expression vector pas2 1 Search Results


gal4 dna binding domain fusion vector pas2 1  (TaKaRa)
92
TaKaRa gal4 dna binding domain fusion vector pas2 1
FIG. 1. Primary structures of DBX, PL10, and Ded1 and their interac- tions with HCV core protein in the yeast two-hybrid assay. A, alignment of deduced amino acid sequences of DBX (Gen- Banky accession number AF000982), PL10 (GenBanky accession number J04847), and Ded1p (GenBanky accession number X57278) is shown. Identical amino acids are shown as white on cyan. Conserved substi- tutions are shown as black on magenta. Dots represent gaps to optimize alignments, which were obtained using the Pileup pro- gram. B, two-hybrid assays showing interac- tion of HCV core protein with DBX and PL10 but not with Ded1p. Yeast strain Y190 was co-transformed with a plasmid express- ing the cytoplasmic domain of HCV fused to the <t>GAL4</t> DNA binding domain and plas- mids expressing either a portion of DBX or the corresponding portions of PL10 or Ded1p fused to the GAL4 transcriptional activation domain. Transformants giving b-galactosid- ase activity (positive interactions) are blue. Control reactions of DBX, PL10, and Dep1p GAL 4 activation domain fusion proteins with GAL4 DNA binding domain alone were negative (data not shown).
Gal4 Dna Binding Domain Fusion Vector Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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expression vector pas2 1  (TaKaRa)
96
TaKaRa expression vector pas2 1
FIG. 1. Primary structures of DBX, PL10, and Ded1 and their interac- tions with HCV core protein in the yeast two-hybrid assay. A, alignment of deduced amino acid sequences of DBX (Gen- Banky accession number AF000982), PL10 (GenBanky accession number J04847), and Ded1p (GenBanky accession number X57278) is shown. Identical amino acids are shown as white on cyan. Conserved substi- tutions are shown as black on magenta. Dots represent gaps to optimize alignments, which were obtained using the Pileup pro- gram. B, two-hybrid assays showing interac- tion of HCV core protein with DBX and PL10 but not with Ded1p. Yeast strain Y190 was co-transformed with a plasmid express- ing the cytoplasmic domain of HCV fused to the <t>GAL4</t> DNA binding domain and plas- mids expressing either a portion of DBX or the corresponding portions of PL10 or Ded1p fused to the GAL4 transcriptional activation domain. Transformants giving b-galactosid- ase activity (positive interactions) are blue. Control reactions of DBX, PL10, and Dep1p GAL 4 activation domain fusion proteins with GAL4 DNA binding domain alone were negative (data not shown).
Expression Vector Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pas2 1 vector  (TaKaRa)
96
TaKaRa pas2 1 vector
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Pas2 1 Vector, supplied by TaKaRa, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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yeast expression vector pas2 1  (TaKaRa)
86
TaKaRa yeast expression vector pas2 1
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Yeast Expression Vector Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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expression vectors pas2 1  (TaKaRa)
86
TaKaRa expression vectors pas2 1
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Expression Vectors Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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expression vectors pas2 1 - by Bioz Stars, 2026-03
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pas2 1  (TaKaRa)
86
TaKaRa pas2 1
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pas2 1 - by Bioz Stars, 2026-03
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pas2-1 yeast expression plasmid  (Becton Dickinson)
90
Becton Dickinson pas2-1 yeast expression plasmid
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Pas2 1 Yeast Expression Plasmid, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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yeast shuttle vectors pas2 1  (TaKaRa)
86
TaKaRa yeast shuttle vectors pas2 1
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Yeast Shuttle Vectors Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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yeast pas2 1  (TaKaRa)
97
TaKaRa yeast pas2 1
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Yeast Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pas2 1 tctex1d4  (TaKaRa)
86
TaKaRa pas2 1 tctex1d4
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Pas2 1 Tctex1d4, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vector pas2 1  (TaKaRa)
99
TaKaRa vector pas2 1
Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid <t>(pAS2-Z1-Z2-is1),</t> and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .
Vector Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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FIG. 1. Primary structures of DBX, PL10, and Ded1 and their interac- tions with HCV core protein in the yeast two-hybrid assay. A, alignment of deduced amino acid sequences of DBX (Gen- Banky accession number AF000982), PL10 (GenBanky accession number J04847), and Ded1p (GenBanky accession number X57278) is shown. Identical amino acids are shown as white on cyan. Conserved substi- tutions are shown as black on magenta. Dots represent gaps to optimize alignments, which were obtained using the Pileup pro- gram. B, two-hybrid assays showing interac- tion of HCV core protein with DBX and PL10 but not with Ded1p. Yeast strain Y190 was co-transformed with a plasmid express- ing the cytoplasmic domain of HCV fused to the GAL4 DNA binding domain and plas- mids expressing either a portion of DBX or the corresponding portions of PL10 or Ded1p fused to the GAL4 transcriptional activation domain. Transformants giving b-galactosid- ase activity (positive interactions) are blue. Control reactions of DBX, PL10, and Dep1p GAL 4 activation domain fusion proteins with GAL4 DNA binding domain alone were negative (data not shown).

