pet30a vector Search Results


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  • 89
    Millipore pet 30a vectors
    Pet 30a Vectors, supplied by Millipore, used in various techniques. Bioz Stars score: 89/100, based on 97 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 30a vectors/product/Millipore
    Average 89 stars, based on 97 article reviews
    Price from $9.99 to $1999.99
    pet 30a vectors - by Bioz Stars, 2020-08
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    93
    Millipore pet30a vector
    r Pc PHB1 prevents WSSV replication. The crayfish were assigned into four groups, namely, Pc PHB1 plus WSSV, <t>PET30A</t> plus WSSV, BSA plus WSSV, and WSSV, and the amounts of virus were analyzed via qRT-PCR using VP28 as a marker (A), as well as Western blot
    Pet30a Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1476 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a vector/product/Millipore
    Average 93 stars, based on 1476 article reviews
    Price from $9.99 to $1999.99
    pet30a vector - by Bioz Stars, 2020-08
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    93
    Merck & Co pet30a vector
    r Pc PHB1 prevents WSSV replication. The crayfish were assigned into four groups, namely, Pc PHB1 plus WSSV, <t>PET30A</t> plus WSSV, BSA plus WSSV, and WSSV, and the amounts of virus were analyzed via qRT-PCR using VP28 as a marker (A), as well as Western blot
    Pet30a Vector, supplied by Merck & Co, used in various techniques. Bioz Stars score: 93/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a vector/product/Merck & Co
    Average 93 stars, based on 62 article reviews
    Price from $9.99 to $1999.99
    pet30a vector - by Bioz Stars, 2020-08
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    91
    TaKaRa pet30a vector
    r Pc PHB1 prevents WSSV replication. The crayfish were assigned into four groups, namely, Pc PHB1 plus WSSV, <t>PET30A</t> plus WSSV, BSA plus WSSV, and WSSV, and the amounts of virus were analyzed via qRT-PCR using VP28 as a marker (A), as well as Western blot
    Pet30a Vector, supplied by TaKaRa, used in various techniques. Bioz Stars score: 91/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a vector/product/TaKaRa
    Average 91 stars, based on 34 article reviews
    Price from $9.99 to $1999.99
    pet30a vector - by Bioz Stars, 2020-08
    91/100 stars
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    91
    Merck KGaA pet30a vector
    r Pc PHB1 prevents WSSV replication. The crayfish were assigned into four groups, namely, Pc PHB1 plus WSSV, <t>PET30A</t> plus WSSV, BSA plus WSSV, and WSSV, and the amounts of virus were analyzed via qRT-PCR using VP28 as a marker (A), as well as Western blot
    Pet30a Vector, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 91/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a vector/product/Merck KGaA
    Average 91 stars, based on 41 article reviews
    Price from $9.99 to $1999.99
    pet30a vector - by Bioz Stars, 2020-08
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    91
    Promega pet30a vector
    r Pc PHB1 prevents WSSV replication. The crayfish were assigned into four groups, namely, Pc PHB1 plus WSSV, <t>PET30A</t> plus WSSV, BSA plus WSSV, and WSSV, and the amounts of virus were analyzed via qRT-PCR using VP28 as a marker (A), as well as Western blot
    Pet30a Vector, supplied by Promega, used in various techniques. Bioz Stars score: 91/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a vector/product/Promega
    Average 91 stars, based on 21 article reviews
    Price from $9.99 to $1999.99
    pet30a vector - by Bioz Stars, 2020-08
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    91
    Thermo Fisher pet30a vector
    Construction of recombinant <t>pET30a‐PoIFN‐ω7</t> and PCR identification of mature PoIFN‐ω7 gens. A, The PoIFN‐ω7 sequence was inserted into the vector at the EcoR I and Hind ‐restriction sites. Plasmid pET30a‐PoIFN‐ω7 consisted of a His tag and the mature PoIFN‐ω7 sequence. B, PCR identification of the mature PoIFN‐ω7 gene. Lane M: 2000 bp DNA marker; Lane 1: mature PoIFN‐ω7 gene. PCR, polymerase chain reaction
    Pet30a Vector, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a vector/product/Thermo Fisher
    Average 91 stars, based on 31 article reviews
    Price from $9.99 to $1999.99
    pet30a vector - by Bioz Stars, 2020-08
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    93
    Novogen pet30a vector
