e.coli reca Search Results


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  • 95
    New England Biolabs e coli reca protein
    D-loop formation promoted by <t>RecA.</t> ( A ) Reaction was performed between pCH110-G1651A plasmid DNA and the X1 <t>ODN</t> in the absence of RecA. Lane 1 represents ethidium-bromide staining of the agarose gel and in lane 2 its autoradiogram. ( B ) Joint formation was performed between pCH110-G1651A plasmid DNA and the ODN-RecA pre-synaptic filament. After deproteinization, synaptic complexes were analyzed on 0.8% agarose gel. The plasmid DNA was visualized by ethidium-bromide staining (left), whereas joint molecules were detected by autoradiography (right). Lanes 1 and 2 depict the X1-JM and X2-JM, respectively. ( C ) Autoradiogram of the purified joints. Lanes 1 and 2 depict X1- and X2-JM, respectively, after removal of unbound ODN. ( D ) Stability of D-loop. After deproteinization, synaptic complexes were incubated at indicated temperatures for 30 min and analyzed on 0.8% agarose gel. Arrows indicate the position of supercoiled DNA (SC), nicked circle (NC) and the D-loop. Arrow with asterisk indicates unincorporated ODN.
    E Coli Reca Protein, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli reca protein/product/New England Biolabs
    Average 95 stars, based on 40 article reviews
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    e coli reca protein - by Bioz Stars, 2020-09
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    86
    ATCC reca positive e coli rr1
    D-loop formation promoted by <t>RecA.</t> ( A ) Reaction was performed between pCH110-G1651A plasmid DNA and the X1 <t>ODN</t> in the absence of RecA. Lane 1 represents ethidium-bromide staining of the agarose gel and in lane 2 its autoradiogram. ( B ) Joint formation was performed between pCH110-G1651A plasmid DNA and the ODN-RecA pre-synaptic filament. After deproteinization, synaptic complexes were analyzed on 0.8% agarose gel. The plasmid DNA was visualized by ethidium-bromide staining (left), whereas joint molecules were detected by autoradiography (right). Lanes 1 and 2 depict the X1-JM and X2-JM, respectively. ( C ) Autoradiogram of the purified joints. Lanes 1 and 2 depict X1- and X2-JM, respectively, after removal of unbound ODN. ( D ) Stability of D-loop. After deproteinization, synaptic complexes were incubated at indicated temperatures for 30 min and analyzed on 0.8% agarose gel. Arrows indicate the position of supercoiled DNA (SC), nicked circle (NC) and the D-loop. Arrow with asterisk indicates unincorporated ODN.
    Reca Positive E Coli Rr1, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/reca positive e coli rr1/product/ATCC
    Average 86 stars, based on 11 article reviews
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    reca positive e coli rr1 - by Bioz Stars, 2020-09
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    85
    Thermo Fisher reca e coli strain dh10b
    D-loop formation promoted by <t>RecA.</t> ( A ) Reaction was performed between pCH110-G1651A plasmid DNA and the X1 <t>ODN</t> in the absence of RecA. Lane 1 represents ethidium-bromide staining of the agarose gel and in lane 2 its autoradiogram. ( B ) Joint formation was performed between pCH110-G1651A plasmid DNA and the ODN-RecA pre-synaptic filament. After deproteinization, synaptic complexes were analyzed on 0.8% agarose gel. The plasmid DNA was visualized by ethidium-bromide staining (left), whereas joint molecules were detected by autoradiography (right). Lanes 1 and 2 depict the X1-JM and X2-JM, respectively. ( C ) Autoradiogram of the purified joints. Lanes 1 and 2 depict X1- and X2-JM, respectively, after removal of unbound ODN. ( D ) Stability of D-loop. After deproteinization, synaptic complexes were incubated at indicated temperatures for 30 min and analyzed on 0.8% agarose gel. Arrows indicate the position of supercoiled DNA (SC), nicked circle (NC) and the D-loop. Arrow with asterisk indicates unincorporated ODN.
    Reca E Coli Strain Dh10b, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare e coli reca
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    E Coli Reca, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 10 article reviews
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    86
    Cosmo Bio anti reca escherichia coli rabbit
