vector pet22b Millipore Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 79
    Millipore vector plasmid pet22b
    Expression and measurement of anion transport of wild-type ACR2 and its mutants. (A) Western blotting analysis of wild-type ACR2 and its mutants. Cells harboring the <t>pET22b</t> vector alone were used as a negative control. (B) Light-induced pH changes of E. coli cells expressing wild-type ACR2 or its mutants in a solution containing 300 mM NaCl in the absence or presence of CCCP (gray and red lines, respectively). The cell suspensions were illuminated with blue light (480±10 nm) for 3 min (blue stripe).
    Vector Plasmid Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 171 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vector plasmid pet22b/product/Millipore
    Average 79 stars, based on 171 article reviews
    Price from $9.99 to $1999.99
    vector plasmid pet22b - by Bioz Stars, 2020-01
    79/100 stars
      Buy from Supplier

    78
    Millipore expression vector plasmid pet22b
    Expression and measurement of anion transport of wild-type ACR2 and its mutants. (A) Western blotting analysis of wild-type ACR2 and its mutants. Cells harboring the <t>pET22b</t> vector alone were used as a negative control. (B) Light-induced pH changes of E. coli cells expressing wild-type ACR2 or its mutants in a solution containing 300 mM NaCl in the absence or presence of CCCP (gray and red lines, respectively). The cell suspensions were illuminated with blue light (480±10 nm) for 3 min (blue stripe).
    Expression Vector Plasmid Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/expression vector plasmid pet22b/product/Millipore
    Average 78 stars, based on 78 article reviews
    Price from $9.99 to $1999.99
    expression vector plasmid pet22b - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    91
    Merck KGaA pet22b vector
    Expression and measurement of anion transport of wild-type ACR2 and its mutants. (A) Western blotting analysis of wild-type ACR2 and its mutants. Cells harboring the <t>pET22b</t> vector alone were used as a negative control. (B) Light-induced pH changes of E. coli cells expressing wild-type ACR2 or its mutants in a solution containing 300 mM NaCl in the absence or presence of CCCP (gray and red lines, respectively). The cell suspensions were illuminated with blue light (480±10 nm) for 3 min (blue stripe).
    Pet22b Vector, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 91/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet22b vector/product/Merck KGaA
    Average 91 stars, based on 25 article reviews
    Price from $9.99 to $1999.99
    pet22b vector - by Bioz Stars, 2020-01
    91/100 stars
      Buy from Supplier

    78
    Millipore dephosphorylated vector pet22b
    Expression and measurement of anion transport of wild-type ACR2 and its mutants. (A) Western blotting analysis of wild-type ACR2 and its mutants. Cells harboring the <t>pET22b</t> vector alone were used as a negative control. (B) Light-induced pH changes of E. coli cells expressing wild-type ACR2 or its mutants in a solution containing 300 mM NaCl in the absence or presence of CCCP (gray and red lines, respectively). The cell suspensions were illuminated with blue light (480±10 nm) for 3 min (blue stripe).
    Dephosphorylated Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dephosphorylated vector pet22b/product/Millipore
    Average 78 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    dephosphorylated vector pet22b - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    92
    Merck KGaA pet22b expression vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Pet22b Expression Vector, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet22b expression vector/product/Merck KGaA
    Average 92 stars, based on 35 article reviews
    Price from $9.99 to $1999.99
    pet22b expression vector - by Bioz Stars, 2020-01
    92/100 stars
      Buy from Supplier

    78
    Millipore ndei avai digested vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Ndei Avai Digested Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ndei avai digested vector pet22b/product/Millipore
    Average 78 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    ndei avai digested vector pet22b - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    84
    Millipore t7 expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    T7 Expression Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t7 expression vector pet22b/product/Millipore
    Average 84 stars, based on 27 article reviews
    Price from $9.99 to $1999.99
    t7 expression vector pet22b - by Bioz Stars, 2020-01
    84/100 stars
      Buy from Supplier