    The inhibitory effects of LvCHH1 and LvCHH2 on the expression of LvIAG . (A) Expression level of LvIAG after unilateral eyestalk ablation. (B) Expression levels of LvIAG after LvCHH1 knockdown. (C) Expression levels of LvIAG after LvCHH2 knockdown. dsEGFP, injected with dsEGFP; dsCHH1, injected with dsCHH1; dsCHH2, injected with dsCHH2. (D) The recombination proteins of LvCHHs. 1–3, inclusion body; 1, <t>pET30a;</t> 2, rCHH1; 3, rCHH2; 4–6, supernatant; 4, pET30a; 5, rCHH1; 6, rCHH2; M, protein ladder. (E) The recombination proteins of LvCHHs after purification and refolding. 1, rCHH1; 2, rCHH2; M, protein ladder. (F) Expression levels of LvIAG after injection with rCHH1 and rCHH2. PBS, injected with PBS; rCHH1, injected with rCHH1; rCHH2, injected with rCHH2. Expression levels of target genes were detected in three replicates. Significant differences of the gene expression levels between two treatments were shown with a star ( ∗ ) at P
    Pet30a Vector, supplied by Novogen, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a vector/product/Novogen
    Average 93 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    pet30a vector - by Bioz Stars, 2020-08
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    89
    Millipore pet 30a vector
    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with <t>pET-30a–</t> Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).
    Pet 30a Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 89/100, based on 560 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 30a vector/product/Millipore
    Average 89 stars, based on 560 article reviews
    Price from $9.99 to $1999.99
    pet 30a vector - by Bioz Stars, 2020-08
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    89
    Merck KGaA pet 30a vector
    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with <t>pET-30a–</t> Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).
    Pet 30a Vector, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 89/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 30a vector/product/Merck KGaA
    Average 89 stars, based on 35 article reviews
    Price from $9.99 to $1999.99
    pet 30a vector - by Bioz Stars, 2020-08
    89/100 stars
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    92
    Merck & Co pet 30a vector
    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with <t>pET-30a–</t> Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).
    Pet 30a Vector, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 30a vector/product/Merck & Co
    Average 92 stars, based on 24 article reviews
    Price from $9.99 to $1999.99
    pet 30a vector - by Bioz Stars, 2020-08
    92/100 stars
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    89
    TaKaRa pet 30a vector
    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with <t>pET-30a–</t> Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).
    Pet 30a Vector, supplied by TaKaRa, used in various techniques. Bioz Stars score: 89/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 30a vector/product/TaKaRa
    Average 89 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    pet 30a vector - by Bioz Stars, 2020-08
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    90
    GenScript pet 30a expression vectors
    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with <t>pET-30a–</t> Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).
    Pet 30a Expression Vectors, supplied by GenScript, used in various techniques. Bioz Stars score: 90/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 30a expression vectors/product/GenScript
    Average 90 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    pet 30a expression vectors - by Bioz Stars, 2020-08
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    93
    GenScript pet30a expression vector
    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with <t>pET-30a–</t> Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).
    Pet30a Expression Vector, supplied by GenScript, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet30a expression vector/product/GenScript
    Average 93 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    pet30a expression vector - by Bioz Stars, 2020-08
    93/100 stars
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    86
    Thermo Fisher expression vector pet30a kmr
    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with <t>pET-30a–</t> Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).
    Expression Vector Pet30a Kmr, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/expression vector pet30a kmr/product/Thermo Fisher
    Average 86 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    expression vector pet30a kmr - by Bioz Stars, 2020-08
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    Image Search Results