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    Anti Reca Escherichia Coli Rabbit, supplied by Cosmo Bio, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Abcam rabbit polyclonal antibody against e coli reca protein
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    Rabbit Polyclonal Antibody Against E Coli Reca Protein, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher competent reca escherichia coli
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    Competent Reca Escherichia Coli, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher e coli reca strain dh5 α
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    E Coli Reca Strain Dh5 α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 11 article reviews
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    e coli reca strain dh5 α - by Bioz Stars, 2020-09
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    88
    Promega e coli reca protein
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    E Coli Reca Protein, supplied by Promega, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli reca protein/product/Promega
    Average 88 stars, based on 4 article reviews
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    e coli reca protein - by Bioz Stars, 2020-09
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    99
    Millipore e coli reca
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    E Coli Reca, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli reca/product/Millipore
    Average 99 stars, based on 11 article reviews
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    85
    Stratagene e coli xl1 blue reca enda1 gyra96 thi 1 hsdr17 supe44 rela1 lac
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    E Coli Xl1 Blue Reca Enda1 Gyra96 Thi 1 Hsdr17 Supe44 Rela1 Lac, supplied by Stratagene, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher reca mutant e coli strains
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    Reca Mutant E Coli Strains, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    reca mutant e coli strains - by Bioz Stars, 2020-09
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    85
    Research Genetics Inc reca e coli dh10b
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    Reca E Coli Dh10b, supplied by Research Genetics Inc, used in various techniques. Bioz Stars score: 85/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 13 article reviews
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    reca e coli dh10b - by Bioz Stars, 2020-09
    85/100 stars
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    85
    Stratagene reca deficient escherichia coli strain xl1 blue
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    Reca Deficient Escherichia Coli Strain Xl1 Blue, supplied by Stratagene, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher reca muntant escherichia coli strains dh5αmcr
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    Reca Muntant Escherichia Coli Strains Dh5αmcr, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC δ reca e coli
    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of <t>ssDNA</t> ( C ) on the ATP hydrolysis mediated by <t>RecA</t> Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.
    δ Reca E Coli, supplied by ATCC, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    D-loop formation promoted by RecA. ( A ) Reaction was performed between pCH110-G1651A plasmid DNA and the X1 ODN in the absence of RecA. Lane 1 represents ethidium-bromide staining of the agarose gel and in lane 2 its autoradiogram. ( B ) Joint formation was performed between pCH110-G1651A plasmid DNA and the ODN-RecA pre-synaptic filament. After deproteinization, synaptic complexes were analyzed on 0.8% agarose gel. The plasmid DNA was visualized by ethidium-bromide staining (left), whereas joint molecules were detected by autoradiography (right). Lanes 1 and 2 depict the X1-JM and X2-JM, respectively. ( C ) Autoradiogram of the purified joints. Lanes 1 and 2 depict X1- and X2-JM, respectively, after removal of unbound ODN. ( D ) Stability of D-loop. After deproteinization, synaptic complexes were incubated at indicated temperatures for 30 min and analyzed on 0.8% agarose gel. Arrows indicate the position of supercoiled DNA (SC), nicked circle (NC) and the D-loop. Arrow with asterisk indicates unincorporated ODN.

