high copy number yeast genomic dna library Search Results


listeria monocytogenes atcc  (ATCC)
99
ATCC listeria monocytogenes atcc
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ycabfb plasmid a s cerevisiae dna fragment  (Thermo Fisher)
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Thermo Fisher ycabfb plasmid a s cerevisiae dna fragment
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yeast genomic dna  (Promega)
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Promega yeast genomic dna
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gal4 dna binding domain fusion vector pas2 1  (TaKaRa)
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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).
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customized reagents designed for gibson assembly® cloning  (SGI-DNA inc)
90
SGI-DNA inc customized reagents designed for gibson assembly® cloning
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).
Customized Reagents Designed For Gibson Assembly® Cloning, supplied by SGI-DNA inc, 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 dna atcc atcc 201388 oligonucleotides  (ATCC)
95
ATCC yeast dna atcc atcc 201388 oligonucleotides
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).
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zymoprep 96 yeast plasmid miniprep kits  (Zymo Research)
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Zymo Research zymoprep 96 yeast plasmid miniprep kits
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).
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ladders  (Bio-Rad)
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Bio-Rad ladders
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).
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masterpure yeast dna purification kit  (Lucigen Corp)
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Lucigen Corp masterpure yeast dna purification kit
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).
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yeast genomic dna extraction kit dp307  (tiangen biotech co)
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tiangen biotech co yeast genomic dna extraction kit dp307
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).
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yeast gene specific primers  (Danaher Inc)
86
Danaher Inc yeast gene specific primers
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).
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m0491s hi t4 dna ligase new england biolabs cat  (New England Biolabs)
98
New England Biolabs m0491s hi t4 dna ligase new england biolabs cat
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).
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Image Search Results


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