    r Pc PHB1 prevents WSSV replication. The crayfish were assigned into four groups, namely, Pc PHB1 plus WSSV, PET30A plus WSSV, BSA plus WSSV, and WSSV, and the amounts of virus were analyzed via qRT-PCR using VP28 as a marker (A), as well as Western blot

    Journal: Journal of Virology

    Article Title: Prohibitin Interacts with Envelope Proteins of White Spot Syndrome Virus and Prevents Infection in the Red Swamp Crayfish, Procambarus clarkii

    doi: 10.1128/JVI.02198-13

    Figure Lengend Snippet: r Pc PHB1 prevents WSSV replication. The crayfish were assigned into four groups, namely, Pc PHB1 plus WSSV, PET30A plus WSSV, BSA plus WSSV, and WSSV, and the amounts of virus were analyzed via qRT-PCR using VP28 as a marker (A), as well as Western blot

    Article Snippet: The PCR products from the ExEcoRF and ExXhoR primers were then cloned into the pET30a vector (Novagen).

    Techniques: Quantitative RT-PCR, Marker, Western Blot

    Analysis of Ni 2+ -NTA column affinity-purified MS2. Lane 1, prestained protein markers; lane 2, 10 μL of eluted solution from the Ni 2+ -NTA affinity column incubated with the protein from control bacteria containing the empty vector pET30a; lane

    Journal: Plant Physiology

    Article Title: Male Sterile2 Encodes a Plastid-Localized Fatty Acyl Carrier Protein Reductase Required for Pollen Exine Development in Arabidopsis 1 Encodes a Plastid-Localized Fatty Acyl Carrier Protein Reductase Required for Pollen Exine Development in Arabidopsis 1 [C] Encodes a Plastid-Localized Fatty Acyl Carrier Protein Reductase Required for Pollen Exine Development in Arabidopsis 1 [C] [W] Encodes a Plastid-Localized Fatty Acyl Carrier Protein Reductase Required for Pollen Exine Development in Arabidopsis 1 [C] [W] [OA]

    doi: 10.1104/pp.111.181693

    Figure Lengend Snippet: Analysis of Ni 2+ -NTA column affinity-purified MS2. Lane 1, prestained protein markers; lane 2, 10 μL of eluted solution from the Ni 2+ -NTA affinity column incubated with the protein from control bacteria containing the empty vector pET30a; lane

    Article Snippet: To this end, we cloned the full-length MS2 cDNA into the expression vector pET30a (Novagen) and introduced it into E. coli BL21 (DE3).

    Techniques: Affinity Column, Purification, Incubation, Plasmid Preparation

    Construction and imaging of GFP-Mos1 fusion transposase. ( A ) Mos1 and GFP-Mos1 transposase fusion protein constructs in pET30a expression vector. ( B ) Coomassie stained 12% SDS-PAGE in Tris-Glycine-SDS buffer of purified Mos1 and GFP-Mos1 transposases. ( C ) Live cell imaging with 60× magnification after transfection of HeLa cells with purified GFP-Mos1 transposase in complex with donor DNA. Scale bar is 10 μm. Images are representatives of 10 image points on a dish. ( D ) Quantification of the GFP signal in the nucleus and cytoplasm over time after transfection; 10 cells were analyzed. Shadowed error bars represent the standard deviation. ( E ) Western blotting analysis of HeLa cells lysates after transfection with GFP-Mos1 and donor plasmid. Proteins were separated on 4–12% NuPAGE SDS-PAGE in MOPS buffer (buffer composition, acrylamide percentage and protein concentration affect protein migration). Lane 1–1 ng of purified GFP, lane 2–10 ng of purified GFP-Mos1, lane 3-mock, no transposase or DNA was added to the cells. In lanes 3–7, 250 μg of total HeLa cell extracts were loaded. Lanes 4–7 contain full-length GFP-Mos1 transposase with no evidence of protein degradation 20 h post transfection. The antibody against GFP recognizes an unspecific protein, which is present in all time points and the mock control. Lane 7 shows lower signal for GFP-Mos1 protein since the cells have undergone division, which dilutes GFP-Mos1 concentration versus total protein concentration.

