matchmaker system 3 dna binding domain Takara Search Results


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  • 99
    TaKaRa dna binding domain
    Dna Binding Domain, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 428 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    TaKaRa pgbkt7 dna bd
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Pgbkt7 Dna Bd, supplied by TaKaRa, used in various techniques. Bioz Stars score: 90/100, based on 658 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    TaKaRa gal4 dna bd antibody
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Gal4 Dna Bd Antibody, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa gal4 dna bd
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Gal4 Dna Bd, supplied by TaKaRa, used in various techniques. Bioz Stars score: 88/100, based on 90 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    TaKaRa gal4 dna binding domain
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Gal4 Dna Binding Domain, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1743 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa gal4 dna binding domain fusion vector pgbt9
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Gal4 Dna Binding Domain Fusion Vector Pgbt9, supplied by TaKaRa, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa gal4 dna binding domain plasmid pgbt9
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Gal4 Dna Binding Domain Plasmid Pgbt9, supplied by TaKaRa, used in various techniques. Bioz Stars score: 79/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa gal4 dna binding domain vector pgbkt7
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Gal4 Dna Binding Domain Vector Pgbkt7, supplied by TaKaRa, used in various techniques. Bioz Stars score: 92/100, based on 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa gal4 dna binding domain vector pas2 1
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Gal4 Dna Binding Domain Vector Pas2 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 83/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa matchmaker gal4 two hybrid system 3
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Matchmaker Gal4 Two Hybrid System 3, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1153 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa matchmaker gal4 two hybrid system 3 protocol
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Matchmaker Gal4 Two Hybrid System 3 Protocol, supplied by TaKaRa, used in various techniques. Bioz Stars score: 80/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa matchmaker system 3
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Matchmaker System 3, supplied by TaKaRa, used in various techniques. Bioz Stars score: 80/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa matchmaker gal4 two hybrid system 3 libraries user manual
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Matchmaker Gal4 Two Hybrid System 3 Libraries User Manual, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa matchmaker gal4 two hybrid system 3 kit
    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, <t>pGBKT7</t> with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.
    Matchmaker Gal4 Two Hybrid System 3 Kit, supplied by TaKaRa, used in various techniques. Bioz Stars score: 96/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa yeast two hybrid matchmaker gal4 two hybrid system 3
    Expression of <t>Ngb-Gal4</t> BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.
    Yeast Two Hybrid Matchmaker Gal4 Two Hybrid System 3, supplied by TaKaRa, used in various techniques. Bioz Stars score: 89/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa yeast matchmaker two hybrid system 3
    Expression of <t>Ngb-Gal4</t> BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.
    Yeast Matchmaker Two Hybrid System 3, supplied by TaKaRa, used in various techniques. Bioz Stars score: 90/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa gal4 based clontech matchmaker 3 system
    Expression of <t>Ngb-Gal4</t> BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.
    Gal4 Based Clontech Matchmaker 3 System, supplied by TaKaRa, used in various techniques. Bioz Stars score: 79/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa matchmaker system 3 yeast expression vectors
    Expression of <t>Ngb-Gal4</t> BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.
    Matchmaker System 3 Yeast Expression Vectors, supplied by TaKaRa, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa ah109 yeast strains
    Expression of <t>Ngb-Gal4</t> BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.
    Ah109 Yeast Strains, supplied by TaKaRa, used in various techniques. Bioz Stars score: 80/100, based on 88 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa plasmids pgadt7
    Expression of <t>Ngb-Gal4</t> BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.
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    TaKaRa nde i
    The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with <t>Nde</t> I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.
    Nde I, supplied by TaKaRa, used in various techniques. Bioz Stars score: 90/100, based on 914 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa matchmaker human skeletal muscle library
    The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with <t>Nde</t> I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.
    Matchmaker Human Skeletal Muscle Library, supplied by TaKaRa, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa gal4p
    The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with <t>Nde</t> I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.
    Gal4p, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    TaKaRa libraries user manual pt3247 1
    The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with <t>Nde</t> I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.
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    97
    TaKaRa pgad10 vector
    The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with <t>Nde</t> I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.
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    90
    TaKaRa human brain matchmaker cdna library
    The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with <t>Nde</t> I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.
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    TaKaRa y2h gold strain
    Mutant Vps33b retains binding to Syntaxin7 SNARE domain. <t>Y2H</t> assays were performed to investigate the interaction of either Vps33b or Vps33b containing ARC mutations with SNARE proteins. Interaction between Vps33b and VIPAS39/SPE-39 was used as a positive
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    79
