pet29b vector (Millipore)
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Pet29b Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pet29b+vector/pet28a/pmc11374688-182-33-35
Average 90 stars, based on 1 article reviews
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other:Article Title: Engineering an Escherichia coli based in vivo mRNA manufacturing platform. Article Snippet: High copy number plasmids were constructed by amplifying the mRNA encoding region from the original Clone Assay:Article Title: Structural insights and membrane binding properties of MGD1, the major galactolipid synthase in plants. Article Snippet: Construction of MGD1 recombinant proteins The generation of the catalytic domain protein construct (cdMGD1) has been described elsewhere (Rocha et al., 2013). .. Briefly, the catalytic domain of MGD1 (residues 137–533), with a C–terminal His6 tag, was cloned into Article Title: Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein Article Snippet: .. The amplified gene was cloned into a Article Title: Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression Article Snippet: Synthetic genes encoding the four designed variants were cloned into the pET29b vector (Novagen) for inducible expression in Eschericia coli and the level of soluble expression and assembly state of all nine possible pairwise combinations of original, negatively, or positively charged A and B subunits was then assessed by mixing cell lysates containing the individually expressed subunits and analyzing the resulting soluble and insoluble fractions by polyacrylamide gel electrophoresis (PAGE). .. Synthetic genes encoding the four designed variants were cloned into the Plasmid Preparation:Article Title: Structural insights and membrane binding properties of MGD1, the major galactolipid synthase in plants. Article Snippet: Construction of MGD1 recombinant proteins The generation of the catalytic domain protein construct (cdMGD1) has been described elsewhere (Rocha et al., 2013). .. Briefly, the catalytic domain of MGD1 (residues 137–533), with a C–terminal His6 tag, was cloned into Article Title: A Lepidopteran-Specific Gene Family Encoding Valine-Rich Midgut Proteins Article Snippet: .. The resulting PCR product was restricted with BamH I and EcoR I, and ligated into the linearized Article Title: Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein Article Snippet: .. The amplified gene was cloned into a Article Title: Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression Article Snippet: Synthetic genes encoding the four designed variants were cloned into the pET29b vector (Novagen) for inducible expression in Eschericia coli and the level of soluble expression and assembly state of all nine possible pairwise combinations of original, negatively, or positively charged A and B subunits was then assessed by mixing cell lysates containing the individually expressed subunits and analyzing the resulting soluble and insoluble fractions by polyacrylamide gel electrophoresis (PAGE). .. Synthetic genes encoding the four designed variants were cloned into the Article Title: Method of improving the pharmacokinetic profile of a therapeutic polypeptide and the use thereof Article Snippet: .. The Polymerase Chain Reaction:Article Title: A Lepidopteran-Specific Gene Family Encoding Valine-Rich Midgut Proteins Article Snippet: .. The resulting PCR product was restricted with BamH I and EcoR I, and ligated into the linearized Protein Purification:Article Title: A Lepidopteran-Specific Gene Family Encoding Valine-Rich Midgut Proteins Article Snippet: .. The resulting PCR product was restricted with BamH I and EcoR I, and ligated into the linearized Construct:Article Title: Structural basis for transthiolation intermediates in the ubiquitin pathway Article Snippet: .. Constructs encoding full-length S. pombe Ubc4(C21S/C107S) with a C-terminal Gly–Gly linker followed by thrombin-cleavable His 6 tag, and constructs for full-length S. pombe Ubc4 with C-terminal His 6 tag were constructed using the Article Title: Method of improving the pharmacokinetic profile of a therapeutic polypeptide and the use thereof Article Snippet: .. The Amplification:Article Title: Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein Article Snippet: .. The amplified gene was cloned into a Article Title: PvdF of pyoverdin biosynthesis is a structurally unique N 10 -formyltetrahydrofolate-dependent formyltransferase Article Snippet: .. The amplified DNA fragment was ligated into the correspondingly digested Control:Article Title: Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein Article Snippet: .. The amplified gene was cloned into a Recombinant:Article Title: Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein Article Snippet: .. The amplified gene was cloned into a Article Title: Method of improving the pharmacokinetic profile of a therapeutic polypeptide and the use thereof Article Snippet: .. The Expressing:Article Title: Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression Article Snippet: Synthetic genes encoding the four designed variants were cloned into the pET29b vector (Novagen) for inducible expression in Eschericia coli and the level of soluble expression and assembly state of all nine possible pairwise combinations of original, negatively, or positively charged A and B subunits was then assessed by mixing cell lysates containing the individually expressed subunits and analyzing the resulting soluble and insoluble fractions by polyacrylamide gel electrophoresis (PAGE). .. Synthetic genes encoding the four designed variants were cloned into the Polyacrylamide Gel Electrophoresis:Article Title: Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression Article Snippet: Synthetic genes encoding the four designed variants were cloned into the pET29b vector (Novagen) for inducible expression in Eschericia coli and the level of soluble expression and assembly state of all nine possible pairwise combinations of original, negatively, or positively charged A and B subunits was then assessed by mixing cell lysates containing the individually expressed subunits and analyzing the resulting soluble and insoluble fractions by polyacrylamide gel electrophoresis (PAGE). .. Synthetic genes encoding the four designed variants were cloned into the |
