pgex-2t Ge Healthcare Search Results


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  • 92
    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: 92/100, based on 2192 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 86/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 85/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 88/100, based on 440 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 80/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    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: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 85/100, based on 67 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: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare bamh i xho i restricted 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
    Bamh I Xho I Restricted Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 92/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GE Healthcare gst
    Identification of ProSAP1/Shank2 and ProSAP2/Shank3 as postsynaptically enriched Syndapin I interaction partners. (A) <t>GST–syndapin</t> I, II, and III specifically precipitate <t>GFP-ProSAP1</t> expressed in HEK293 cells. (B) Coprecipitation analysis with GST–syndapin I and deletion mutants thereof. The SH3 domain is critical and sufficient for binding. A mutant SH3 domain (P434L; SH3*) did not bind. White lines indicate lanes omitted from blots (B and F). (C) Syndapin I SH3 precipitates GFP-ProSAP1 and GFP-ProSAP2 but not GFP-Shank1. (D) Alignment of +++APPPP motifs in ProSAP1 (NCBI Protein database accession no. NP_001004133 ), ProSAP2 (accession no. NP_067708 ), and Cobl (accession no. NP_766084 ; conserved amino acids are highlighted) and of corresponding residues in Shank1 (accession no. Q9WV48 ). (E) Scheme of rat ProSAP1b and deletion mutants used. Indicated are the N-terminal PDZ domain (medium grey), several proline-rich motifs (dark grey lines), and the C-terminal SAM (sterile alpha motif) domain (light grey). (F) GST–syndapin I precipitated GFP-ProSAP1 1–235 but none of the other ProSAP1 deletion mutants. (G) GFP fusion peptides encompassing the +++APPPP motifs of ProSAP1, ProSAP2, and Cobl associated with syndapin I SH3. (H and I) RKKAPPPPKR to GAGAAAAAAG mutation (amino acids 141–150 in ProSAP1; ProSAP1 1–235*) disrupted direct binding of ProSAP1 to syndapin I in both in vitro reconstitutions with purified proteins (H) and in coprecipitation analyses (I).
    Gst, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 1872 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare overexpression vector pgex 2t
    Identification of ProSAP1/Shank2 and ProSAP2/Shank3 as postsynaptically enriched Syndapin I interaction partners. (A) <t>GST–syndapin</t> I, II, and III specifically precipitate <t>GFP-ProSAP1</t> expressed in HEK293 cells. (B) Coprecipitation analysis with GST–syndapin I and deletion mutants thereof. The SH3 domain is critical and sufficient for binding. A mutant SH3 domain (P434L; SH3*) did not bind. White lines indicate lanes omitted from blots (B and F). (C) Syndapin I SH3 precipitates GFP-ProSAP1 and GFP-ProSAP2 but not GFP-Shank1. (D) Alignment of +++APPPP motifs in ProSAP1 (NCBI Protein database accession no. NP_001004133 ), ProSAP2 (accession no. NP_067708 ), and Cobl (accession no. NP_766084 ; conserved amino acids are highlighted) and of corresponding residues in Shank1 (accession no. Q9WV48 ). (E) Scheme of rat ProSAP1b and deletion mutants used. Indicated are the N-terminal PDZ domain (medium grey), several proline-rich motifs (dark grey lines), and the C-terminal SAM (sterile alpha motif) domain (light grey). (F) GST–syndapin I precipitated GFP-ProSAP1 1–235 but none of the other ProSAP1 deletion mutants. (G) GFP fusion peptides encompassing the +++APPPP motifs of ProSAP1, ProSAP2, and Cobl associated with syndapin I SH3. (H and I) RKKAPPPPKR to GAGAAAAAAG mutation (amino acids 141–150 in ProSAP1; ProSAP1 1–235*) disrupted direct binding of ProSAP1 to syndapin I in both in vitro reconstitutions with purified proteins (H) and in coprecipitation analyses (I).
    Overexpression Vector Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare gst fusion vector pgex 2t