    TaKaRa libraries user manual pt3247 1 pr94575 protocol
    Mutant Vps33b retains binding to Syntaxin7 SNARE domain. <t>Y2H</t> assays were performed to investigate the interaction of either Vps33b or Vps33b containing ARC mutations with SNARE proteins. Interaction between Vps33b and VIPAS39/SPE-39 was used as a positive
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    99
    TaKaRa transformants
    Identification of hDUS2 as PKR and PACT interacting protein. ( A ) Yeast two-hybrid interaction assay. The indicated plasmids were transformed into yeast strain Hf7C and the <t>transformants</t> were streaked on triple dropout medium lacking leucine, tryptophan and histidine. A: hDUS2/pGBKT7 and empty vector pGADT7, B: hDUS2/pGBKT7 and PKR/pGADT7, C: hDUS2/pGBKT7 and PACT/pGADT7, D: empty vector pGBKT7 and hDUS2/pGADT7, E: PKR/pGBKT7 and hDUS2/pGADT7, F: PACT/pGBKT7 and hDUS2/pGADT7. ( B ) β-Galactosidase assay for the interactions in yeast. The indicated plasmids were transformed into yeast strain Hf7C and the transformants were streaked on double dropout medium lacking leucine, and tryptophan. After 4 days the growth was lifted on nitrocellulose membrane and β-galactosidase activity assay was performed after lysis of yeast cells on the membrane. Blue color indicates a positive interaction and white color indicates no interaction. ( C ) Biochemical interaction assay. In vitro -translated hDUS2 protein was allowed to interact with hexahistidine-tagged pure recombinant PKR or PACT proteins that were bound to Ni-agarose affinity beads. The bound proteins remaining on the beads were analyzed by SDS–PAGE followed by phosphorimager analysis. Lane 1: total protein from the translation mix (20% of input in lanes 2–4), lanes 2–4: hDUS2 protein bound to beads. Lane 2: protein bound to his-DRIL1 beads: negative control, lane 3: protein bound to his-PKR beads, lane 4: protein bound to his-PACT beads. ( D ) Domain structure of hDUS2. A schematic representation of the DUS and dsRBM domains in hDUS2 protein. The DUS domain is shown as a hatched box and the dsRBM is shown as a gray box. The amino acid numbers are indicated on the top and bottom of the boxes. ( E ) Alignment of hDUS2 dsRBM with dsRBMs from three other human dsRNA-binding proteins PKR, PACT and TRBP. ClustalW alignment of the dsRBMs present in PKR, PACT and TRBP is shown. The conserved residues are shown in dark gray and similarities are shown in light gray. The consensus is shown at the bottom.
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    90
    TaKaRa bgl ii pst
    Identification of hDUS2 as PKR and PACT interacting protein. ( A ) Yeast two-hybrid interaction assay. The indicated plasmids were transformed into yeast strain Hf7C and the <t>transformants</t> were streaked on triple dropout medium lacking leucine, tryptophan and histidine. A: hDUS2/pGBKT7 and empty vector pGADT7, B: hDUS2/pGBKT7 and PKR/pGADT7, C: hDUS2/pGBKT7 and PACT/pGADT7, D: empty vector pGBKT7 and hDUS2/pGADT7, E: PKR/pGBKT7 and hDUS2/pGADT7, F: PACT/pGBKT7 and hDUS2/pGADT7. ( B ) β-Galactosidase assay for the interactions in yeast. The indicated plasmids were transformed into yeast strain Hf7C and the transformants were streaked on double dropout medium lacking leucine, and tryptophan. After 4 days the growth was lifted on nitrocellulose membrane and β-galactosidase activity assay was performed after lysis of yeast cells on the membrane. Blue color indicates a positive interaction and white color indicates no interaction. ( C ) Biochemical interaction assay. In vitro -translated hDUS2 protein was allowed to interact with hexahistidine-tagged pure recombinant PKR or PACT proteins that were bound to Ni-agarose affinity beads. The bound proteins remaining on the beads were analyzed by SDS–PAGE followed by phosphorimager analysis. Lane 1: total protein from the translation mix (20% of input in lanes 2–4), lanes 2–4: hDUS2 protein bound to beads. Lane 2: protein bound to his-DRIL1 beads: negative control, lane 3: protein bound to his-PKR beads, lane 4: protein bound to his-PACT beads. ( D ) Domain structure of hDUS2. A schematic representation of the DUS and dsRBM domains in hDUS2 protein. The DUS domain is shown as a hatched box and the dsRBM is shown as a gray box. The amino acid numbers are indicated on the top and bottom of the boxes. ( E ) Alignment of hDUS2 dsRBM with dsRBMs from three other human dsRNA-binding proteins PKR, PACT and TRBP. ClustalW alignment of the dsRBMs present in PKR, PACT and TRBP is shown. The conserved residues are shown in dark gray and similarities are shown in light gray. The consensus is shown at the bottom.
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    y2h  (TaKaRa)
    99
    TaKaRa y2h
    Conserved domains of PilQ. Panel A. Conserved domains of MxPilQ (901 residues) and TtPilQ (757 residues) [58] . The conserved feature are drawn to scale and areindicated by shaded letters below both protein. Each has the PilQ region at their C-terminus consisting of the highly conserved Secretin domain and the region immediately N-terminal of secretin (Secretin_N). Two AMIN domains [59] are found at the N-terminus of MxPilQ but not TtPilQ. The brackets and the labels above indicate the different <t>Y2H</t> constructs and/or subdomains in each protein. Panel B. Structural alignment of the N-termini of TtPilQ and the T2SS secretin GspD from Enterotoxigenic E. coli (ETEC) [50] , [55] . The boundaries between N0 and N1 as well as N1 and N2 subdomains in GspD are indicated by arrows (↑). The secondary structure of GspD from crystallography and that of TtPilQ predicted from modeling are indicated below and above the aligned sequences, respectively, with β strands represented by block arrows and α helices by cylinders.
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    77
    TaKaRa k562 cdna library
    Fli-1 overexpression in <t>K562</t> cells in the maintained presence of endogenous GATA-1. (A) Northern blot analysis of K562 cell lines stably transfected with control plasmid pIRES2-EGFP (lane 1) or Fli-1 expression plasmid pIRES2-Fli-1-EGFP (lane 2). Each lane contains 3 μg of poly(A + ) RNA. The membrane was hybridized with the indicated 32 P-labeled <t>cDNA</t> probes in the order shown. Membranes were stripped prior to each hybridization in the presence of boiling 0.1% SDS. (B) Flow cytometric analysis of K562-GFP and K562-Fli-1-GFP cell lines for the surface expression of markers associated with terminal differentiation of megakaryocytes. The indicated cell lines were incubated in the presence of anti-GPIX, anti-GPIbα, or anti-GPIIb primary antibodies prior to being labeled with phycoerythrin-conjugated secondary antibody, as shown.
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    Image Search Results


    Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, pGBKT7 with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.

    Journal: Autophagy

    Article Title: Pex3 and Atg37 compete to regulate the interaction between the pexophagy receptor, Atg30, and the Hrr25 kinase

    doi: 10.1080/15548627.2017.1413521

    Figure Lengend Snippet: Lack of methionine in the medium induces expression of HA-Atg30 or irrelevant protein (X) from the MET25 promoter, and lack of histidine in the medium, with or without 3-AT, was used to assess protein-protein interaction. Empty plasmids, pGBKT7 with Gal4 DNA-binding domain (BD) and pGAD-GH with Gal4-activation domain (AD), were used to monitor the levels of self-activation of each analyzed construct. 3-AT, 3-amino-1,2,4-triazole; ACBD, acyl-CoA-binding domain; TM, transmembrane domain. i. Schematic depicting competition between AD-Atg37(84-278) and HA-Atg30 for Pex3 in the Y2H assay; ii. schematic depicting interaction between BD-Pex3 and AD-Atg37(84-274) in the Y3H assay. Interaction between BD-Pex3 and HA-Atg30 affects reporter gene expression.

    Article Snippet: Full-length open reading frames or truncated forms were inserted in pGAD-GH (Clontech Laboratories, 638853), pGADT7-AD (Clontech Laboratories, 630442) or pDEST-GADT7 (Arabidopsis Biological Resource Center, CD3-763; Shaw Laboratory) (AD) and pGBT9 (Clontech Laboratories, K1605-A), pGBKT7 (Clontech Laboratories, 630443), pDEST-GBKT7 (Arabidopsis Biological Resource Center, CD3-764; Shaw Laboratory) (BD) plasmids.