    80
    Millipore iptg inducible pet22b vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Iptg Inducible Pet22b Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/iptg inducible pet22b vector/product/Millipore
    Average 80 stars, based on 16 article reviews
    Price from $9.99 to $1999.99
    iptg inducible pet22b vector - by Bioz Stars, 2020-01
    80/100 stars
      Buy from Supplier

    78
    Millipore his6 fusion expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    His6 Fusion Expression Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/his6 fusion expression vector pet22b/product/Millipore
    Average 78 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    his6 fusion expression vector pet22b - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    88
    Millipore nde i restriction enzymes pet22b vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Nde I Restriction Enzymes Pet22b Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nde i restriction enzymes pet22b vector/product/Millipore
    Average 88 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    nde i restriction enzymes pet22b vector - by Bioz Stars, 2020-01
    88/100 stars
      Buy from Supplier

    77
    Millipore i hin diii restricted expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    I Hin Diii Restricted Expression Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/i hin diii restricted expression vector pet22b/product/Millipore
    Average 77 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    i hin diii restricted expression vector pet22b - by Bioz Stars, 2020-01
    77/100 stars
      Buy from Supplier

    79
    Millipore t7 promoter polymerase based expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    T7 Promoter Polymerase Based Expression Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t7 promoter polymerase based expression vector pet22b/product/Millipore
    Average 79 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    t7 promoter polymerase based expression vector pet22b - by Bioz Stars, 2020-01
    79/100 stars
      Buy from Supplier

    78
    Millipore pet22b human wt sorcin expression vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Pet22b Human Wt Sorcin Expression Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet22b human wt sorcin expression vector/product/Millipore
    Average 78 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    pet22b human wt sorcin expression vector - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    79
    Millipore nde i hind iii digested expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Nde I Hind Iii Digested Expression Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nde i hind iii digested expression vector pet22b/product/Millipore
    Average 79 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    nde i hind iii digested expression vector pet22b - by Bioz Stars, 2020-01
    79/100 stars
      Buy from Supplier

    78
    Merck & Co pet22b plasmid
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Pet22b Plasmid, supplied by Merck & Co, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet22b plasmid/product/Merck & Co
    Average 78 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    pet22b plasmid - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    70
    Millipore escherichia coli expression plasmid pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Escherichia Coli Expression Plasmid Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 70/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/escherichia coli expression plasmid pet22b/product/Millipore
    Average 70 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    escherichia coli expression plasmid pet22b - by Bioz Stars, 2020-01
    70/100 stars
      Buy from Supplier

    87
    Millipore pet22b vectors
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Pet22b Vectors, supplied by Millipore, used in various techniques. Bioz Stars score: 87/100, based on 299 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet22b vectors/product/Millipore
    Average 87 stars, based on 299 article reviews
    Price from $9.99 to $1999.99
    pet22b vectors - by Bioz Stars, 2020-01
    87/100 stars
      Buy from Supplier

    78
    Millipore vectors pet 22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Vectors Pet 22b, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 259 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vectors pet 22b/product/Millipore
    Average 78 stars, based on 259 article reviews
    Price from $9.99 to $1999.99
    vectors pet 22b - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    84
    Millipore expression vectors pet 22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Expression Vectors Pet 22b, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/expression vectors pet 22b/product/Millipore
    Average 84 stars, based on 40 article reviews
    Price from $9.99 to $1999.99
    expression vectors pet 22b - by Bioz Stars, 2020-01
    84/100 stars
      Buy from Supplier

    99
    Millipore pet 22b vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Pet 22b Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 538 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 22b vector/product/Millipore
    Average 99 stars, based on 538 article reviews
    Price from $9.99 to $1999.99
    pet 22b vector - by Bioz Stars, 2020-01
    99/100 stars
      Buy from Supplier

    98
    Millipore pet 22b expression vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Pet 22b Expression Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 169 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pet 22b expression vector/product/Millipore
    Average 98 stars, based on 169 article reviews
    Price from $9.99 to $1999.99
    pet 22b expression vector - by Bioz Stars, 2020-01
    98/100 stars
      Buy from Supplier