    Journal: Nucleic Acids Research

    Article Title: Transcription affects formation and processing of intermediates in oligonucleotide-mediated gene alteration

    doi:

    Figure Lengend Snippet: D-loop formation promoted by RecA. ( A ) Reaction was performed between pCH110-G1651A plasmid DNA and the X1 ODN in the absence of RecA. Lane 1 represents ethidium-bromide staining of the agarose gel and in lane 2 its autoradiogram. ( B ) Joint formation was performed between pCH110-G1651A plasmid DNA and the ODN-RecA pre-synaptic filament. After deproteinization, synaptic complexes were analyzed on 0.8% agarose gel. The plasmid DNA was visualized by ethidium-bromide staining (left), whereas joint molecules were detected by autoradiography (right). Lanes 1 and 2 depict the X1-JM and X2-JM, respectively. ( C ) Autoradiogram of the purified joints. Lanes 1 and 2 depict X1- and X2-JM, respectively, after removal of unbound ODN. ( D ) Stability of D-loop. After deproteinization, synaptic complexes were incubated at indicated temperatures for 30 min and analyzed on 0.8% agarose gel. Arrows indicate the position of supercoiled DNA (SC), nicked circle (NC) and the D-loop. Arrow with asterisk indicates unincorporated ODN.

    Article Snippet: Initially, the 32 P 5′-labeled ODN (84 nM) was pre-incubated with 2.0 µg of E.coli RecA protein (New England Biolabs, Beverly, MA) in a reaction buffer containing Tris–HCl at pH 7.4, 1 mM DTT, 1.0 mM Mg(OAc)2 , 0.3 mM ATPγS, 100 mg/ml BSA in a total volume of 20 µl for 15 min at 37°C.

    Techniques: Plasmid Preparation, Staining, Agarose Gel Electrophoresis, Autoradiography, Purification, Incubation

    Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of ssDNA ( C ) on the ATP hydrolysis mediated by RecA Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.

    Journal: Brazilian Journal of Medical and Biological Research

    Article Title: The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae

    doi: 10.1590/S0100-879X2012007500160

    Figure Lengend Snippet: Effect of the RecX Hs protein concentration ( A ), the order of its addition ( B ) and the effect of ssDNA ( C ) on the ATP hydrolysis mediated by RecA Hs . A , The RecA Hs protein, φX174 circular ssDNA and increasing concentrations of RecX Hs protein (0 µM, filled triangles; 0.1 µm, filled squares; 0.5 µm, open squares; 2 µm, crosses; 5 µm, open triangles; 10 µM, filled circles) were incubated in ATPase buffer at 37°C for 10 min. After this period, the SSB protein and [α 32 P]-ATP were added. As a control without RecA, 5 µM RecX Hs was incubated with ssDNA (open lozenges). B , Two of the following components: φX174 circular ssDNA, RecA Hs and RecX Hs proteins were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, the third component (RecX, ssDNA or RecA) was added together with the SSB protein and [α 32 P]-ATP (filled squares, filled circles, open squares). Alternatively, all three components were pre-incubated together under the same conditions, before the addition of the SSB protein and [α 32 P]-ATP after 10 min (crosses). As controls, RecA Hs was incubated with ssDNA in the absence of RecX (filled triangles) or incubated with RecX Hs in the absence of ssDNA (open lozenges). C , RecX Hs (0.5 or 5 µM) and φX174 circular ssDNA were pre-incubated in ATPase buffer at 37°C for 10 min. After this period, RecA alone (filled lozenges, open triangles), RecA plus ssDNA (132 µM, open squares) or RecA and then ssDNA (132 µM, added just 20 min later, as indicated by the gray arrow; filled squares) were added together with the SSB protein and [α 32 P]-ATP. The concentration of RecA Hs was unchanged and ssDNA [↑] and RecX [↓] indicate the following unusual concentrations: 132 µM ssDNA and 0.5 µM RecX, respectively. In all of the assays after the addition of [α 32 P]-ATP (zero time), aliquots were collected and stopped.

    Article Snippet: ATP hydrolysis by the H. seropedicae RecA protein in the presence of ssDNA was slightly less efficient than the E. coli RecA.

    Techniques: Protein Concentration, Incubation, Concentration Assay

    Inhibition by RecX of RecA-mediated DNA strand exchange and ATP binding. Effect of increasing concentrations of the RecX Hs protein on the DNA strand exchange mediated by Herbaspirillum seropedicae RecA (RecA Hs ) ( A ) or Escherichia coli RecA (RecA Ec ) ( B ). Effect of RecX Hs on the RecA ATP-binding activity ( C ). (+) indicates the presence and (-) the absence of the indicated components. S 1 is circular ssDNA, S 2 is linear dsDNA and P is nicked circular dsDNA.

    Journal: Brazilian Journal of Medical and Biological Research

    Article Title: The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae

    doi: 10.1590/S0100-879X2012007500160

    Figure Lengend Snippet: Inhibition by RecX of RecA-mediated DNA strand exchange and ATP binding. Effect of increasing concentrations of the RecX Hs protein on the DNA strand exchange mediated by Herbaspirillum seropedicae RecA (RecA Hs ) ( A ) or Escherichia coli RecA (RecA Ec ) ( B ). Effect of RecX Hs on the RecA ATP-binding activity ( C ). (+) indicates the presence and (-) the absence of the indicated components. S 1 is circular ssDNA, S 2 is linear dsDNA and P is nicked circular dsDNA.

    Article Snippet: ATP hydrolysis by the H. seropedicae RecA protein in the presence of ssDNA was slightly less efficient than the E. coli RecA.

    Techniques: Inhibition, Binding Assay, Activity Assay