    Techniques: Expressing, Binding Assay, Activation Assay, Construct, Y2H Assay

    DUSP5 interacts specifically and directly with the ERK1 and ERK2 MAP kinases. (A) Yeast two-hybrid assays. pGBKT7.DUSP5 was transformed into PJ69-4A and mated with PJ69-4α expressing the GAL4 activation domain (AD) fusions pGADT7.ERK1, pGADT7.ERK2,

    Journal:

    Article Title: Specific Inactivation and Nuclear Anchoring of Extracellular Signal-Regulated Kinase 2 by the Inducible Dual-Specificity Protein Phosphatase DUSP5

    doi: 10.1128/MCB.25.5.1830-1845.2005

    Figure Lengend Snippet: DUSP5 interacts specifically and directly with the ERK1 and ERK2 MAP kinases. (A) Yeast two-hybrid assays. pGBKT7.DUSP5 was transformed into PJ69-4A and mated with PJ69-4α expressing the GAL4 activation domain (AD) fusions pGADT7.ERK1, pGADT7.ERK2,

    Article Snippet: The PCR product was subcloned as an NdeI-XhoI fragment into bacterial expression vector pET15b (Novagen) and Matchmaker System 3 DNA binding domain and activation domain fusion vectors pGBKT7 and pGADT7 (Clontech).

    Techniques: Transformation Assay, Expressing, Activation Assay

    Selection of Ngb-interacting gene products in yeast two-hybrid screening. Mating reaction was set up between Y187 transformed with pGBKT7-Ngb vector and AH109 pretransformed with mouse cDNA library. Representative selected clones were shown. (A) Positive clones in both Drop Out medium and alpha-glactosidase activity test. (B) Clones positive in Drop Out medium selection but negative in alpha-glactosidase activity.

    Journal: Neuroscience

    Article Title: Identification of Neuroglobin-interacting Proteins Using Yeast Two-hybrid Screening

    doi: 10.1016/j.neuroscience.2011.10.046

    Figure Lengend Snippet: Selection of Ngb-interacting gene products in yeast two-hybrid screening. Mating reaction was set up between Y187 transformed with pGBKT7-Ngb vector and AH109 pretransformed with mouse cDNA library. Representative selected clones were shown. (A) Positive clones in both Drop Out medium and alpha-glactosidase activity test. (B) Clones positive in Drop Out medium selection but negative in alpha-glactosidase activity.

    Article Snippet: Mouse Ngb cDNA was amplified by PCR; the PCR fragment was then digested with Nde I and Bam HI, and inserted into the pGBKT7 vector (Clontech) to generate a construct of mouse Ngb cDNA fused in-frame to the GAL4 DNA-binding domain (BD) (amino acids [a.a.] 1–147 of GAL4) as the bait.

    Techniques: Selection, Two Hybrid Screening, Transformation Assay, Plasmid Preparation, cDNA Library Assay, Clone Assay, Activity Assay

    Expression of Ngb-Gal4 BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.

    Journal: Neuroscience

    Article Title: Identification of Neuroglobin-interacting Proteins Using Yeast Two-hybrid Screening

    doi: 10.1016/j.neuroscience.2011.10.046

    Figure Lengend Snippet: Expression of Ngb-Gal4 BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.

    Article Snippet: Mouse Ngb cDNA was amplified by PCR; the PCR fragment was then digested with Nde I and Bam HI, and inserted into the pGBKT7 vector (Clontech) to generate a construct of mouse Ngb cDNA fused in-frame to the GAL4 DNA-binding domain (BD) (amino acids [a.a.] 1–147 of GAL4) as the bait.

    Techniques: Expressing, Transformation Assay, SDS Page, Plasmid Preparation

    Yeast two-hybrid interaction between Hd16 and Ghd7. (a) Schematic diagrams of the Ghd7 fragments used in the yeast two-hybrid interaction assay. Numbers in parentheses indicate the number of amino acid residues (aa). (b) Results of the yeast two-hybrid interaction assay between Hd16 and Ghd7. Yeast strain AH109 was transformed with the indicated plasmid combinations of the bait and the prey, respectively. Values are means ± standard deviations of β-galactosidase activities from three individual colonies. pGBKT7, bait vector; pGADT7, prey vector; Hd16(Ni), Nipponbare Hd16 protein; Hd16(Ko), Koshihikari Hd16 protein.

    Journal: The Plant Journal

    Article Title: Hd16, a gene for casein kinase I, is involved in the control of rice flowering time by modulating the day-length response

    doi: 10.1111/tpj.12268

    Figure Lengend Snippet: Yeast two-hybrid interaction between Hd16 and Ghd7. (a) Schematic diagrams of the Ghd7 fragments used in the yeast two-hybrid interaction assay. Numbers in parentheses indicate the number of amino acid residues (aa). (b) Results of the yeast two-hybrid interaction assay between Hd16 and Ghd7. Yeast strain AH109 was transformed with the indicated plasmid combinations of the bait and the prey, respectively. Values are means ± standard deviations of β-galactosidase activities from three individual colonies. pGBKT7, bait vector; pGADT7, prey vector; Hd16(Ni), Nipponbare Hd16 protein; Hd16(Ko), Koshihikari Hd16 protein.

