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pet29b vector  (Millipore)


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    Structured Review

    Millipore pet29b vector
    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
    pet29b vector - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    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 pET29b (Novagen) vector by polymerase chain reaction (PCR), and inserting it into pRNA128A (Williams et al., 2010), a vector with the ColE1 origin of replication.

    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 pET29b vector (Novagen, http://www.novagen.com/). ..

    Article Title: Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein
    Article Snippet: .. The amplified gene was cloned into a pET29b vector (Novagen, Inc., Madison, WI) under the control of a T7 promoter (pET29b-SSB BA recombinant plasmid). ..

    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 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). ..

    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 pET29b vector (Novagen, http://www.novagen.com/). ..

    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 pET29b vector (Novagen), which encodes a carboxy-terminal hexa-His-Tag for protein purification. ..

    Article Title: Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein
    Article Snippet: .. The amplified gene was cloned into a pET29b vector (Novagen, Inc., Madison, WI) under the control of a T7 promoter (pET29b-SSB BA recombinant plasmid). ..

    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 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). ..

    Article Title: Method of improving the pharmacokinetic profile of a therapeutic polypeptide and the use thereof
    Article Snippet: .. The pET29b vector (Novagen) was used to construct a recombinant plasmid containing the GLP-1-Fn7-COL18NC1 fusion gene. .. First, human COL18NC1 was cloned into pET29b by BamHI and XhoI to result in the pET29b-COL18NC1 vector.

    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 pET29b vector (Novagen), which encodes a carboxy-terminal hexa-His-Tag for protein purification. ..

    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 pET29b vector (Novagen), which encodes a carboxy-terminal hexa-His-Tag for protein purification. ..

    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 pET29b vector (Novagen). ..

    Article Title: Method of improving the pharmacokinetic profile of a therapeutic polypeptide and the use thereof
    Article Snippet: .. The pET29b vector (Novagen) was used to construct a recombinant plasmid containing the GLP-1-Fn7-COL18NC1 fusion gene. .. First, human COL18NC1 was cloned into pET29b by BamHI and XhoI to result in the pET29b-COL18NC1 vector.

    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 pET29b vector (Novagen, Inc., Madison, WI) under the control of a T7 promoter (pET29b-SSB BA recombinant plasmid). ..

    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 pET29b vector (Novagen) with T4 DNA ligase (New England BioLabs). ..

    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 pET29b vector (Novagen, Inc., Madison, WI) under the control of a T7 promoter (pET29b-SSB BA recombinant plasmid). ..

    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 pET29b vector (Novagen, Inc., Madison, WI) under the control of a T7 promoter (pET29b-SSB BA recombinant plasmid). ..

    Article Title: Method of improving the pharmacokinetic profile of a therapeutic polypeptide and the use thereof
    Article Snippet: .. The pET29b vector (Novagen) was used to construct a recombinant plasmid containing the GLP-1-Fn7-COL18NC1 fusion gene. .. First, human COL18NC1 was cloned into pET29b by BamHI and XhoI to result in the pET29b-COL18NC1 vector.

    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 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). ..

    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 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). ..



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    Image Search Results


    (a) 3D structure, and (b) topology diagram of the haloalkane dehalogenase DhaA31 (PDB:3RK4). The lid domain is shown in red and the Rossman fold domain is shown in green. α Helices and β strands belonging to the ‘Rossman’ fold domain (lid domain) are represented by green (red) rectangles and green (red) arrows, respectively. The location and identity of the catalytic triad is indicated by blue dots. Both the (c) 3D structure and (d) topology diagram of the lipase (PDB:1OIL) are highly similar to the dehalogenase.

    Journal: bioRxiv

    Article Title: Framework for Martini-based Coarse-grained Model of Enzymes: Model Development and Experimental Validation

    doi: 10.1101/2024.09.22.614383

    Figure Lengend Snippet: (a) 3D structure, and (b) topology diagram of the haloalkane dehalogenase DhaA31 (PDB:3RK4). The lid domain is shown in red and the Rossman fold domain is shown in green. α Helices and β strands belonging to the ‘Rossman’ fold domain (lid domain) are represented by green (red) rectangles and green (red) arrows, respectively. The location and identity of the catalytic triad is indicated by blue dots. Both the (c) 3D structure and (d) topology diagram of the lipase (PDB:1OIL) are highly similar to the dehalogenase.

    Article Snippet: DhaA31 was overexpressed in competent cells of the E. coli BL21 strain, which were transformed with a pET29b+ vector containing the DhaA31 gene (Twist Biosciences) with a C-terminal 6xHis-tag.

    Techniques: