37 °C. Samples were resolved by electrophoresis. ( B ) Chemical structure of PMB with potential DNA binding sites (including the Dab residues) highlighted.
    Figure Legend Snippet: PMB had high affinity for DNA and inhibited electrophoretic migration of plasmid at higher concentrations. ( A ) 60 ng of pBlueScript II DNA incubated with PMB (12.5–500 μM) in a topoisomerase I buffer for 2 h at 37 °C. Samples were resolved by electrophoresis. ( B ) Chemical structure of PMB with potential DNA binding sites (including the Dab residues) highlighted.

    Techniques Used: Migration, Plasmid Preparation, Incubation, Electrophoresis, Binding Assay

    3) Product Images from "Sodium Selenide Toxicity Is Mediated by O2-Dependent DNA Breaks"

    Article Title: Sodium Selenide Toxicity Is Mediated by O2-Dependent DNA Breaks

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0036343

    Effect of sodium selenide on DNA integrity in vitro . Purified pNOY102 plasmid DNA was submitted to native gel electrophoresis after incubation during 1 h at 37°C with different combinations of the indicated compounds: 15 µM Na 2 Se, 25 µM sodium selenite (Na 2 SeO 3 ), 500 µM glutathione (GSH), 200 units/ml SOD, 80 mM mannitol, 50 units/ml catalase, 200 units/ml topoisomerase I (Topo I) or 500 units/ml SalI. The different topomers, as detected after ethidium bromide staining, are indicated on the left. The star on the right side of the figure points a contaminant systematically present in our pNOY102 preparations. The numbers at the bottom of the figure show the ratios between nicked and supercoiled DNA band intensities. With topoisomerase, the ratio is between relaxed and supercoiled DNA.
    Figure Legend Snippet: Effect of sodium selenide on DNA integrity in vitro . Purified pNOY102 plasmid DNA was submitted to native gel electrophoresis after incubation during 1 h at 37°C with different combinations of the indicated compounds: 15 µM Na 2 Se, 25 µM sodium selenite (Na 2 SeO 3 ), 500 µM glutathione (GSH), 200 units/ml SOD, 80 mM mannitol, 50 units/ml catalase, 200 units/ml topoisomerase I (Topo I) or 500 units/ml SalI. The different topomers, as detected after ethidium bromide staining, are indicated on the left. The star on the right side of the figure points a contaminant systematically present in our pNOY102 preparations. The numbers at the bottom of the figure show the ratios between nicked and supercoiled DNA band intensities. With topoisomerase, the ratio is between relaxed and supercoiled DNA.

    Techniques Used: In Vitro, Purification, Plasmid Preparation, Nucleic Acid Electrophoresis, Incubation, Staining

    Effect of dioxygen on the in vitro Na 2 Se-induced DNA nicking. Purified pNOY102 plasmid DNA was incubated for 1 min at 20°C with the indicated concentrations of sodium selenide in either a deoxygenated (left) or an oxygenated buffer (right). The reaction was quenched by the addition of mannitol. The different topomers were then separated by native gel electrophoresis and detected by ethidium bromide staining. Lane T corresponds to a topoisomerase I-relaxed DNA sample.
    Figure Legend Snippet: Effect of dioxygen on the in vitro Na 2 Se-induced DNA nicking. Purified pNOY102 plasmid DNA was incubated for 1 min at 20°C with the indicated concentrations of sodium selenide in either a deoxygenated (left) or an oxygenated buffer (right). The reaction was quenched by the addition of mannitol. The different topomers were then separated by native gel electrophoresis and detected by ethidium bromide staining. Lane T corresponds to a topoisomerase I-relaxed DNA sample.