    Journal: Nucleic Acids Research

    Article Title: Use of mariner transposases for one-step delivery and integration of DNA in prokaryotes and eukaryotes by transfection

    doi: 10.1093/nar/gkx113

    Figure Lengend Snippet: Construction and imaging of GFP-Mos1 fusion transposase. ( A ) Mos1 and GFP-Mos1 transposase fusion protein constructs in pET30a expression vector. ( B ) Coomassie stained 12% SDS-PAGE in Tris-Glycine-SDS buffer of purified Mos1 and GFP-Mos1 transposases. ( C ) Live cell imaging with 60× magnification after transfection of HeLa cells with purified GFP-Mos1 transposase in complex with donor DNA. Scale bar is 10 μm. Images are representatives of 10 image points on a dish. ( D ) Quantification of the GFP signal in the nucleus and cytoplasm over time after transfection; 10 cells were analyzed. Shadowed error bars represent the standard deviation. ( E ) Western blotting analysis of HeLa cells lysates after transfection with GFP-Mos1 and donor plasmid. Proteins were separated on 4–12% NuPAGE SDS-PAGE in MOPS buffer (buffer composition, acrylamide percentage and protein concentration affect protein migration). Lane 1–1 ng of purified GFP, lane 2–10 ng of purified GFP-Mos1, lane 3-mock, no transposase or DNA was added to the cells. In lanes 3–7, 250 μg of total HeLa cell extracts were loaded. Lanes 4–7 contain full-length GFP-Mos1 transposase with no evidence of protein degradation 20 h post transfection. The antibody against GFP recognizes an unspecific protein, which is present in all time points and the mock control. Lane 7 shows lower signal for GFP-Mos1 protein since the cells have undergone division, which dilutes GFP-Mos1 concentration versus total protein concentration.

    Article Snippet: The N-terminal Green Fluorescent Protein (GFP) fusion of Mos1 was assembled with pET30a expression vector (Novagen) using the PaperClip DNA assembly method ( ).

    Techniques: Imaging, Construct, Expressing, Plasmid Preparation, Staining, SDS Page, Purification, Live Cell Imaging, Transfection, Standard Deviation, Western Blot, Protein Concentration, Migration, Concentration Assay

    Construction of recombinant pET30a‐PoIFN‐ω7 and PCR identification of mature PoIFN‐ω7 gens. A, The PoIFN‐ω7 sequence was inserted into the vector at the EcoR I and Hind ‐restriction sites. Plasmid pET30a‐PoIFN‐ω7 consisted of a His tag and the mature PoIFN‐ω7 sequence. B, PCR identification of the mature PoIFN‐ω7 gene. Lane M: 2000 bp DNA marker; Lane 1: mature PoIFN‐ω7 gene. PCR, polymerase chain reaction

    Journal: Journal of Medical Virology

    Article Title: Antiviral activity of porcine interferon omega 7 against foot‐and‐mouth disease virus in vitro, et al. Antiviral activity of porcine interferon omega 7 against foot‐and‐mouth disease virus in vitro

    doi: 10.1002/jmv.25272

    Figure Lengend Snippet: Construction of recombinant pET30a‐PoIFN‐ω7 and PCR identification of mature PoIFN‐ω7 gens. A, The PoIFN‐ω7 sequence was inserted into the vector at the EcoR I and Hind ‐restriction sites. Plasmid pET30a‐PoIFN‐ω7 consisted of a His tag and the mature PoIFN‐ω7 sequence. B, PCR identification of the mature PoIFN‐ω7 gene. Lane M: 2000 bp DNA marker; Lane 1: mature PoIFN‐ω7 gene. PCR, polymerase chain reaction

    Article Snippet: After digested by Eco RI and Hin d III restriction sites from the vector, the target gene was ligated into the corresponding sites in the pET30a vector (Invitrogen, CA).