    Article Snippet: Amplified cDNA fragments were cloned into pGBKT7 DNA-BD and pGADT7 AD vectors from the Matchmaker Two-Hybrid System 3 (Clontech, http://www.clontech.com ).

    Techniques: Transformation Assay, Plasmid Preparation

    Expression of Ngb-Gal4 BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.

    Journal: Neuroscience

    Article Title: Identification of Neuroglobin-interacting Proteins Using Yeast Two-hybrid Screening

    doi: 10.1016/j.neuroscience.2011.10.046

    Figure Lengend Snippet: Expression of Ngb-Gal4 BD fusion protein in yeast. Yeast strain Y187 was transformed with pGBKT7-Ngb and transformants were selected on appropriate SD medium. Soluble protein extracts were prepared and protein samples were subjected to SDS-PAGE. Ngb expression was detected using anti-Ngb antibody. Lane 1: control Y187 transformed with pGBKT7 vector. Lane 2: Y187 transformed with pGBKT7-Ngb.

    Article Snippet: Yeast two-hybrid screening was carried out using a GAL4-based yeast two-hybrid system (MATCHMAKER Two-Hybrid System 3; Clontech, Palo Alto, CA); screening and assays were performed following the manufacturer’s instruction (Clontech).

    Techniques: Expressing, Transformation Assay, SDS Page, Plasmid Preparation

    The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with Nde I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.

    Journal: PLoS ONE

    Article Title: Identification and Characterization of MT-1X as a Novel FHL3-Binding Partner

    doi: 10.1371/journal.pone.0093723

    Figure Lengend Snippet: The interaction between full length MT-1X and FHL3 by yeast two hybrid assay. (A) Identification of recombinant plasmid pAS2-1/FHL3d4 by restriction analysis. M:DNA marker; Lane1: Digested pAS2-1/FHL3d4 plasmid with Nde I and Eco RI. (B) Identification of recombinant plasmid pACT2/MT-1X by restriction analysis. M:DNA marker; Lane1-4: Digested pACT2/MT-1X plasmid with Bam HI and Eco RI. (C) Detection of MT-1X auto-activation by yeast two hybrid analysis. Line1:1,2: positive control; Line1: 3,4: negative control; Line2:1-5:transform pACT2/MT-1X. (D) Coloration analysis to verify the interaction between full length MT-1X and FHL3. Line1:1,2:positive control; Line1: 3,4: negative control. Line2:1–7: Co-transform pAS2-1/FHL3d4 and pACT2/MT-1X.

    Article Snippet: The PCR product was digested with Nde I and Eco RI, and then inserted into the Nde I and Eco RI site of vector pAS2-1 of the yeast two-hybrid system (Matchmaker 2, Clontech), resulting in an in-frame fusion of human FHL3 mutants with sequential deletion of LIM4 cDNA downstream with GAL4 DNA-binding domain.

    Techniques: Y2H Assay, Recombinant, Plasmid Preparation, Marker, Activation Assay, Positive Control, Negative Control

    Mutant Vps33b retains binding to Syntaxin7 SNARE domain. Y2H assays were performed to investigate the interaction of either Vps33b or Vps33b containing ARC mutations with SNARE proteins. Interaction between Vps33b and VIPAS39/SPE-39 was used as a positive

    Journal: Human Molecular Genetics

    Article Title: Vps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive endosomes

    doi: 10.1093/hmg/ddt378

    Figure Lengend Snippet: Mutant Vps33b retains binding to Syntaxin7 SNARE domain. Y2H assays were performed to investigate the interaction of either Vps33b or Vps33b containing ARC mutations with SNARE proteins. Interaction between Vps33b and VIPAS39/SPE-39 was used as a positive

    Article Snippet: Y2H Gold strain, the DNA-binding domain and activation domain vectors, pGBKT7 and pGADT7, respectively, came from the Matchmaker Two-Hybrid System 3 (Clontech, Mountain View, CA, USA).

    Techniques: Mutagenesis, Binding Assay

    Direct interaction between VIPAS39/SPE-39 and Vps33b. ( A ) The yeast HOPS complex (left) and two possible models for how VIPAS39/SPE-39 interacts with other proteins in the metazoan HOPS complex. ( B and C ) Y2H assays testing possible interaction between

    Journal: Human Molecular Genetics

    Article Title: Vps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive endosomes

    doi: 10.1093/hmg/ddt378

    Figure Lengend Snippet: Direct interaction between VIPAS39/SPE-39 and Vps33b. ( A ) The yeast HOPS complex (left) and two possible models for how VIPAS39/SPE-39 interacts with other proteins in the metazoan HOPS complex. ( B and C ) Y2H assays testing possible interaction between

    Article Snippet: Y2H Gold strain, the DNA-binding domain and activation domain vectors, pGBKT7 and pGADT7, respectively, came from the Matchmaker Two-Hybrid System 3 (Clontech, Mountain View, CA, USA).