    Techniques Used: In Vitro, Purification, Plasmid Preparation, Incubation, Nucleic Acid Electrophoresis, Staining

    4) Product Images from "The Neisseria gonorrhoeae photolyase orthologue phrB is required for proper DNA supercoiling but does not function in photo-reactivation"

    Article Title: The Neisseria gonorrhoeae photolyase orthologue phrB is required for proper DNA supercoiling but does not function in photo-reactivation

    Journal: Molecular microbiology

    doi: 10.1111/j.1365-2958.2010.07481.x

    Analysis of PhrB DNA binding and bending in vitro A. Fluorescence anisotropy of PhrB plotted at increasing protein concentrations per amount of 30 bp dsDNA oligonucleotide substrate (o30dsDNA). Error bars represent the standard error of the mean for 3 independent experiments with a total of 6 replicates. B. Fluorescence anisotropy of PhrB plotted at increasing protein concentrations per amount of UV irradiated (1000 joules/m 2 ) o30dsDNA oligonucleotide substrate. Error bars represent the standard error of the mean for 3 independent experiments with a total of 6 replicates. C. Protein duplex DNA bending assay. Shown is a (2.5 μg/ml) chloroquine gel of plasmid DNA (pCRBlunt2bp) incubated with topoisomerase I, DNA gyrase with or without the addition of topoisomerase I, and increasing concentrations of PhrB to DNA (1:1, 10:1, 100:1) with or without the addition of topoisomerase I. The direction of migration of less negatively supercoiled DNA (+) and more negatively supercoiled DNA (−) is indicated.
    Figure Legend Snippet: Analysis of PhrB DNA binding and bending in vitro A. Fluorescence anisotropy of PhrB plotted at increasing protein concentrations per amount of 30 bp dsDNA oligonucleotide substrate (o30dsDNA). Error bars represent the standard error of the mean for 3 independent experiments with a total of 6 replicates. B. Fluorescence anisotropy of PhrB plotted at increasing protein concentrations per amount of UV irradiated (1000 joules/m 2 ) o30dsDNA oligonucleotide substrate. Error bars represent the standard error of the mean for 3 independent experiments with a total of 6 replicates. C. Protein duplex DNA bending assay. Shown is a (2.5 μg/ml) chloroquine gel of plasmid DNA (pCRBlunt2bp) incubated with topoisomerase I, DNA gyrase with or without the addition of topoisomerase I, and increasing concentrations of PhrB to DNA (1:1, 10:1, 100:1) with or without the addition of topoisomerase I. The direction of migration of less negatively supercoiled DNA (+) and more negatively supercoiled DNA (−) is indicated.

    Techniques Used: Binding Assay, In Vitro, Fluorescence, Irradiation, Plasmid Preparation, Incubation, Migration

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    New England Biolabs e coli topo i
    Constructing ssRNA topological structures with the junction-based method. ( a ) Preparation of the ssRNA strand with uniform ends and proper end groups for the DNA-splinted <t>RNA</t> ligation. ( b ) Both the positive ( TK j ( + )) and negative ( TK j ( − )) RNA trefoil knots of the same sequence are constructed by configuring tensegrity triangles with different handedness. The same scaffolds (blue) are threaded by different staple sets (grey or purple) to form a 17-bp-edged right-handed tensegrity triangle for the positive trefoil knot, or a 14-bp-edged left-handed tensegrity triangle for the negative one, respectively. Each topology is designated by the Alexander–Briggs notation n i or , where n is the minimal number of nodes, C is the number of components (for links), and i distinguishes different topologies with the same n and C . ( c ) dPAGE analysis of TK j ( + ) (lanes 1 and 2), TK j ( − ) (lanes 3 and 4), and their circular ( C j , lanes 5 and 6) and linear ( L j , lanes 7 and 8) counterparts. Lanes 2, 4, 6 and 8 contain samples digested by RNase R. ( d ) The assembly complex for the hybrid BR contains tensegrity triangles of both handedness to generate three positive nodes plus three negative nodes. ( e ) Topological analyses of the hybrid BR. Lane 1, gel-purified BR; lanes 2–6, BR treated by RNase H, Nt.AlwI (for cleaving the red ring), Nt.BspQI (for cleaving the green ring), DNase I, and E. coli DNA Topo I; lanes 7 and 8, DNA and RNA references of the three individual components. During the purification of BR, the breaking down of the 95-nt circular RNA component is unavoidable, and a portion of BR falls apart as a result. The treatment of BR by RNase H, Nt.AlwI and Nt.BspQI is conducted in the presence of an assisting DNA strand complementary to the corresponding ssRNA or ssDNA ring. LX and CX represent X-nt linear and circular species, respectively. In all the gels, lane M contains the DNA size markers.
    E Coli Topo I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli topo i/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    e coli topo i - by Bioz Stars, 2022-05
    95/100 stars
      Buy from Supplier

    Image Search Results


    Constructing ssRNA topological structures with the junction-based method. ( a ) Preparation of the ssRNA strand with uniform ends and proper end groups for the DNA-splinted RNA ligation. ( b ) Both the positive ( TK j ( + )) and negative ( TK j ( − )) RNA trefoil knots of the same sequence are constructed by configuring tensegrity triangles with different handedness. The same scaffolds (blue) are threaded by different staple sets (grey or purple) to form a 17-bp-edged right-handed tensegrity triangle for the positive trefoil knot, or a 14-bp-edged left-handed tensegrity triangle for the negative one, respectively. Each topology is designated by the Alexander–Briggs notation n i or , where n is the minimal number of nodes, C is the number of components (for links), and i distinguishes different topologies with the same n and C . ( c ) dPAGE analysis of TK j ( + ) (lanes 1 and 2), TK j ( − ) (lanes 3 and 4), and their circular ( C j , lanes 5 and 6) and linear ( L j , lanes 7 and 8) counterparts. Lanes 2, 4, 6 and 8 contain samples digested by RNase R. ( d ) The assembly complex for the hybrid BR contains tensegrity triangles of both handedness to generate three positive nodes plus three negative nodes. ( e ) Topological analyses of the hybrid BR. Lane 1, gel-purified BR; lanes 2–6, BR treated by RNase H, Nt.AlwI (for cleaving the red ring), Nt.BspQI (for cleaving the green ring), DNase I, and E. coli DNA Topo I; lanes 7 and 8, DNA and RNA references of the three individual components. During the purification of BR, the breaking down of the 95-nt circular RNA component is unavoidable, and a portion of BR falls apart as a result. The treatment of BR by RNase H, Nt.AlwI and Nt.BspQI is conducted in the presence of an assisting DNA strand complementary to the corresponding ssRNA or ssDNA ring. LX and CX represent X-nt linear and circular species, respectively. In all the gels, lane M contains the DNA size markers.

    Journal: Nature Communications

    Article Title: Synthesizing topological structures containing RNA

    doi: 10.1038/ncomms14936

    Figure Lengend Snippet: Constructing ssRNA topological structures with the junction-based method. ( a ) Preparation of the ssRNA strand with uniform ends and proper end groups for the DNA-splinted RNA ligation. ( b ) Both the positive ( TK j ( + )) and negative ( TK j ( − )) RNA trefoil knots of the same sequence are constructed by configuring tensegrity triangles with different handedness. The same scaffolds (blue) are threaded by different staple sets (grey or purple) to form a 17-bp-edged right-handed tensegrity triangle for the positive trefoil knot, or a 14-bp-edged left-handed tensegrity triangle for the negative one, respectively. Each topology is designated by the Alexander–Briggs notation n i or , where n is the minimal number of nodes, C is the number of components (for links), and i distinguishes different topologies with the same n and C . ( c ) dPAGE analysis of TK j ( + ) (lanes 1 and 2), TK j ( − ) (lanes 3 and 4), and their circular ( C j , lanes 5 and 6) and linear ( L j , lanes 7 and 8) counterparts. Lanes 2, 4, 6 and 8 contain samples digested by RNase R. ( d ) The assembly complex for the hybrid BR contains tensegrity triangles of both handedness to generate three positive nodes plus three negative nodes. ( e ) Topological analyses of the hybrid BR. Lane 1, gel-purified BR; lanes 2–6, BR treated by RNase H, Nt.AlwI (for cleaving the red ring), Nt.BspQI (for cleaving the green ring), DNase I, and E. coli DNA Topo I; lanes 7 and 8, DNA and RNA references of the three individual components. During the purification of BR, the breaking down of the 95-nt circular RNA component is unavoidable, and a portion of BR falls apart as a result. The treatment of BR by RNase H, Nt.AlwI and Nt.BspQI is conducted in the presence of an assisting DNA strand complementary to the corresponding ssRNA or ssDNA ring. LX and CX represent X-nt linear and circular species, respectively. In all the gels, lane M contains the DNA size markers.

    Article Snippet: Commercial product of E. coli Topo I (NEB) was also tested and its RNA Topo activity was found to be slightly higher than that of the in-house prepared WT enzyme, probably due to the contamination of E. coli Topo III ( ).

    Techniques: Ligation, Sequencing, Construct, Purification

    Comparing probes for RNA topoisomerase (RNA Topo) activity. ( a ) dPAGE analyses of various structures: monomeric linear ( L h , lane 1), trefoil knot ( TK h , lane 2), and circular ( C h , lane 3) RNA molecules with the sequence for helix-based topological structures; dimeric granny knot ( GK h , lane 4), and circular ( C2 h , lane 5) species with the same sequence; and the junction-based negative trefoil knot ( TK j , lane 6). ( b ) Hypothetical conversions of junction-based (between C j and TK j ) and helix-based (between C h and TK h , and between C2 h , TK2 h and GK h ) topological structures under ‘ideal' RNA Topo condition, when the RNA strand-passage event can freely take place. ( c – e ) Topological relaxations of TK j ( c ), C h ( d ) and C2 h ( e ) catalysed by increasing concentrations of WT E. coli DNA Topo I (30 min incubation at 37 °C). In c , e , the RNA probe substrates ( TK j or C2 h ) were 80 nM and Topo I in lanes 1–4 was 40, 80, 160 and 320 nM. In d , the RNA probe substrate ( C h ) was 160 nM and Topo I in lanes 1–4 was 80, 160, 320 and 640 nM. In e , C2 h is relaxed to the trefoil knot TK2 h and to GK h after one and two strand-passage events, respectively. All lanes contain the linear break-down products of the closed RNA structures and they are annotated by LX, in which X represents X-mer.

    Journal: Nature Communications

    Article Title: Synthesizing topological structures containing RNA

    doi: 10.1038/ncomms14936

    Figure Lengend Snippet: Comparing probes for RNA topoisomerase (RNA Topo) activity. ( a ) dPAGE analyses of various structures: monomeric linear ( L h , lane 1), trefoil knot ( TK h , lane 2), and circular ( C h , lane 3) RNA molecules with the sequence for helix-based topological structures; dimeric granny knot ( GK h , lane 4), and circular ( C2 h , lane 5) species with the same sequence; and the junction-based negative trefoil knot ( TK j , lane 6). ( b ) Hypothetical conversions of junction-based (between C j and TK j ) and helix-based (between C h and TK h , and between C2 h , TK2 h and GK h ) topological structures under ‘ideal' RNA Topo condition, when the RNA strand-passage event can freely take place. ( c – e ) Topological relaxations of TK j ( c ), C h ( d ) and C2 h ( e ) catalysed by increasing concentrations of WT E. coli DNA Topo I (30 min incubation at 37 °C). In c , e , the RNA probe substrates ( TK j or C2 h ) were 80 nM and Topo I in lanes 1–4 was 40, 80, 160 and 320 nM. In d , the RNA probe substrate ( C h ) was 160 nM and Topo I in lanes 1–4 was 80, 160, 320 and 640 nM. In e , C2 h is relaxed to the trefoil knot TK2 h and to GK h after one and two strand-passage events, respectively. All lanes contain the linear break-down products of the closed RNA structures and they are annotated by LX, in which X represents X-mer.

    Article Snippet: Commercial product of E. coli Topo I (NEB) was also tested and its RNA Topo activity was found to be slightly higher than that of the in-house prepared WT enzyme, probably due to the contamination of E. coli Topo III ( ).

    Techniques: Activity Assay, Sequencing, Incubation

    Release of topological tension from supercoiled pUC19 using the topoisomerase I-mediated relaxation assay in the presence Ag-phendione ( A ) or Cu-phendione ( B ). pUC19 treated with increasing concentrations of Ag-phendione in the absence of reductant over 24 h ( C ). pUC19 treated with increasing concentrations of Cu-phendione in the absence of reductant over 3 h ( D )

    Journal: Journal of Biological Inorganic Chemistry

    Article Title: Copper(II) and silver(I)-1,10-phenanthroline-5,6-dione complexes interact with double-stranded DNA: further evidence of their apparent multi-modal activity towards Pseudomonas aeruginosa

    doi: 10.1007/s00775-021-01922-3

    Figure Lengend Snippet: Release of topological tension from supercoiled pUC19 using the topoisomerase I-mediated relaxation assay in the presence Ag-phendione ( A ) or Cu-phendione ( B ). pUC19 treated with increasing concentrations of Ag-phendione in the absence of reductant over 24 h ( C ). pUC19 treated with increasing concentrations of Cu-phendione in the absence of reductant over 3 h ( D )

    Article Snippet: One unit of topoisomerase I (E. coli) (NEB) was added to the mixture and incubated for 20 min at 37 °C.

