pgex 2t Ge Healthcare Search Results


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  • 95
    Millipore pgex 4t 1 expression vector
    Pgex 4t 1 Expression Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare pgex 2t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 2196 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare bamhi noti digested pgex 2t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Bamhi Noti Digested Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    GE Healthcare pgex 2t expression system
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t Expression System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 81/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare bamhi ecori restricted pgex 2t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Bamhi Ecori Restricted Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    GE Healthcare pgex 2t plasmid
    The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the <t>pGEX-2T</t> plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).
    Pgex 2t Plasmid, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 445 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare pgex 2t 4t
    The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the <t>pGEX-2T</t> plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).
    Pgex 2t 4t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    GE Healthcare gst empty vector pgex 2t
    The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the <t>pGEX-2T</t> plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).
    Gst Empty Vector Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare various gst fusion pgex 2t
    The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the <t>pGEX-2T</t> plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).
    Various Gst Fusion Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    GE Healthcare pgex 2t expression plasmid
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Pgex 2t Expression Plasmid, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare gst containing pgex 2t plasmid
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Gst Containing Pgex 2t Plasmid, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare template pgex 2t
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Template Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    GE Healthcare pgex 2t plin2
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Pgex 2t Plin2, supplied by GE Healthcare, 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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    86
    GE Healthcare overexpression vector pgex 2t
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Overexpression Vector Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    GE Healthcare bamhi hindiii digested pgex 2t
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Bamhi Hindiii Digested Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GE Healthcare gst fusion vector pgex 2t
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Gst Fusion Vector Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    GE Healthcare pgex 2t bacterial expression vector
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Pgex 2t Bacterial Expression Vector, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    GE Healthcare pgex 2t gst expression vector
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Pgex 2t Gst Expression Vector, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 91/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare prokaryotic expression plasmid pgex 2t
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Prokaryotic Expression Plasmid Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare pgex 2t 1
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
    Pgex 2t 1, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare bamhi digested pgex 2t
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    GE Healthcare pgex 2t system
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    GE Healthcare pgex 2t pgex 3x
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    GE Healthcare expression vector pgex 2t linkeri
    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    GE Healthcare s japonicum gst fusions
    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    GE Healthcare xho i digested pgex 2t vector
    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    GE Healthcare bamhi ecori digested vector pgex 2t
    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    GE Healthcare recombinant proteins pgex 2t
    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. <t>japonicum</t> <t>GST-HPV-16</t> E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.
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    Image Search Results


    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.

    Journal: Biochemical Journal

    Article Title: Characterization of a sterol carrier protein 2/3-oxoacyl-CoA thiolase from the cotton leafworm (Spodoptera littoralis): a lepidopteran mechanism closer to that in mammals than that in dipterans

    doi: 10.1042/BJ20040717

    Figure Lengend Snippet: Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.

    Article Snippet: The product was cut out with Bam HI and Eco RI from the plasmid and transferred into pGEX-2T (Amersham Biosciences).

    Techniques: Western Blot, Recombinant, Plasmid Preparation, Expressing

    The developmental profile of SCPx during the sixth instar ( A ) A 10 #x3BC;g portion of total RNA from midgut at various time points within the sixth larval instar, as indicated, was used. The blot was hybridized with a 32 P-labelled SCPx cDNA probe corresponding to the open reading frame. The same blot was stripped and reprobed with 18S rRNA probe. G, W and PP refer to the stages ‘gut purge’, ‘wandering’and ‘prepupa’ respectively that occur before pupation. ( B ) Western-blot analysis of SCPx protein. Top panel: 100 #x3BC;g of protein from midgut at various time points within the sixth larval instar, as indicated, was used. Bottom panel: Western-blot analysis of the recombinant S. littoralis SCPx protein. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing the SCPx cDNA without induction of expression; lane 3, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression; lane 4, whole extract from C. elegans . The antibody against C. elegans P-44 was used to detect the SCPx protein.

    Journal: Biochemical Journal

    Article Title: Characterization of a sterol carrier protein 2/3-oxoacyl-CoA thiolase from the cotton leafworm (Spodoptera littoralis): a lepidopteran mechanism closer to that in mammals than that in dipterans

    doi: 10.1042/BJ20040717

    Figure Lengend Snippet: The developmental profile of SCPx during the sixth instar ( A ) A 10 #x3BC;g portion of total RNA from midgut at various time points within the sixth larval instar, as indicated, was used. The blot was hybridized with a 32 P-labelled SCPx cDNA probe corresponding to the open reading frame. The same blot was stripped and reprobed with 18S rRNA probe. G, W and PP refer to the stages ‘gut purge’, ‘wandering’and ‘prepupa’ respectively that occur before pupation. ( B ) Western-blot analysis of SCPx protein. Top panel: 100 #x3BC;g of protein from midgut at various time points within the sixth larval instar, as indicated, was used. Bottom panel: Western-blot analysis of the recombinant S. littoralis SCPx protein. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing the SCPx cDNA without induction of expression; lane 3, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression; lane 4, whole extract from C. elegans . The antibody against C. elegans P-44 was used to detect the SCPx protein.