    Techniques:

    Identification of hDUS2 as PKR and PACT interacting protein. ( A ) Yeast two-hybrid interaction assay. The indicated plasmids were transformed into yeast strain Hf7C and the transformants were streaked on triple dropout medium lacking leucine, tryptophan and histidine. A: hDUS2/pGBKT7 and empty vector pGADT7, B: hDUS2/pGBKT7 and PKR/pGADT7, C: hDUS2/pGBKT7 and PACT/pGADT7, D: empty vector pGBKT7 and hDUS2/pGADT7, E: PKR/pGBKT7 and hDUS2/pGADT7, F: PACT/pGBKT7 and hDUS2/pGADT7. ( B ) β-Galactosidase assay for the interactions in yeast. The indicated plasmids were transformed into yeast strain Hf7C and the transformants were streaked on double dropout medium lacking leucine, and tryptophan. After 4 days the growth was lifted on nitrocellulose membrane and β-galactosidase activity assay was performed after lysis of yeast cells on the membrane. Blue color indicates a positive interaction and white color indicates no interaction. ( C ) Biochemical interaction assay. In vitro -translated hDUS2 protein was allowed to interact with hexahistidine-tagged pure recombinant PKR or PACT proteins that were bound to Ni-agarose affinity beads. The bound proteins remaining on the beads were analyzed by SDS–PAGE followed by phosphorimager analysis. Lane 1: total protein from the translation mix (20% of input in lanes 2–4), lanes 2–4: hDUS2 protein bound to beads. Lane 2: protein bound to his-DRIL1 beads: negative control, lane 3: protein bound to his-PKR beads, lane 4: protein bound to his-PACT beads. ( D ) Domain structure of hDUS2. A schematic representation of the DUS and dsRBM domains in hDUS2 protein. The DUS domain is shown as a hatched box and the dsRBM is shown as a gray box. The amino acid numbers are indicated on the top and bottom of the boxes. ( E ) Alignment of hDUS2 dsRBM with dsRBMs from three other human dsRNA-binding proteins PKR, PACT and TRBP. ClustalW alignment of the dsRBMs present in PKR, PACT and TRBP is shown. The conserved residues are shown in dark gray and similarities are shown in light gray. The consensus is shown at the bottom.

    Journal: Nucleic Acids Research

    Article Title: Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR

    doi: 10.1093/nar/gkm1129

    Figure Lengend Snippet: Identification of hDUS2 as PKR and PACT interacting protein. ( A ) Yeast two-hybrid interaction assay. The indicated plasmids were transformed into yeast strain Hf7C and the transformants were streaked on triple dropout medium lacking leucine, tryptophan and histidine. A: hDUS2/pGBKT7 and empty vector pGADT7, B: hDUS2/pGBKT7 and PKR/pGADT7, C: hDUS2/pGBKT7 and PACT/pGADT7, D: empty vector pGBKT7 and hDUS2/pGADT7, E: PKR/pGBKT7 and hDUS2/pGADT7, F: PACT/pGBKT7 and hDUS2/pGADT7. ( B ) β-Galactosidase assay for the interactions in yeast. The indicated plasmids were transformed into yeast strain Hf7C and the transformants were streaked on double dropout medium lacking leucine, and tryptophan. After 4 days the growth was lifted on nitrocellulose membrane and β-galactosidase activity assay was performed after lysis of yeast cells on the membrane. Blue color indicates a positive interaction and white color indicates no interaction. ( C ) Biochemical interaction assay. In vitro -translated hDUS2 protein was allowed to interact with hexahistidine-tagged pure recombinant PKR or PACT proteins that were bound to Ni-agarose affinity beads. The bound proteins remaining on the beads were analyzed by SDS–PAGE followed by phosphorimager analysis. Lane 1: total protein from the translation mix (20% of input in lanes 2–4), lanes 2–4: hDUS2 protein bound to beads. Lane 2: protein bound to his-DRIL1 beads: negative control, lane 3: protein bound to his-PKR beads, lane 4: protein bound to his-PACT beads. ( D ) Domain structure of hDUS2. A schematic representation of the DUS and dsRBM domains in hDUS2 protein. The DUS domain is shown as a hatched box and the dsRBM is shown as a gray box. The amino acid numbers are indicated on the top and bottom of the boxes. ( E ) Alignment of hDUS2 dsRBM with dsRBMs from three other human dsRNA-binding proteins PKR, PACT and TRBP. ClustalW alignment of the dsRBMs present in PKR, PACT and TRBP is shown. The conserved residues are shown in dark gray and similarities are shown in light gray. The consensus is shown at the bottom.