    80
    Millipore periplasmic expression vector pet 22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Periplasmic Expression Vector Pet 22b, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/periplasmic expression vector pet 22b/product/Millipore
    Average 80 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    periplasmic expression vector pet 22b - by Bioz Stars, 2020-01
    80/100 stars
      Buy from Supplier

    70
    Millipore noti linearized expression vector pet 22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Noti Linearized Expression Vector Pet 22b, supplied by Millipore, used in various techniques. Bioz Stars score: 70/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/noti linearized expression vector pet 22b/product/Millipore
    Average 70 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    noti linearized expression vector pet 22b - by Bioz Stars, 2020-01
    70/100 stars
      Buy from Supplier

    78
    Millipore pa83 pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Pa83 Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pa83 pet22b/product/Millipore
    Average 78 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    pa83 pet22b - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    87
    Millipore protein expression vector pet 22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a <t>pET22b</t> vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.
    Protein Expression Vector Pet 22b, supplied by Millipore, used in various techniques. Bioz Stars score: 87/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protein expression vector pet 22b/product/Millipore
    Average 87 stars, based on 37 article reviews
    Price from $9.99 to $1999.99
    protein expression vector pet 22b - by Bioz Stars, 2020-01
    87/100 stars
      Buy from Supplier

    85
    Millipore standard pet 22b vector
    Loci acclimation in vitro . E. coli expressing the Yiu transporter require a threefold greater time to acclimate under nutrient-limiting conditions than E. coli expressing the Yfe transporter. ( a , b , c ) Periplasmic fractions of E. coli constructs growing in various in vitro media conditions. Black arrows denote the positions of electrophoretic migration for YfeA ( b ) and YiuA ( c ). Lanes 1–4 represent time points 3, 5, 7 and 10 h from M9 minimal medium base conditions. Lanes 5–8 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 5 µ M Fe 2 (SO 4 ) 3 supplementation. Lanes 9–12 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 1 m M EDDA supplementation. Molecular-weight markers are labeled in kDa. ( d , e , f ) Growth curves for the <t>pET-22b</t> construct ( d ), pYFE3 construct ( e ) and pYIU3 construct ( f ). Error bars represent the standard deviation in OD 600 from experiments performed in triplicate.
    Standard Pet 22b Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/standard pet 22b vector/product/Millipore
    Average 85 stars, based on 16 article reviews
    Price from $9.99 to $1999.99
    standard pet 22b vector - by Bioz Stars, 2020-01
    85/100 stars
      Buy from Supplier

    79
    Millipore escherichia coli pet 22b expression vectors
    Loci acclimation in vitro . E. coli expressing the Yiu transporter require a threefold greater time to acclimate under nutrient-limiting conditions than E. coli expressing the Yfe transporter. ( a , b , c ) Periplasmic fractions of E. coli constructs growing in various in vitro media conditions. Black arrows denote the positions of electrophoretic migration for YfeA ( b ) and YiuA ( c ). Lanes 1–4 represent time points 3, 5, 7 and 10 h from M9 minimal medium base conditions. Lanes 5–8 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 5 µ M Fe 2 (SO 4 ) 3 supplementation. Lanes 9–12 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 1 m M EDDA supplementation. Molecular-weight markers are labeled in kDa. ( d , e , f ) Growth curves for the <t>pET-22b</t> construct ( d ), pYFE3 construct ( e ) and pYIU3 construct ( f ). Error bars represent the standard deviation in OD 600 from experiments performed in triplicate.
    Escherichia Coli Pet 22b Expression Vectors, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/escherichia coli pet 22b expression vectors/product/Millipore
    Average 79 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    escherichia coli pet 22b expression vectors - by Bioz Stars, 2020-01
    79/100 stars
      Buy from Supplier

