e coli bl21 Thermo Fisher Search Results


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  • 98
    Thermo Fisher host escherichia coli bl21
    Host Escherichia Coli Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 468 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher e coli bl21 ai thermo fisher
    E Coli Bl21 Ai Thermo Fisher, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher escherichia coli e coli bl21
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Escherichia Coli E Coli Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 246 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher escherichia coli e coli bl21 de3 cells
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Escherichia Coli E Coli Bl21 De3 Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher escherichia coli
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Escherichia Coli, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 6904 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher e coli bl21 de3
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    E Coli Bl21 De3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 1283 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher escherichia coli host
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Escherichia Coli Host, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 203 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher expression host escherichia coli bl21 star de3
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Expression Host Escherichia Coli Bl21 Star De3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher bl21 competent escherichia coli
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Bl21 Competent Escherichia Coli, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher protease deficient escherichia coli
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Protease Deficient Escherichia Coli, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher purification escherichia coli bl21
    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains <t>BL21</t> (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160
    Purification Escherichia Coli Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher e coli bl21 ai
    ( A ) SDS PAGE gel showing the heterologous expression of PnpE1 and PnpE2 in E. coli <t>BL21</t> AI. The lane M: Marker; Lane 1 4: Uninduced supernatant of pnpE1 and pnpE2; Lane 2 5: Induced whole cell lysate of pnpE1 and pnpE2; Lane 3 6: Supernatant of pnpE1 and pnpE2 (pnpE1 not present in the supernatant); Lane 7 8: purified and pnpE1 (refolded) and pnpE2 respectively ( B ) Size exclusion chromatography of subunits of hydroquinone dioxygenase using sephacryl-200 ( i ) Gel filtration of PnpE1 eluted at 59.1 ml from the column and found to be a monomer of 40 kDa, ( ii ) Gel filtration of PnpE2 eluted at 65 ml and found to be a monomer of 20 kDa, ( iii ) Mixture of both the subunits found to be eluted at approximately 44 ml and the molecular weight of the hydroquinone dioxygenase predicted as approximately 120 kDa.
    E Coli Bl21 Ai, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 598 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher escherichia coli gold bl21
    ( A ) SDS PAGE gel showing the heterologous expression of PnpE1 and PnpE2 in E. coli <t>BL21</t> AI. The lane M: Marker; Lane 1 4: Uninduced supernatant of pnpE1 and pnpE2; Lane 2 5: Induced whole cell lysate of pnpE1 and pnpE2; Lane 3 6: Supernatant of pnpE1 and pnpE2 (pnpE1 not present in the supernatant); Lane 7 8: purified and pnpE1 (refolded) and pnpE2 respectively ( B ) Size exclusion chromatography of subunits of hydroquinone dioxygenase using sephacryl-200 ( i ) Gel filtration of PnpE1 eluted at 59.1 ml from the column and found to be a monomer of 40 kDa, ( ii ) Gel filtration of PnpE2 eluted at 65 ml and found to be a monomer of 20 kDa, ( iii ) Mixture of both the subunits found to be eluted at approximately 44 ml and the molecular weight of the hydroquinone dioxygenase predicted as approximately 120 kDa.
    Escherichia Coli Gold Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains BL21 (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160

    Journal: Journal of Biomedical Science

    Article Title: Recombinant lipidated Zika virus envelope protein domain III elicits durable neutralizing antibody responses against Zika virus in mice