    Article Snippet: The product was cut out with Bam HI and Eco RI from the plasmid and transferred into pGEX-2T (Amersham Biosciences).

    Techniques: Western Blot, Recombinant, Plasmid Preparation, Expressing

    The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the pGEX-2T plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).

    Journal: Nucleic Acids Research

    Article Title: Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain

    doi: 10.1093/nar/gkm162

    Figure Lengend Snippet: The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the pGEX-2T plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).

    Article Snippet: Construction of expression vectors, site-directed mutagenesis, overexpression and purification of the wild-type and mutant proteins The plasmid pGEX-2T (Amersham Biosciences, Freiburg, Germany) containing the lac Iq gene was used for the expression of DBDs as fusion proteins with Schistosoma japonicum glutathione-S-transferase (GST) in Escherichia coli strain BL21(DE3)pLysS (Novagen, Germany).

    Techniques: Construct, Crystallization Assay, Clone Assay, Plasmid Preparation

    (A) Schematic representation of various truncated p53 constructs and TIP30. p53 constructs were fused in frame to the 3′ end of the GST gene in the pGEX-2T vector. His-tagged constructs of TIP30 and p53 DBD or CTD were fused in frame at the 3′

    Journal: Molecules and Cells

    Article Title: TIP30 Directly Binds p53 Tumor Suppressor Protein In Vitro

    doi: 10.1007/s10059-012-0232-x

    Figure Lengend Snippet: (A) Schematic representation of various truncated p53 constructs and TIP30. p53 constructs were fused in frame to the 3′ end of the GST gene in the pGEX-2T vector. His-tagged constructs of TIP30 and p53 DBD or CTD were fused in frame at the 3′

    Article Snippet: GST-tagged p53 constructs for use in GST pull-down assays were prepared by digesting PCR products with Bam HI and Eco RI and inserting into the corresponding sites in the pGEX-2T vector (GE Healthcare).

    Techniques: Construct, Plasmid Preparation

    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector pGEX-2T. b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences

    Journal: Inflammation Research

    Article Title: Monoclonal antibodies for human and porcine histamine N-methyltransferase (HMT) facilitate protein expression and localization studies

    doi: 10.1007/s00011-016-0987-1

    Figure Lengend Snippet: Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector pGEX-2T. b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences

    Article Snippet: Preparation of recombinant HMT proteins Full-length human and porcine HMT cDNAs [ , , ] were amplified by PCR with specific primers from total human and porcine kidney cDNA, respectively, and cloned in frame into the bacterial expression vector pGEX-2T (GE Healthcare, Vienna, Austria).

    Techniques: Recombinant, HMT Assay, Clone Assay, Expressing, Plasmid Preparation, Staining, Purification, Mouse Assay, Molecular Weight, Sequencing, Produced

    HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. japonicum GST-HPV-16 E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.

    Journal: PLoS ONE

    Article Title: Human Papillomavirus-16 E7 Interacts with Glutathione S-Transferase P1 and Enhances Its Role in Cell Survival

    doi: 10.1371/journal.pone.0007254

    Figure Lengend Snippet: HPV-16 E7 physically interacts with GSTP1. A: HaCaT cell lysate was incubated with the S. japonicum GST-HPV-16 E7 chimeric protein. Co-precipitated proteins were separated by SDS-PAGE and visualized after silver staining. The dotted arrow indicates the band that was cut out and identified by peptide mass fingerprinting as human GSTP1. B: In vitro interaction of radiolabeled IVT HPV-16 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein. C: Western blot for GSTP1 after immunoprecipitation with an anti-T7 Tag antibody (to precipitate tagged HPV-16 E7), in control and HPV-16 E7-transfected Phoenix cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. D: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of GSTP1 only in HPV-16 E7-expressing cells. E: Western blot using an anti-HA antibody (to detect tagged HPV-16 E7) after immunoprecipitation with an anti-GSTP1 antibody in control and HPV-16 E7-expressing HaCaT cells shows co-precipitation of HPV-16 E7. F: Western blot for GSTP1 after immunoprecipitation with an anti-HPV-16 E7 antibody in control and HPV-16 E7-expressing HaCaT cells as well as in the CaSki and SiHa cell lines expressing endogenous HPV-16 E7. G: In vitro interaction of radiolabeled IVT HPV-33 E7 and HPV-18 E7 with N-6His-GSTP1 recombinant protein and lack of interaction with control N-6His-RCC1 recombinant protein.

    Article Snippet: Recombinant HPV-16 E7 and human pRb were expressed in BL21 E. coli cells as S. japonicum GST fusions (pGEX-4T-1 and pGEX-2T, respectively; Amersham Biosciences, Piscataway, NJ), whereas human GSTP1 was expressed in BL21 E. coli cells as an N-terminally 6His-tagged protein (pDEST17; Gateway cloning system, Invitrogen).

    Techniques: Incubation, SDS Page, Silver Staining, Peptide Mass Fingerprinting, In Vitro, Recombinant, Western Blot, Immunoprecipitation, Transfection, Expressing

    Generation of HPV-16 E7 Mut and its in vitro interaction with GSTP1 and pRb. A. Legend as in Figure 3A . The red spheres shown on one HPV-16 E7 subunit (green tube representation) highlight the alpha-carbon atoms of amino acid residues 49–60, while the blue spheres highlight the alpha-carbons of amino acid residues 88–98 (see Figure 2 ). The residues Val 55, Phe 57 and Met 84, mutated in HPV-16 E7 Mut, are highlighted by the white clouds. B: In vitro interaction of radiolabeled IVT HPV-16 E7, but not of HPV-16 E7 Mut, with N-6His-GSTP1 recombinant protein. N-6His-RCC1 recombinant protein was used as a negative control. C: In vitro interaction of radiolabeled IVT HPV-16 E7 and HPV-16 E7 Mut with recombinant S. japonicum GST-pRb protein. S. japonicum GST was used as a negative control. D: Western blot for GSTP1 after immunoprecipitation with an anti-HA antibody (to precipitate tagged HPV-16 E7 and HPV-16 E7 Mut), in control, HPV-16 E7- and HPV-16 E7 Mut-expressing HaCaT cells shows a less efficient co-precipitation of GSTP1 in HPV-16 E7 Mut-expressing cells; the same membrane was probed using an anti-HA antibody to assess the efficiency of the immunoprecipitation procedure. Cell lysate was from HPV-16 E7-infected HaCaT cells. E: Reverse co-precipitation: Western blot for HA (to detect tagged HPV-16 E7 and HPV-16 E7 Mut) after immunoprecipitation with an anti-GSTP1 antibody in control, HPV-16 E7- and HPV-16 E7 Mut-expressing HaCaT cells shows a less efficient co-precipitation of HPV-16 E7 Mut with GSTP1 when compared to HPV-16 E7; the same membrane was probed using an anti-GSTP1 antibody to assess the efficiency of the immunoprecipitation procedure. Cell lysate was from HPV-16 E7-infected HaCaT cells.

    Journal: PLoS ONE

    Article Title: Human Papillomavirus-16 E7 Interacts with Glutathione S-Transferase P1 and Enhances Its Role in Cell Survival

    doi: 10.1371/journal.pone.0007254

    Figure Lengend Snippet: Generation of HPV-16 E7 Mut and its in vitro interaction with GSTP1 and pRb. A. Legend as in Figure 3A . The red spheres shown on one HPV-16 E7 subunit (green tube representation) highlight the alpha-carbon atoms of amino acid residues 49–60, while the blue spheres highlight the alpha-carbons of amino acid residues 88–98 (see Figure 2 ). The residues Val 55, Phe 57 and Met 84, mutated in HPV-16 E7 Mut, are highlighted by the white clouds. B: In vitro interaction of radiolabeled IVT HPV-16 E7, but not of HPV-16 E7 Mut, with N-6His-GSTP1 recombinant protein. N-6His-RCC1 recombinant protein was used as a negative control. C: In vitro interaction of radiolabeled IVT HPV-16 E7 and HPV-16 E7 Mut with recombinant S. japonicum GST-pRb protein. S. japonicum GST was used as a negative control. D: Western blot for GSTP1 after immunoprecipitation with an anti-HA antibody (to precipitate tagged HPV-16 E7 and HPV-16 E7 Mut), in control, HPV-16 E7- and HPV-16 E7 Mut-expressing HaCaT cells shows a less efficient co-precipitation of GSTP1 in HPV-16 E7 Mut-expressing cells; the same membrane was probed using an anti-HA antibody to assess the efficiency of the immunoprecipitation procedure. Cell lysate was from HPV-16 E7-infected HaCaT cells. E: Reverse co-precipitation: Western blot for HA (to detect tagged HPV-16 E7 and HPV-16 E7 Mut) after immunoprecipitation with an anti-GSTP1 antibody in control, HPV-16 E7- and HPV-16 E7 Mut-expressing HaCaT cells shows a less efficient co-precipitation of HPV-16 E7 Mut with GSTP1 when compared to HPV-16 E7; the same membrane was probed using an anti-GSTP1 antibody to assess the efficiency of the immunoprecipitation procedure. Cell lysate was from HPV-16 E7-infected HaCaT cells.

    Article Snippet: Recombinant HPV-16 E7 and human pRb were expressed in BL21 E. coli cells as S. japonicum GST fusions (pGEX-4T-1 and pGEX-2T, respectively; Amersham Biosciences, Piscataway, NJ), whereas human GSTP1 was expressed in BL21 E. coli cells as an N-terminally 6His-tagged protein (pDEST17; Gateway cloning system, Invitrogen).

    Techniques: In Vitro, Recombinant, Negative Control, Western Blot, Immunoprecipitation, Expressing, Infection