Journal: The Journal of biological chemistry

Article Title: Hepatitis C virus core protein binds to a DEAD box RNA helicase.

doi: 10.1074/jbc.274.22.15751

Figure Lengend Snippet: FIG. 1. Primary structures of DBX, PL10, and Ded1 and their interac- tions with HCV core protein in the yeast two-hybrid assay. A, alignment of deduced amino acid sequences of DBX (Gen- Banky accession number AF000982), PL10 (GenBanky accession number J04847), and Ded1p (GenBanky accession number X57278) is shown. Identical amino acids are shown as white on cyan. Conserved substi- tutions are shown as black on magenta. Dots represent gaps to optimize alignments, which were obtained using the Pileup pro- gram. B, two-hybrid assays showing interac- tion of HCV core protein with DBX and PL10 but not with Ded1p. Yeast strain Y190 was co-transformed with a plasmid express- ing the cytoplasmic domain of HCV fused to the GAL4 DNA binding domain and plas- mids expressing either a portion of DBX or the corresponding portions of PL10 or Ded1p fused to the GAL4 transcriptional activation domain. Transformants giving b-galactosid- ase activity (positive interactions) are blue. Control reactions of DBX, PL10, and Dep1p GAL 4 activation domain fusion proteins with GAL4 DNA binding domain alone were negative (data not shown).

Article Snippet: The amplified DNA was cloned into the GAL4 DNA binding domain fusion vector pAS2–1 (CLONTECH) to yield pAS2–1-HCV-core1–123.

Techniques: Y2H Assay, Transformation Assay, Plasmid Preparation, Binding Assay, Expressing, Activation Assay, Activity Assay, Control

Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid (pAS2-Z1-Z2-is1), and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .

Journal: The Journal of Cell Biology

Article Title: The NH 2 Terminus of Titin Spans the Z-Disc: Its Interaction with a Novel 19-kD Ligand (T-cap) Is Required for Sarcomeric Integrity

doi:

Figure Lengend Snippet: Interaction of T-cap and the titin Z1-Z2 domains. ( a ) Titin repeats Z1 and Z2 specifically interact with the 19-kD titin-cap protein by yeast two-hybrid analysis. Numbers above the schematic layout of the NH -terminal titin region indicate the nucleotide residue numbers corresponding to the human entry (EMBL data library X90568 ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). Two immunoglobulin domains at the NH terminus of titin are indicated as Z1 and Z2, respectively. Bars indicate positions of the cDNAs used for the bait plasmid (pAS2-Z1-Z2-is1), and the truncation constructs, pAS2-Z1-Z2 (containing the Z1 and Z2 domains), pAS2-Z1 (containing Z1 domain only), and pAS2Z2-is1 (containing the Z2 domain fused to residues 200– 257), used for the binding assay to T-cap. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( b ) Interaction of the NH -terminal 16 kD of T-cap with the titin Z1-Z2 Ig domains in the yeast two-hybrid system. Schematic of T-cap cDNA clone. Numbers above the titin-cap cDNA indicate the nucleotide residues of the human full-length cDNA sequence (sequence data available from EMBL under accession number AJ000491 ; from ) ( top ) and residue numbers of the deduced amino acid sequence ( bottom ). AA...A , a poly(A + ) tail at the 3′ terminus of the corresponding cDNA clone. Bars indicate positions of cDNA inserts derived from the two-hybrid screening using pAS2-Z1-Z2-is1 (see a ) as bait (T-cap-1, -3, -5, -6, and -7), and the truncation constructs of T-cap (T-cap-Δ1 and -Δ2) described in Materials and Methods. +/− signs refer to growth on minus (Leu, Trp, and His) plates supplemented with 3-AT, and numbers in parentheses refer to β-galactosidase activities (arbitrary units). ( c ) Interaction of expressed T-cap and titin Z1-Z2 peptides. A Coomassie blue– stained 18% Laemmli SDS gel of a whole-cell lysate of BL21 cells expressing tagless titin Z1-Z2 (lane C ). These cells were mixed with a His 6 -tagged 16-kD fragment of T-cap and lysed. Lysates were passed over Ni-NTA agarose columns. Interaction of a stable complex of titin Z1-Z2 and T-cap is indicated by retaining also the nontagged titin Z1-Z2 on the column ( arrow marks Z1-Z2 and T-cap in third lane ). Lane M , molecular mass markers as in legend for Fig. .

Article Snippet: The fragment was inserted into the pAS2-1 vector ( CLONTECH Labs, Palo Alto, CA) to obtain a GAL4 reporter fusion protein for the detection of protein–protein interactions.

Techniques: Sequencing, Plasmid Preparation, Construct, Binding Assay, Derivative Assay, Two Hybrid Screening, Staining, SDS-Gel, Expressing