    Identification of ProSAP1/Shank2 and ProSAP2/Shank3 as postsynaptically enriched Syndapin I interaction partners. (A) <t>GST–syndapin</t> I, II, and III specifically precipitate <t>GFP-ProSAP1</t> expressed in HEK293 cells. (B) Coprecipitation analysis with GST–syndapin I and deletion mutants thereof. The SH3 domain is critical and sufficient for binding. A mutant SH3 domain (P434L; SH3*) did not bind. White lines indicate lanes omitted from blots (B and F). (C) Syndapin I SH3 precipitates GFP-ProSAP1 and GFP-ProSAP2 but not GFP-Shank1. (D) Alignment of +++APPPP motifs in ProSAP1 (NCBI Protein database accession no. NP_001004133 ), ProSAP2 (accession no. NP_067708 ), and Cobl (accession no. NP_766084 ; conserved amino acids are highlighted) and of corresponding residues in Shank1 (accession no. Q9WV48 ). (E) Scheme of rat ProSAP1b and deletion mutants used. Indicated are the N-terminal PDZ domain (medium grey), several proline-rich motifs (dark grey lines), and the C-terminal SAM (sterile alpha motif) domain (light grey). (F) GST–syndapin I precipitated GFP-ProSAP1 1–235 but none of the other ProSAP1 deletion mutants. (G) GFP fusion peptides encompassing the +++APPPP motifs of ProSAP1, ProSAP2, and Cobl associated with syndapin I SH3. (H and I) RKKAPPPPKR to GAGAAAAAAG mutation (amino acids 141–150 in ProSAP1; ProSAP1 1–235*) disrupted direct binding of ProSAP1 to syndapin I in both in vitro reconstitutions with purified proteins (H) and in coprecipitation analyses (I).
    Gst Fusion Vector Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare bamhi hindiii digested pgex 2t
    Identification of ProSAP1/Shank2 and ProSAP2/Shank3 as postsynaptically enriched Syndapin I interaction partners. (A) <t>GST–syndapin</t> I, II, and III specifically precipitate <t>GFP-ProSAP1</t> expressed in HEK293 cells. (B) Coprecipitation analysis with GST–syndapin I and deletion mutants thereof. The SH3 domain is critical and sufficient for binding. A mutant SH3 domain (P434L; SH3*) did not bind. White lines indicate lanes omitted from blots (B and F). (C) Syndapin I SH3 precipitates GFP-ProSAP1 and GFP-ProSAP2 but not GFP-Shank1. (D) Alignment of +++APPPP motifs in ProSAP1 (NCBI Protein database accession no. NP_001004133 ), ProSAP2 (accession no. NP_067708 ), and Cobl (accession no. NP_766084 ; conserved amino acids are highlighted) and of corresponding residues in Shank1 (accession no. Q9WV48 ). (E) Scheme of rat ProSAP1b and deletion mutants used. Indicated are the N-terminal PDZ domain (medium grey), several proline-rich motifs (dark grey lines), and the C-terminal SAM (sterile alpha motif) domain (light grey). (F) GST–syndapin I precipitated GFP-ProSAP1 1–235 but none of the other ProSAP1 deletion mutants. (G) GFP fusion peptides encompassing the +++APPPP motifs of ProSAP1, ProSAP2, and Cobl associated with syndapin I SH3. (H and I) RKKAPPPPKR to GAGAAAAAAG mutation (amino acids 141–150 in ProSAP1; ProSAP1 1–235*) disrupted direct binding of ProSAP1 to syndapin I in both in vitro reconstitutions with purified proteins (H) and in coprecipitation analyses (I).
    Bamhi Hindiii Digested Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare pgex 2t bacterial expression vector
    Identification of ProSAP1/Shank2 and ProSAP2/Shank3 as postsynaptically enriched Syndapin I interaction partners. (A) <t>GST–syndapin</t> I, II, and III specifically precipitate <t>GFP-ProSAP1</t> expressed in HEK293 cells. (B) Coprecipitation analysis with GST–syndapin I and deletion mutants thereof. The SH3 domain is critical and sufficient for binding. A mutant SH3 domain (P434L; SH3*) did not bind. White lines indicate lanes omitted from blots (B and F). (C) Syndapin I SH3 precipitates GFP-ProSAP1 and GFP-ProSAP2 but not GFP-Shank1. (D) Alignment of +++APPPP motifs in ProSAP1 (NCBI Protein database accession no. NP_001004133 ), ProSAP2 (accession no. NP_067708 ), and Cobl (accession no. NP_766084 ; conserved amino acids are highlighted) and of corresponding residues in Shank1 (accession no. Q9WV48 ). (E) Scheme of rat ProSAP1b and deletion mutants used. Indicated are the N-terminal PDZ domain (medium grey), several proline-rich motifs (dark grey lines), and the C-terminal SAM (sterile alpha motif) domain (light grey). (F) GST–syndapin I precipitated GFP-ProSAP1 1–235 but none of the other ProSAP1 deletion mutants. (G) GFP fusion peptides encompassing the +++APPPP motifs of ProSAP1, ProSAP2, and Cobl associated with syndapin I SH3. (H and I) RKKAPPPPKR to GAGAAAAAAG mutation (amino acids 141–150 in ProSAP1; ProSAP1 1–235*) disrupted direct binding of ProSAP1 to syndapin I in both in vitro reconstitutions with purified proteins (H) and in coprecipitation analyses (I).
    Pgex 2t Bacterial Expression Vector, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 90/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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

    Identification of ProSAP1/Shank2 and ProSAP2/Shank3 as postsynaptically enriched Syndapin I interaction partners. (A) GST–syndapin I, II, and III specifically precipitate GFP-ProSAP1 expressed in HEK293 cells. (B) Coprecipitation analysis with GST–syndapin I and deletion mutants thereof. The SH3 domain is critical and sufficient for binding. A mutant SH3 domain (P434L; SH3*) did not bind. White lines indicate lanes omitted from blots (B and F). (C) Syndapin I SH3 precipitates GFP-ProSAP1 and GFP-ProSAP2 but not GFP-Shank1. (D) Alignment of +++APPPP motifs in ProSAP1 (NCBI Protein database accession no. NP_001004133 ), ProSAP2 (accession no. NP_067708 ), and Cobl (accession no. NP_766084 ; conserved amino acids are highlighted) and of corresponding residues in Shank1 (accession no. Q9WV48 ). (E) Scheme of rat ProSAP1b and deletion mutants used. Indicated are the N-terminal PDZ domain (medium grey), several proline-rich motifs (dark grey lines), and the C-terminal SAM (sterile alpha motif) domain (light grey). (F) GST–syndapin I precipitated GFP-ProSAP1 1–235 but none of the other ProSAP1 deletion mutants. (G) GFP fusion peptides encompassing the +++APPPP motifs of ProSAP1, ProSAP2, and Cobl associated with syndapin I SH3. (H and I) RKKAPPPPKR to GAGAAAAAAG mutation (amino acids 141–150 in ProSAP1; ProSAP1 1–235*) disrupted direct binding of ProSAP1 to syndapin I in both in vitro reconstitutions with purified proteins (H) and in coprecipitation analyses (I).

    Journal: The Journal of Cell Biology

    Article Title: ProSAP1 and membrane nanodomain-associated syndapin I promote postsynapse formation and function

    doi: 10.1083/jcb.201307088

    Figure Lengend Snippet: Identification of ProSAP1/Shank2 and ProSAP2/Shank3 as postsynaptically enriched Syndapin I interaction partners. (A) GST–syndapin I, II, and III specifically precipitate GFP-ProSAP1 expressed in HEK293 cells. (B) Coprecipitation analysis with GST–syndapin I and deletion mutants thereof. The SH3 domain is critical and sufficient for binding. A mutant SH3 domain (P434L; SH3*) did not bind. White lines indicate lanes omitted from blots (B and F). (C) Syndapin I SH3 precipitates GFP-ProSAP1 and GFP-ProSAP2 but not GFP-Shank1. (D) Alignment of +++APPPP motifs in ProSAP1 (NCBI Protein database accession no. NP_001004133 ), ProSAP2 (accession no. NP_067708 ), and Cobl (accession no. NP_766084 ; conserved amino acids are highlighted) and of corresponding residues in Shank1 (accession no. Q9WV48 ). (E) Scheme of rat ProSAP1b and deletion mutants used. Indicated are the N-terminal PDZ domain (medium grey), several proline-rich motifs (dark grey lines), and the C-terminal SAM (sterile alpha motif) domain (light grey). (F) GST–syndapin I precipitated GFP-ProSAP1 1–235 but none of the other ProSAP1 deletion mutants. (G) GFP fusion peptides encompassing the +++APPPP motifs of ProSAP1, ProSAP2, and Cobl associated with syndapin I SH3. (H and I) RKKAPPPPKR to GAGAAAAAAG mutation (amino acids 141–150 in ProSAP1; ProSAP1 1–235*) disrupted direct binding of ProSAP1 to syndapin I in both in vitro reconstitutions with purified proteins (H) and in coprecipitation analyses (I).

    Article Snippet: DNA constructs Plasmids encoding for GFP (pEGFP-C1; Takara Bio Inc.)-, GST (pGEX-2T; GE Healthcare)-, Xpress (pcDNA 3.1/HisC; Invitrogen)-, and FLAG-tagged (pCMV-Tag2b; Agilent Technologies) full-length syndapin I as well as for GST–syndapin I SH3 domain (aa 376–441, pGEX-2T; aa 378–441, pGEX-5X-1; GE Healthcare), GST–syndapin I SH3P434L (GST-Sdp I SH3*; aa 376–441, pGEX-2T), and GST–syndapin IΔSH3 (aa 1–382, pGEX-2T) were described in , , and , respectively.

    Techniques: Binding Assay, Mutagenesis, In Vitro, Purification

    Syndapin I interacts with ProSAP1 in vivo. (A) Specific coimmunoprecipitation of GFP-ProSAP1 with anti-FLAG antibodies immunoprecipitating FLAG–syndapin I. (B) Consistently, FLAG–syndapin I (arrowhead) was specifically coimmunoprecipitated with GFP-ProSAP1. (C) Immobilized GST–syndapin I SH3 specifically precipitated endogenous ProSAP1 from mouse brain cytosol (MBC). (D) Endogenous syndapin I was precipitated from rat brain preparations (RBC) with immobilized GST-ProSAP1 139–153 comprising the RKKAPPPP motif. (E–H) Syndapin I constitutively targeted to outer mitochondrial membranes recruited GFP-ProSAP1 (E) and GFP-ProSAP1 1–235 (F) in intact COS-7 cells, whereas Sdp I ΔSH3 did not (G and H). Bars, 10 µm. (I) Syndapin I and ProSAP1 immunolabeling of brain sections from adult mice. Colocalization in synapses of mossy fibers with dendrites of pyramidal cells in the stratum lucidum in the hippocampus CA3 is shown. Blue signal in merge, DAPI. Insets, 2.5-fold enlargements of the boxed areas. Bars, 25 µm. (J) Immunolabeling of neurons transfected with Xpress–syndapin I at DIV 12 and stained for syndapin I, ProSAP1, and the dendritic marker MAP2 at DIV 14. Insets, 1.5-fold enlargements of boxed areas. Bar, 10 µm. (K) Endogenous syndapin I colocalized with ProSAP1 and synapsin 1 (DIV 21). Insets, twofold enlargements of boxed areas. Bars: (main panels) 5 µm; (insets) 2 µm.

    Journal: The Journal of Cell Biology

    Article Title: ProSAP1 and membrane nanodomain-associated syndapin I promote postsynapse formation and function

    doi: 10.1083/jcb.201307088

    Figure Lengend Snippet: Syndapin I interacts with ProSAP1 in vivo. (A) Specific coimmunoprecipitation of GFP-ProSAP1 with anti-FLAG antibodies immunoprecipitating FLAG–syndapin I. (B) Consistently, FLAG–syndapin I (arrowhead) was specifically coimmunoprecipitated with GFP-ProSAP1. (C) Immobilized GST–syndapin I SH3 specifically precipitated endogenous ProSAP1 from mouse brain cytosol (MBC). (D) Endogenous syndapin I was precipitated from rat brain preparations (RBC) with immobilized GST-ProSAP1 139–153 comprising the RKKAPPPP motif. (E–H) Syndapin I constitutively targeted to outer mitochondrial membranes recruited GFP-ProSAP1 (E) and GFP-ProSAP1 1–235 (F) in intact COS-7 cells, whereas Sdp I ΔSH3 did not (G and H). Bars, 10 µm. (I) Syndapin I and ProSAP1 immunolabeling of brain sections from adult mice. Colocalization in synapses of mossy fibers with dendrites of pyramidal cells in the stratum lucidum in the hippocampus CA3 is shown. Blue signal in merge, DAPI. Insets, 2.5-fold enlargements of the boxed areas. Bars, 25 µm. (J) Immunolabeling of neurons transfected with Xpress–syndapin I at DIV 12 and stained for syndapin I, ProSAP1, and the dendritic marker MAP2 at DIV 14. Insets, 1.5-fold enlargements of boxed areas. Bar, 10 µm. (K) Endogenous syndapin I colocalized with ProSAP1 and synapsin 1 (DIV 21). Insets, twofold enlargements of boxed areas. Bars: (main panels) 5 µm; (insets) 2 µm.

    Article Snippet: DNA constructs Plasmids encoding for GFP (pEGFP-C1; Takara Bio Inc.)-, GST (pGEX-2T; GE Healthcare)-, Xpress (pcDNA 3.1/HisC; Invitrogen)-, and FLAG-tagged (pCMV-Tag2b; Agilent Technologies) full-length syndapin I as well as for GST–syndapin I SH3 domain (aa 376–441, pGEX-2T; aa 378–441, pGEX-5X-1; GE Healthcare), GST–syndapin I SH3P434L (GST-Sdp I SH3*; aa 376–441, pGEX-2T), and GST–syndapin IΔSH3 (aa 1–382, pGEX-2T) were described in , , and , respectively.

    Techniques: In Vivo, Immunolabeling, Mouse Assay, Transfection, Staining, Marker