    Article Snippet: A total of 3 million transformants from a human placenta matchmaker library (Clontech) were screened in the yeast strain HF7c (Clontech) and 250 colonies were recovered on triple dropout medium lacking histidine, leucine and tryptophan, out of which 22 tested positive for β-galactosidase.

    Techniques: Transformation Assay, Plasmid Preparation, Activity Assay, Lysis, In Vitro, Recombinant, SDS Page, Negative Control, Binding Assay

    Conserved domains of PilQ. Panel A. Conserved domains of MxPilQ (901 residues) and TtPilQ (757 residues) [58] . The conserved feature are drawn to scale and areindicated by shaded letters below both protein. Each has the PilQ region at their C-terminus consisting of the highly conserved Secretin domain and the region immediately N-terminal of secretin (Secretin_N). Two AMIN domains [59] are found at the N-terminus of MxPilQ but not TtPilQ. The brackets and the labels above indicate the different Y2H constructs and/or subdomains in each protein. Panel B. Structural alignment of the N-termini of TtPilQ and the T2SS secretin GspD from Enterotoxigenic E. coli (ETEC) [50] , [55] . The boundaries between N0 and N1 as well as N1 and N2 subdomains in GspD are indicated by arrows (↑). The secondary structure of GspD from crystallography and that of TtPilQ predicted from modeling are indicated below and above the aligned sequences, respectively, with β strands represented by block arrows and α helices by cylinders.

    Journal: PLoS ONE

    Article Title: Type IV Pilus Proteins Form an Integrated Structure Extending from the Cytoplasm to the Outer Membrane

    doi: 10.1371/journal.pone.0070144

    Figure Lengend Snippet: Conserved domains of PilQ. Panel A. Conserved domains of MxPilQ (901 residues) and TtPilQ (757 residues) [58] . The conserved feature are drawn to scale and areindicated by shaded letters below both protein. Each has the PilQ region at their C-terminus consisting of the highly conserved Secretin domain and the region immediately N-terminal of secretin (Secretin_N). Two AMIN domains [59] are found at the N-terminus of MxPilQ but not TtPilQ. The brackets and the labels above indicate the different Y2H constructs and/or subdomains in each protein. Panel B. Structural alignment of the N-termini of TtPilQ and the T2SS secretin GspD from Enterotoxigenic E. coli (ETEC) [50] , [55] . The boundaries between N0 and N1 as well as N1 and N2 subdomains in GspD are indicated by arrows (↑). The secondary structure of GspD from crystallography and that of TtPilQ predicted from modeling are indicated below and above the aligned sequences, respectively, with β strands represented by block arrows and α helices by cylinders.

    Article Snippet: Plasmids for Y2H Experiments ( ) The MATCHMAKER System 3 from Clontech was used for the Y2H experiments in this study.

    Techniques: Construct, Blocking Assay

    Pairwise interactions among Pil proteins in Y2H system. Panels A and B . Interactions among M. xanthus Pil proteins. Panels C, D and E . Interactions among T. thermophilus Pil proteins. The first and second columns on the left of each panel indicate Pil proteins or fragments fused to GAD and GBD in Y2H plasmids by their last letter, respectively. V indicates an empty Y2H vector. N0, N1, N2 and their combinations are represented by their numerals only. Last row in each panel contained the positive control with T-antigen (T) and p53 (53). The left half of each panel shows growth on SD-His and the right on SD-Ade plates, respectively. The spots in each row in a panel were inoculated by serial dilutions of the same yeast cells with the indicated Y2H plasmids. See text and Materials and Methods for details.

    Journal: PLoS ONE

    Article Title: Type IV Pilus Proteins Form an Integrated Structure Extending from the Cytoplasm to the Outer Membrane

    doi: 10.1371/journal.pone.0070144

    Figure Lengend Snippet: Pairwise interactions among Pil proteins in Y2H system. Panels A and B . Interactions among M. xanthus Pil proteins. Panels C, D and E . Interactions among T. thermophilus Pil proteins. The first and second columns on the left of each panel indicate Pil proteins or fragments fused to GAD and GBD in Y2H plasmids by their last letter, respectively. V indicates an empty Y2H vector. N0, N1, N2 and their combinations are represented by their numerals only. Last row in each panel contained the positive control with T-antigen (T) and p53 (53). The left half of each panel shows growth on SD-His and the right on SD-Ade plates, respectively. The spots in each row in a panel were inoculated by serial dilutions of the same yeast cells with the indicated Y2H plasmids. See text and Materials and Methods for details.