    Techniques: Recombinant, Polymerase Chain Reaction, Sequencing, Plasmid Preparation, Marker

    Analysis of the expressed and purified PoIFN‐ω7 protein by SDS‐PAGE and Western‐blot, respectively. A, Lane M: protein marker; Lane 1: pET‐30a vector after induction; Lane 2: pET30a‐PoIFN‐ω7 in soluble fraction after induction; Lane 3: pET30a‐PoIFN‐ω7 in inclusion bodies after induction; Lane 4: before loading onto column; Lane 5: purified and dialyzed PoIFN‐ω7. B, Western blot confirmation of PoIFN‐ω7 using anti‐polyhistidine monoclonal antibody. Lane M: Protein marker; Lane 1: pET‐30a vector after induction; Lane 2: purified PoIFN‐ω7 protein

    Journal: Journal of Medical Virology

    Article Title: Antiviral activity of porcine interferon omega 7 against foot‐and‐mouth disease virus in vitro, et al. Antiviral activity of porcine interferon omega 7 against foot‐and‐mouth disease virus in vitro

    doi: 10.1002/jmv.25272

    Figure Lengend Snippet: Analysis of the expressed and purified PoIFN‐ω7 protein by SDS‐PAGE and Western‐blot, respectively. A, Lane M: protein marker; Lane 1: pET‐30a vector after induction; Lane 2: pET30a‐PoIFN‐ω7 in soluble fraction after induction; Lane 3: pET30a‐PoIFN‐ω7 in inclusion bodies after induction; Lane 4: before loading onto column; Lane 5: purified and dialyzed PoIFN‐ω7. B, Western blot confirmation of PoIFN‐ω7 using anti‐polyhistidine monoclonal antibody. Lane M: Protein marker; Lane 1: pET‐30a vector after induction; Lane 2: purified PoIFN‐ω7 protein

    Article Snippet: After digested by Eco RI and Hin d III restriction sites from the vector, the target gene was ligated into the corresponding sites in the pET30a vector (Invitrogen, CA).

    Techniques: Purification, SDS Page, Western Blot, Marker, Positron Emission Tomography, Plasmid Preparation

    The inhibitory effects of LvCHH1 and LvCHH2 on the expression of LvIAG . (A) Expression level of LvIAG after unilateral eyestalk ablation. (B) Expression levels of LvIAG after LvCHH1 knockdown. (C) Expression levels of LvIAG after LvCHH2 knockdown. dsEGFP, injected with dsEGFP; dsCHH1, injected with dsCHH1; dsCHH2, injected with dsCHH2. (D) The recombination proteins of LvCHHs. 1–3, inclusion body; 1, pET30a; 2, rCHH1; 3, rCHH2; 4–6, supernatant; 4, pET30a; 5, rCHH1; 6, rCHH2; M, protein ladder. (E) The recombination proteins of LvCHHs after purification and refolding. 1, rCHH1; 2, rCHH2; M, protein ladder. (F) Expression levels of LvIAG after injection with rCHH1 and rCHH2. PBS, injected with PBS; rCHH1, injected with rCHH1; rCHH2, injected with rCHH2. Expression levels of target genes were detected in three replicates. Significant differences of the gene expression levels between two treatments were shown with a star ( ∗ ) at P

    Journal: Frontiers in Physiology

    Article Title: Sex-Biased CHHs and Their Putative Receptor Regulate the Expression of IAG Gene in the Shrimp Litopenaeus vannamei

    doi: 10.3389/fphys.2019.01525

    Figure Lengend Snippet: The inhibitory effects of LvCHH1 and LvCHH2 on the expression of LvIAG . (A) Expression level of LvIAG after unilateral eyestalk ablation. (B) Expression levels of LvIAG after LvCHH1 knockdown. (C) Expression levels of LvIAG after LvCHH2 knockdown. dsEGFP, injected with dsEGFP; dsCHH1, injected with dsCHH1; dsCHH2, injected with dsCHH2. (D) The recombination proteins of LvCHHs. 1–3, inclusion body; 1, pET30a; 2, rCHH1; 3, rCHH2; 4–6, supernatant; 4, pET30a; 5, rCHH1; 6, rCHH2; M, protein ladder. (E) The recombination proteins of LvCHHs after purification and refolding. 1, rCHH1; 2, rCHH2; M, protein ladder. (F) Expression levels of LvIAG after injection with rCHH1 and rCHH2. PBS, injected with PBS; rCHH1, injected with rCHH1; rCHH2, injected with rCHH2. Expression levels of target genes were detected in three replicates. Significant differences of the gene expression levels between two treatments were shown with a star ( ∗ ) at P