    Techniques:

    Topoisomerase I relaxes negative supercoiled plasmid DNA in present RstA. Lane 1, 0.4 μg pUC19 plasmid with no added protein. Lane 2, 0.4 μg pUC19 plasmid with BSA protein. And the other lanes contain the same concentrations of plasmid as lane 2, but different amounts of purified protein. Lanes 3–8 contain decreasing amounts of purified RstA protein (from 500 ng to 0 μg) and one unit Topoisomerase I. Lane 9, 500 ng purified RstA protein without Topoisomerase I. 6×loading buffer was added to stop the reaction and analyzed by 0.8% agrose gel electrophoresis.

    Journal: PLoS ONE

    Article Title: Absence of RstA results in delayed initiation of DNA replication in Escherichia coli

    doi: 10.1371/journal.pone.0200688

    Figure Lengend Snippet: Topoisomerase I relaxes negative supercoiled plasmid DNA in present RstA. Lane 1, 0.4 μg pUC19 plasmid with no added protein. Lane 2, 0.4 μg pUC19 plasmid with BSA protein. And the other lanes contain the same concentrations of plasmid as lane 2, but different amounts of purified protein. Lanes 3–8 contain decreasing amounts of purified RstA protein (from 500 ng to 0 μg) and one unit Topoisomerase I. Lane 9, 500 ng purified RstA protein without Topoisomerase I. 6×loading buffer was added to stop the reaction and analyzed by 0.8% agrose gel electrophoresis.

    Article Snippet: Add various amounts of purified RstA or one unit E . coli topoisomerase I protein (NEB, USA) to the tubes, then incubate 10 min at 37°C.

    Techniques: Plasmid Preparation, Purification, Nucleic Acid Electrophoresis

    ( A ) Mean tail moments of untreated SKOV-3 cells and 1.0 μM Cu-Oda, Cu-Terph and Dox. ( B ) Topoisomerase I unwinding across concentration range 0.10–400 μM for Cu-Oda and Cu-Terph . ( C ). DSBs induced by Cu-Oda and Cu-Terph , detected by immunostaining of γH2AX with MFI presented for di -Cu 2+ complexes and Dox. ( D ) CD spectra of Cu-Oda with stDNA and alternating co-polymers poly[d(A⋅T) 2 ] and poly[d(G⋅C) 2 ] (100 μM) at loading ratios 0.01–0.075.

    Journal: Nucleic Acids Research

    Article Title: Di-copper metallodrugs promote NCI-60 chemotherapy via singlet oxygen and superoxide production with tandem TA/TA and AT/AT oligonucleotide discrimination

    doi: 10.1093/nar/gky105

    Figure Lengend Snippet: ( A ) Mean tail moments of untreated SKOV-3 cells and 1.0 μM Cu-Oda, Cu-Terph and Dox. ( B ) Topoisomerase I unwinding across concentration range 0.10–400 μM for Cu-Oda and Cu-Terph . ( C ). DSBs induced by Cu-Oda and Cu-Terph , detected by immunostaining of γH2AX with MFI presented for di -Cu 2+ complexes and Dox. ( D ) CD spectra of Cu-Oda with stDNA and alternating co-polymers poly[d(A⋅T) 2 ] and poly[d(G⋅C) 2 ] (100 μM) at loading ratios 0.01–0.075.

    Article Snippet: Doxorubicin (Dox) hydrochloride (D2975000), dihydroethidium (D7008), salmon testes DNA (D1626), synthetic double stranded alternating co-polymers, poly[d(G⋅C)2 ] (P9389) and poly[d(A⋅T)2 ] (P0883) and Micrococcus Lysodeikticus (D8259) were purchased from Sigma-Aldrich. pUC19 plasmid DNA (N3041), CutSmart® buffer (B7204), 100× bovine serum albumin (BSA) (B9000) and topoisomerase I (E. coli) (M0301) were all purchased from New England Biolabs.

    Techniques: Concentration Assay, Immunostaining