    Article Snippet: Plasmids for Y2H Experiments ( ) The MATCHMAKER System 3 from Clontech was used for the Y2H experiments in this study.

    Techniques: Plasmid Preparation, Positive Control

    Quantification of β-galactosidase in Y2H experiment. The upper and lower panels show the β-galactosidase activity for Pil protein interactions in Y2H experiments from M. xanthus and T. thermophilus , respectively. The values for β-galactosidase activity were the average of three independent experiments and samples in each experiment were analyzed in triplicate. See Figure 4 for protein designations under each panel. The bars for the vector controls are shaded for comparison. See text and Materials and Methods for more details.

    Journal: PLoS ONE

    Article Title: Type IV Pilus Proteins Form an Integrated Structure Extending from the Cytoplasm to the Outer Membrane

    doi: 10.1371/journal.pone.0070144

    Figure Lengend Snippet: Quantification of β-galactosidase in Y2H experiment. The upper and lower panels show the β-galactosidase activity for Pil protein interactions in Y2H experiments from M. xanthus and T. thermophilus , respectively. The values for β-galactosidase activity were the average of three independent experiments and samples in each experiment were analyzed in triplicate. See Figure 4 for protein designations under each panel. The bars for the vector controls are shaded for comparison. See text and Materials and Methods for more details.

    Article Snippet: Plasmids for Y2H Experiments ( ) The MATCHMAKER System 3 from Clontech was used for the Y2H experiments in this study.

    Techniques: Activity Assay, Plasmid Preparation

    Fli-1 overexpression in K562 cells in the maintained presence of endogenous GATA-1. (A) Northern blot analysis of K562 cell lines stably transfected with control plasmid pIRES2-EGFP (lane 1) or Fli-1 expression plasmid pIRES2-Fli-1-EGFP (lane 2). Each lane contains 3 μg of poly(A + ) RNA. The membrane was hybridized with the indicated 32 P-labeled cDNA probes in the order shown. Membranes were stripped prior to each hybridization in the presence of boiling 0.1% SDS. (B) Flow cytometric analysis of K562-GFP and K562-Fli-1-GFP cell lines for the surface expression of markers associated with terminal differentiation of megakaryocytes. The indicated cell lines were incubated in the presence of anti-GPIX, anti-GPIbα, or anti-GPIIb primary antibodies prior to being labeled with phycoerythrin-conjugated secondary antibody, as shown.

    Journal: Molecular and Cellular Biology

    Article Title: Protein-Protein Interaction between Fli-1 and GATA-1 Mediates Synergistic Expression of Megakaryocyte-Specific Genes through Cooperative DNA Binding

    doi: 10.1128/MCB.23.10.3427-3441.2003

    Figure Lengend Snippet: Fli-1 overexpression in K562 cells in the maintained presence of endogenous GATA-1. (A) Northern blot analysis of K562 cell lines stably transfected with control plasmid pIRES2-EGFP (lane 1) or Fli-1 expression plasmid pIRES2-Fli-1-EGFP (lane 2). Each lane contains 3 μg of poly(A + ) RNA. The membrane was hybridized with the indicated 32 P-labeled cDNA probes in the order shown. Membranes were stripped prior to each hybridization in the presence of boiling 0.1% SDS. (B) Flow cytometric analysis of K562-GFP and K562-Fli-1-GFP cell lines for the surface expression of markers associated with terminal differentiation of megakaryocytes. The indicated cell lines were incubated in the presence of anti-GPIX, anti-GPIbα, or anti-GPIIb primary antibodies prior to being labeled with phycoerythrin-conjugated secondary antibody, as shown.

    Article Snippet: The Ets and carboxy-terminus activation domains of human Fli-1 (amino acids 238 to 452) were fused in frame to the GAL4 DNA-binding domain (GAL4DBD) in the pGBKT7 vector (Clontech) and used to screen a K562 cDNA library inserted into the Eco RI sites of the pGAD10 vector (Clontech) in Saccharomyces cerevisiae strain AH109 as described in the Matchmaker GAL4 Two-Hybrid System 3 protocol (Clontech).

    Techniques: Over Expression, Northern Blot, Stable Transfection, Transfection, Plasmid Preparation, Expressing, Labeling, Hybridization, Flow Cytometry, Incubation