    78
    Millipore escherichia coli periplasmic targeting vector pet 22b
    ( a ) The architecture of gp41. FP (residues 512–527), fusion peptide; FPPR (residues 528–539), fusion peptide proximal region; NHR (residues 540–­590), N-terminal heptad-repeat region; CHR (residues 628–661), C-­terminal heptad-repeat region; MPER (residues 662–684), membrane-proximal external region; MPR (residues 647–684, hatched), membrane-proximal region; TM (residues 685–705), transmembrane domain; CTD (residues 706–856), cytoplasmic C-terminal domain. ( b , c , d ) DNA constructs for the expression in E. coli of the indicated CTB-MPR fusion proteins are based on elements of the <t>pET-22b</t> expression vector. P, T7 bacteriophage promoter; 5′-UTR, upstream untranslated region; pelB, the <t>periplasmic</t> targeting sequence of pectate lyase B of Erwinia carotovora ; CTB, cholera toxin B subunit; MPR, the membrane-proximal region of the gp41 protein of HIV-1; 3′-UTR, downstream untranslated region; T, T7 terminator. The GPGP and AAAA linkers are indicated above their respective constructs. The three constructs encode the fusion proteins CTB GPGP MPR ( b ), CTBMPR ( c ) and CTB AAAA MPR ( d ) with expected molecular masses (after the processing of the pelB leader sequence) of 16.7, 16.4 and 16.7 kDa, respectively.
    Escherichia Coli Periplasmic Targeting Vector Pet 22b, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/escherichia coli periplasmic targeting vector pet 22b/product/Millipore
    Average 78 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    escherichia coli periplasmic targeting vector pet 22b - by Bioz Stars, 2020-01
    78/100 stars
      Buy from Supplier

    Image Search Results


    Expression and measurement of anion transport of wild-type ACR2 and its mutants. (A) Western blotting analysis of wild-type ACR2 and its mutants. Cells harboring the pET22b vector alone were used as a negative control. (B) Light-induced pH changes of E. coli cells expressing wild-type ACR2 or its mutants in a solution containing 300 mM NaCl in the absence or presence of CCCP (gray and red lines, respectively). The cell suspensions were illuminated with blue light (480±10 nm) for 3 min (blue stripe).

    Journal: Biophysics and Physicobiology

    Article Title: Mutational analysis of the conserved carboxylates of anion channelrhodopsin-2 (ACR2) expressed in Escherichia coli and their roles in anion transport

    doi: 10.2142/biophysico.15.0_179

    Figure Lengend Snippet: Expression and measurement of anion transport of wild-type ACR2 and its mutants. (A) Western blotting analysis of wild-type ACR2 and its mutants. Cells harboring the pET22b vector alone were used as a negative control. (B) Light-induced pH changes of E. coli cells expressing wild-type ACR2 or its mutants in a solution containing 300 mM NaCl in the absence or presence of CCCP (gray and red lines, respectively). The cell suspensions were illuminated with blue light (480±10 nm) for 3 min (blue stripe).

    Article Snippet: A cDNA encoding the 7-transmembrane domain of ACR2 (Genbank accession no. , amino acid residues from the first to the 266th position) was inserted into the pET22b plasmid vector (Novagen, USA) with NdeI and XhoI restriction enzyme sites as previously described [ ].

    Techniques: Expressing, Western Blot, Plasmid Preparation, Negative Control

    Expression of NSP3 in E. coli and purification of deletion mutants. (A) The cDNA encoding NSP3 from group A and group C rotavirus was cloned in pET22b+LS− and introduced in E. coli BL21(DE3). Expression of the viral proteins was induced by addition of 1 mM IPTG to the cell culture for 3 h. Whole-cell proteins were resolved by SDS-PAGE and stained with Coomassie blue. (B) Recombinant proteins were purified on an Ni 2+ -Sepharose column and renatured by step dialysis. Proteins were resolved by SDS-PAGE and stained with Coomassie blue. MW, molecular weight (in thousands).

