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  • 99
    Millipore escherichia coli pet28
    Escherichia Coli Pet28, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet 28
    Pet 28, supplied by Millipore, used in various techniques. Bioz Stars score: 87/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet 28 vector
    Pet 28 Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet28 a
    Pet28 A, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 144 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet28
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet28, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1694 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck & Co pet28
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet28, supplied by Merck & Co, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher pet28
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet28, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 101 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck KGaA pet28
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet28, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 89/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa pet28
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet28, supplied by TaKaRa, used in various techniques. Bioz Stars score: 90/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson pet28
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet28, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 87/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio Basic Canada pet28
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet28, supplied by Bio Basic Canada, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet 28 sumo plasmid
    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying <t>pET28_lux</t> plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.
    Pet 28 Sumo Plasmid, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet28 b
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    Pet28 B, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Addgene inc pet28 mhl
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    Pet28 Mhl, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet 28 expression vector
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    Pet 28 Expression Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 228 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet28 c
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    Pet28 C, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 58 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Addgene inc pet28 hpkm1
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    Pet28 Hpkm1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher expression vector pet 28
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    Expression Vector Pet 28, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore 1 thio­galactopyranoside inducible pet 28 vector
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    1 Thio­Galactopyranoside Inducible Pet 28 Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pet28 a
    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either <t>pET28-b</t> or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.
    Pet28 A, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene pet28
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28, supplied by Stratagene, used in various techniques. Bioz Stars score: 90/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore vector pet28
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Vector Pet28, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 256 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New Brunswick Scientific pet28
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28, supplied by New Brunswick Scientific, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Addgene inc pet28
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher pet28 a vector
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28 A Vector, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GenScript pet28
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28, supplied by GenScript, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GenScript pet28 vector
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28 Vector, supplied by GenScript, used in various techniques. Bioz Stars score: 94/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa pet28 plasmid
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28 Plasmid, supplied by TaKaRa, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Expression Systems Inc pet 28 expression system
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet 28 Expression System, supplied by Expression Systems Inc, 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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    Merck KGaA novagen pet28 vector
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Novagen Pet28 Vector, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet28 hmt vectors
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28 Hmt Vectors, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pet28 expression vectors
    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the <t>pET28</t> vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.
    Pet28 Expression Vectors, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying pET28_lux plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.

    Journal: Nucleic Acids Research

    Article Title: Controller protein of restriction–modification system Kpn2I affects transcription of its gene by acting as a transcription elongation roadblock

    doi: 10.1093/nar/gky880

    Figure Lengend Snippet: C.Kpn2I binding inhibits transcription elongation through the binding site. ( A ) At the top, three DNA fragments used as templates in in vitro transcription reactions are shown. Expected sizes of run-off transcripts and the position of the C.Kpn2I binding site relative to transcription start point (black bent arrow) are indicated. The gel below shows the results of transcription from the three templates in the presence or in the absence of C.Kpn2I. Where indicated, reactions were supplemented with transcript cleavage factor GreA. ( B ) At the top, schemes of plasmids used in in vivo experiment are shown. Distances from transcription start site and C.Kpn2I binding site in these constructs are the same as in the Kpn2I system. Levels of luminescence of cells carrying pET28_lux plasmid with a compatible pACYC plasmid with or without the kpn 2I. C gene were measured in the presence or absence of rhamnose. Mean values and standard deviations obtained from four independent experiments are presented.

    Article Snippet: To generate pCkpn2I-6His plasmid for expression of hexahistidine-tagged C.Kpn2I, a 321-bp PCR fragment containing the kpn 2I.C gene with incorporated flanking NdeI and EcoRI restriction sites was inserted between the NdeI and EcoRI sites of pET28 (Novagen).

    Techniques: Binding Assay, In Vitro, In Vivo, Construct, Plasmid Preparation

    Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either pET28-b or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.

    Journal: Journal of Bacteriology

    Article Title: The Alternative Sigma Factor ?B of Bacillus cereus: Response to Stress and Role in Heat Adaptation

    doi: 10.1128/JB.186.2.316-325.2004

    Figure Lengend Snippet: Overproduction and purification of σ B . (Left panel) SDS-PAGE of protein extracts from E. coli BL21-Codonplus-(DE3)-RIL carrying either pET28-b or pMT01. (Right panel) Immunodetection of σ B with anti-σ B antiserum. Ten micrograms of protein was loaded for each sample. Lane 1, crude protein extract from E. coli carrying pET28-b; lane 2, crude protein extract from E. coli carrying pMT01; lane 3, crude protein extract from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 4, inclusion bodies isolated from E. coli carrying pMT01 after induction with 1 mM IPTG for 2 h; lane 5, representative fraction of purified σ B after elution from an Ni 2+ affinity column. The arrow indicates the position of the overproduced σ B protein.

    Article Snippet: The PCR product was cloned into pET28-b (Novagen, Madison, Wis.), and the resulting vector (pMT01) was transformed into E. coli BL21-Codonplus-(DE3)-RIL.

    Techniques: Purification, SDS Page, Immunodetection, Isolation, Affinity Column

    Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the pET28 vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.

    Journal: Plant Physiology

    Article Title: A Novel Red Clover Hydroxycinnamoyl Transferase Has Enzymatic Activities Consistent with a Role in Phaselic Acid Biosynthesis 1A Novel Red Clover Hydroxycinnamoyl Transferase Has Enzymatic Activities Consistent with a Role in Phaselic Acid Biosynthesis 1 [OA]

    doi: 10.1104/pp.109.136689

    Figure Lengend Snippet: Expression of HCT1 and HCT2 proteins in E. coli . Soluble extracts (5 μ g of protein) of E. coli transformed with the pET28 vector (Vector) or HCT1 or HCT2 expression constructs were resolved on a 10% SDS-PAGE gel. Arrowheads indicate protein bands derived from the HCT1 and HCT2 expression constructs.

    Article Snippet: pET28 derivatives containing HCT1 or HCT2 coding regions (detailed above) or pET28 (as a negative control) were transformed into BL21(DE3)RIL Codon Plus E. coli (Stratagene).

    Techniques: Expressing, Transformation Assay, Plasmid Preparation, Construct, SDS Page, Derivative Assay