    doi: 10.1186/s12929-020-00646-x

    Figure Lengend Snippet: Production and purification of recombinant Zika virus envelope protein domain III (rZE3) and recombinant lipidated Zika virus envelope protein domain III (rLZE3). The plasmid maps of pZE3 ( a ) and pLZE3 ( d ) for the production of rZE3 and rLZE3, respectively. The purification of rZE3 ( b , c ) and rLZE3 ( e , f ) was monitored by 10% reducing Tricine-SDS-PAGE followed by Coomassie Blue staining and immunoblotting with anti-His-tag antibodies. rZE3 and rLZE3 were expressed in the E. coli strains BL21 (DE3) and C43 (DE3), respectively. Lanes 1, 5, 9, and 13: protein expression without IPTG induction; lanes 2, 6, 10, and 14: protein expression after IPTG induction; lanes 3 and 7: extraction of rZE3 from inclusion bodies; lanes 11 and 15: soluble fraction of rLZE3; and lanes 4, 8, 12, and 16: purified proteins. Lanes 5–8 and lanes 13–16 show the induction and purification processes for rZE3 and rLZE3, respectively, evaluated by immunoblotting. The arrows show the electrophoretic positions of rZE3 or rLZE3. g Mass spectrum analysis of rLZE3. The N-terminus of the rLZE3 fragments was obtained by trypsin digestion and further examined with a WatersR MALDI micro MX™ mass spectrometer. MALDI-TOF MS spectra revealed lipid peptide signals with three m/z value peaks of 1452.129, 1466.144, and 1480.160

    Article Snippet: For expression of rZE3, pZE3 was transformed into E. coli BL21 (Invitrogen, Carlsbad, CA).

    Techniques: Purification, Recombinant, Plasmid Preparation, SDS Page, Staining, Expressing, Mass Spectrometry

    Electron microscopy analysis of oligomerization properties of Hcp proteins. Hcp proteins fused at C terminus to a 3xAla-6xHis-tag were over-expressed in E. coli BL21 Star (Invitrogen) and purified by affinity chromatography using Ni-NTA Agarose (QIAGEN). For electron microscopy, the protein samples were diluted to a final concentration of 0.02 mg/ml and negatively stained with uranyl formate. Electron micrographs were recorded with an FEI Tecnai G2 Spirit BioTWIN electron microscope. Arrows point to polymeric structures. ( A ) PA1512 (Hcp2, P. aeruginosa PAO1), ( B ) c3391 (Hcp, E. coli CFT073), ( C ) PA2367 (Hcp3, P. aeruginosa PAO1), ( D ) An aliquot of purified PA2367 protein sample was denatured by adding solid urea (Fluka) to 8 M concentration. The protein was refolded by 500× dilution into a buffer without urea.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin

    doi: 10.1073/pnas.0813360106

    Figure Lengend Snippet: Electron microscopy analysis of oligomerization properties of Hcp proteins. Hcp proteins fused at C terminus to a 3xAla-6xHis-tag were over-expressed in E. coli BL21 Star (Invitrogen) and purified by affinity chromatography using Ni-NTA Agarose (QIAGEN). For electron microscopy, the protein samples were diluted to a final concentration of 0.02 mg/ml and negatively stained with uranyl formate. Electron micrographs were recorded with an FEI Tecnai G2 Spirit BioTWIN electron microscope. Arrows point to polymeric structures. ( A ) PA1512 (Hcp2, P. aeruginosa PAO1), ( B ) c3391 (Hcp, E. coli CFT073), ( C ) PA2367 (Hcp3, P. aeruginosa PAO1), ( D ) An aliquot of purified PA2367 protein sample was denatured by adding solid urea (Fluka) to 8 M concentration. The protein was refolded by 500× dilution into a buffer without urea.

    Article Snippet: The proteins were over-expressed using E. coli BL21 Star (Invitrogen).

    Techniques: Electron Microscopy, Purification, Affinity Chromatography, Concentration Assay, Staining, Microscopy

    ( A ) SDS PAGE gel showing the heterologous expression of PnpE1 and PnpE2 in E. coli BL21 AI. The lane M: Marker; Lane 1 4: Uninduced supernatant of pnpE1 and pnpE2; Lane 2 5: Induced whole cell lysate of pnpE1 and pnpE2; Lane 3 6: Supernatant of pnpE1 and pnpE2 (pnpE1 not present in the supernatant); Lane 7 8: purified and pnpE1 (refolded) and pnpE2 respectively ( B ) Size exclusion chromatography of subunits of hydroquinone dioxygenase using sephacryl-200 ( i ) Gel filtration of PnpE1 eluted at 59.1 ml from the column and found to be a monomer of 40 kDa, ( ii ) Gel filtration of PnpE2 eluted at 65 ml and found to be a monomer of 20 kDa, ( iii ) Mixture of both the subunits found to be eluted at approximately 44 ml and the molecular weight of the hydroquinone dioxygenase predicted as approximately 120 kDa.

    Journal: AMB Express

    Article Title: Branching of the p-nitrophenol (PNP) degradation pathway in burkholderia sp. Strain SJ98: Evidences from genetic characterization of PNP gene cluster

    doi: 10.1186/2191-0855-2-30

    Figure Lengend Snippet: ( A ) SDS PAGE gel showing the heterologous expression of PnpE1 and PnpE2 in E. coli BL21 AI. The lane M: Marker; Lane 1 4: Uninduced supernatant of pnpE1 and pnpE2; Lane 2 5: Induced whole cell lysate of pnpE1 and pnpE2; Lane 3 6: Supernatant of pnpE1 and pnpE2 (pnpE1 not present in the supernatant); Lane 7 8: purified and pnpE1 (refolded) and pnpE2 respectively ( B ) Size exclusion chromatography of subunits of hydroquinone dioxygenase using sephacryl-200 ( i ) Gel filtration of PnpE1 eluted at 59.1 ml from the column and found to be a monomer of 40 kDa, ( ii ) Gel filtration of PnpE2 eluted at 65 ml and found to be a monomer of 20 kDa, ( iii ) Mixture of both the subunits found to be eluted at approximately 44 ml and the molecular weight of the hydroquinone dioxygenase predicted as approximately 120 kDa.

    Article Snippet: Heterologous expression of pnp E1 and pnp E2 ORFs pnpE1 and pnpE2 were cloned into pDSET17 and expressed as N-terminal 6x His tagged recombinant proteins in E. coli BL21- AI (Invitrogen Inc. CA, USA).

    Techniques: SDS Page, Expressing, Marker, Purification, Size-exclusion Chromatography, Filtration, Molecular Weight

    ( A ) Enzyme activity of hydroquinone dioxygenase assayed by UV-Visible spectrophotometer. ( i ) Negative control for the hydroquinone transformation E. coli BL21-AI (without pDEST-pnpE1 and pDEST-pnpE2) cell lysate ( ii ) Hydroquinone transformed into γ-hydroxymuconic semialdehyde and detected at the wavelength 320 nm. ( B ) The percent activity of the hydroquinone at different ( i ) pHs, ( ii ) Temperatures and ( iii ) The Michaelis-menten curve for the hydroquinone dioxygenase activity.

    Journal: AMB Express

    Article Title: Branching of the p-nitrophenol (PNP) degradation pathway in burkholderia sp. Strain SJ98: Evidences from genetic characterization of PNP gene cluster

    doi: 10.1186/2191-0855-2-30

    Figure Lengend Snippet: ( A ) Enzyme activity of hydroquinone dioxygenase assayed by UV-Visible spectrophotometer. ( i ) Negative control for the hydroquinone transformation E. coli BL21-AI (without pDEST-pnpE1 and pDEST-pnpE2) cell lysate ( ii ) Hydroquinone transformed into γ-hydroxymuconic semialdehyde and detected at the wavelength 320 nm. ( B ) The percent activity of the hydroquinone at different ( i ) pHs, ( ii ) Temperatures and ( iii ) The Michaelis-menten curve for the hydroquinone dioxygenase activity.

    Article Snippet: Heterologous expression of pnp E1 and pnp E2 ORFs pnpE1 and pnpE2 were cloned into pDSET17 and expressed as N-terminal 6x His tagged recombinant proteins in E. coli BL21- AI (Invitrogen Inc. CA, USA).

    Techniques: Activity Assay, Spectrophotometry, Negative Control, Transformation Assay