    Article Snippet: Primers LvCHH1-rpF/rpR, LvCHH2-rpF/rpR were designed with 15 bp extension homologous of linearized pET30a vector (Novogen, France) ends at both ends to amply the ORF of LvCHH1 and LvCHH2 excluding sequence encoding signal peptide, respectively.

    Techniques: Expressing, Injection, Purification

    Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with pET-30a– Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).

    Journal: mSphere

    Article Title: Genetic Validation of Leishmania donovani Lysyl-tRNA Synthetase Shows that It Is Indispensable for Parasite Growth and Infectivity

    doi: 10.1128/mSphereDirect.00340-17

    Figure Lengend Snippet: Protein induction, purification, and enzymatic characterization of recombinant Ld LysRS-1. (A) SDS-PAGE analysis of whole-cell lysate of uninduced and induced E. coli BL21(DE3) cells transformed with pET-30a– Ld LysRS-1. M, molecular mass marker; lane 1, uninduced bacterial cell lysate; lane 2, induced bacterial cell lysate. (B) Purification of r Ld LysRS-1 protein on Ni 2+ -NTA affinity resin. M, molecular mass marker; lane 1, eluted fraction with 100 mM imidazole showing purified r Ld LysRS-1. (C) GPC elution profile of purified Ld LysRS-1. Comparison with standard markers indicates that Ld LysRS-1 elutes at a size corresponding to the dimeric state. mAU, milli-absorbance unit. (D) Western blot analysis of the r Ld LysRS-1 protein and promastigote cell lysates of wild-type (WT) parasites using anti- Ld LysRS-1 antibody. Lane 1, 0.5 μg r Ld LysRS-1 protein; lane 2, 1 μg r Ld LysRS-1 protein; lane 3, 2 μg r Ld LysRS-1 protein; lane 4, Leishmania promastigote cell lysate (~40 μg). (E) Western blot analysis of the r Ld LysRS-1 protein and amastigote cell lysates of WT parasites. Lane 1, 2 μg recombinant Ld LysRS-1 protein; lane 2, Leishmania amastigote cell lysate (~40 μg). (F) Time course of tRNA Lys aminoacylation by recombinant Ld LysRS-1. Reactions were performed with l -lysine and tRNA Lys as the substrates. The data show an average from three experiments performed in duplicate ± SD. (G and H) Aminoacylation kinetics of Ld LysRS-1 as a function of l -lysine concentration (G) and tRNA Lys concentration (H). The results represent means ± SD ( n = 3).

    Article Snippet: The digested 1,761-bp PCR product covering the Ld LysRS open reading frame (ORF) was cloned in frame into BamHI and HindIII restriction sites of pET-30a vector (Novagen).

    Techniques: Purification, Recombinant, SDS Page, Transformation Assay, Positron Emission Tomography, Marker, Gel Permeation Chromatography, Western Blot, Concentration Assay

    Agarose gel electrophoresis of PCR products and recombinant plasmids digested with Eco RI and Xho I. (a) Lane M, DNA marker; Lane 1, the 2163-bp fragment product from VD1-ORF4 . (b) Lane M, DNA marker; Lane 1, pMD18-T- VD1-ORF4 /2163 digested with Eco RI and Xho I. (c) Lane M, DNA marker; Lane 1, the 3318-bp fragment product from VD1-ORF4 . (d) Lane M, DNA marker; Lane 1, pMD18-T- VD1-ORF4 digested with Eco RI and Xho I. (e) Lane M, DNA maker; Lane 1, pET-30a- VD1-ORF4 /2163 digested with Eco RI and Xho I; Lane 2, the 2163-bp PCR product from VD1-ORF4 .

    Journal: Genetics and Molecular Biology

    Article Title: Molecular cloning and expression of key gene encoding hypothetical DNA polymerase from B. mori parvo-like virus

    doi: 10.1590/S1415-47572010005000083

    Figure Lengend Snippet: Agarose gel electrophoresis of PCR products and recombinant plasmids digested with Eco RI and Xho I. (a) Lane M, DNA marker; Lane 1, the 2163-bp fragment product from VD1-ORF4 . (b) Lane M, DNA marker; Lane 1, pMD18-T- VD1-ORF4 /2163 digested with Eco RI and Xho I. (c) Lane M, DNA marker; Lane 1, the 3318-bp fragment product from VD1-ORF4 . (d) Lane M, DNA marker; Lane 1, pMD18-T- VD1-ORF4 digested with Eco RI and Xho I. (e) Lane M, DNA maker; Lane 1, pET-30a- VD1-ORF4 /2163 digested with Eco RI and Xho I; Lane 2, the 2163-bp PCR product from VD1-ORF4 .

    Article Snippet: Expression of BmPLV-Z VD1-ORF4 (2163 bp) in E.coli and Western blot analysis The 2163-bp fragment was excised from pMD18-T-VD1-ORF4 (2163 bp) by Eco RI and Xho I, and subsequently subcloned into the pET-30a expression vector (Novagen, USA) in frame with a 6xHis tag at the N terminus.

    Techniques: Agarose Gel Electrophoresis, Polymerase Chain Reaction, Recombinant, Marker, Positron Emission Tomography

    Identification of induced target-protein expression in E. coli Rosetta TM 2 (DE3) pLysS, together with Western blot and MALDI-TOF analysis of the induced protein. (a) SDS-PAGE and Western blot analysis of the target protein induced in RosettaTM 2 (DE3) pLysS. Lane M, protein marker; Lane 1, RosettaTM 2 (DE3) plysS with pET-30a- VD1-ORF4 /2163 induced without IPTG; Lane 2-4, Rosetta TM 2 (DE3) plysS with pET-30a- VD1-ORF4 /2163 induced by IPTG concentrations of 0.2, 0.5, 0.8 mmol/L, respectively; Lane 5, the target protein was examined with an antibody against the 6xHis tag. (b) Peptide sequences identified by mass spectrometry. The Bm PLV-Z VD1-ORF4 deduced amino acid sequence is shown, and the matched peptide sequences are indicated as red characters.

    Journal: Genetics and Molecular Biology

    Article Title: Molecular cloning and expression of key gene encoding hypothetical DNA polymerase from B. mori parvo-like virus

    doi: 10.1590/S1415-47572010005000083

    Figure Lengend Snippet: Identification of induced target-protein expression in E. coli Rosetta TM 2 (DE3) pLysS, together with Western blot and MALDI-TOF analysis of the induced protein. (a) SDS-PAGE and Western blot analysis of the target protein induced in RosettaTM 2 (DE3) pLysS. Lane M, protein marker; Lane 1, RosettaTM 2 (DE3) plysS with pET-30a- VD1-ORF4 /2163 induced without IPTG; Lane 2-4, Rosetta TM 2 (DE3) plysS with pET-30a- VD1-ORF4 /2163 induced by IPTG concentrations of 0.2, 0.5, 0.8 mmol/L, respectively; Lane 5, the target protein was examined with an antibody against the 6xHis tag. (b) Peptide sequences identified by mass spectrometry. The Bm PLV-Z VD1-ORF4 deduced amino acid sequence is shown, and the matched peptide sequences are indicated as red characters.

    Article Snippet: Expression of BmPLV-Z VD1-ORF4 (2163 bp) in E.coli and Western blot analysis The 2163-bp fragment was excised from pMD18-T-VD1-ORF4 (2163 bp) by Eco RI and Xho I, and subsequently subcloned into the pET-30a expression vector (Novagen, USA) in frame with a 6xHis tag at the N terminus.

    Techniques: Expressing, Western Blot, SDS Page, Marker, Positron Emission Tomography, Mass Spectrometry, Sequencing