    Journal: Journal of Virology

    Article Title: Identification of the RNA-Binding, Dimerization, and eIF4GI-Binding Domains of Rotavirus Nonstructural Protein NSP3

    doi:

    Figure Lengend Snippet: Expression of NSP3 in E. coli and purification of deletion mutants. (A) The cDNA encoding NSP3 from group A and group C rotavirus was cloned in pET22b+LS− and introduced in E. coli BL21(DE3). Expression of the viral proteins was induced by addition of 1 mM IPTG to the cell culture for 3 h. Whole-cell proteins were resolved by SDS-PAGE and stained with Coomassie blue. (B) Recombinant proteins were purified on an Ni 2+ -Sepharose column and renatured by step dialysis. Proteins were resolved by SDS-PAGE and stained with Coomassie blue. MW, molecular weight (in thousands).

    Article Snippet: Recombinant proteins were expressed with a C-terminal His6 tag in a modified pET22b+ plasmid (Novagen).

    Techniques: Expressing, Purification, Clone Assay, Cell Culture, SDS Page, Staining, Recombinant, Molecular Weight

    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a pET22b vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.

    Journal: Frontiers in Microbiology

    Article Title: Characterization of ML-005, a Novel Metaproteomics-Derived Esterase

    doi: 10.3389/fmicb.2018.01925

    Figure Lengend Snippet: (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis ) showed a sequence identity of 28.44% (highlighted in black, similar amino acids in shades of gray). Residues forming the catalytic triad i.e., serine, (99), aspartic acid (164), and histidine (191) are highlighted in yellow. These residues form an integral part of the active site. The pentapeptide Ala – His – Ser – Leu – Gly motif is highlighted in green. This represents the nucleophilic elbow and is a conserved structure found within lipolytic enzymes. Residues 1–20 form a signal peptide (red) which was processed in E. coli (see panel C ). (B) Three dimensional structure of ML-005 was modeled using the Phyre 2 ). Potential catalytic triad residues (His-191, Asp-164, and Ser-99) were predicted to be in close proximity to each other. The structural alignment with YdeN from B. subtilis (green ribbon) shows substantial similarity (C) ML-005 was cloned into a pET22b vector with a T7 promoter system and a C-terminal His 6 -tag und purified to homogeneity. The purified ML-005 band showed a size that approximates 23.4 kDa, consistent with the calculated mass of His 6 -tagged ML-005 with a removed signal peptide.

    Article Snippet: In short, the codon-optimized and artificially synthesized ML-005 gene sequence (645 bp) was cloned into the pET22b expression vector (Merck Millipore, Billerica, MA, United States) containing a T7-promotor. pET22b additionally codes for a C-terminal His6 -tag that was thus fused to ML-005 (For the vector sequence including insert see Supplementary Data Sheet ).

    Techniques: Sequencing, Clone Assay, Plasmid Preparation, Purification

    Loci acclimation in vitro . E. coli expressing the Yiu transporter require a threefold greater time to acclimate under nutrient-limiting conditions than E. coli expressing the Yfe transporter. ( a , b , c ) Periplasmic fractions of E. coli constructs growing in various in vitro media conditions. Black arrows denote the positions of electrophoretic migration for YfeA ( b ) and YiuA ( c ). Lanes 1–4 represent time points 3, 5, 7 and 10 h from M9 minimal medium base conditions. Lanes 5–8 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 5 µ M Fe 2 (SO 4 ) 3 supplementation. Lanes 9–12 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 1 m M EDDA supplementation. Molecular-weight markers are labeled in kDa. ( d , e , f ) Growth curves for the pET-22b construct ( d ), pYFE3 construct ( e ) and pYIU3 construct ( f ). Error bars represent the standard deviation in OD 600 from experiments performed in triplicate.

    Journal: Acta Crystallographica. Section D, Structural Biology

    Article Title: The crystal structure of the Yersinia pestis iron chaperone YiuA reveals a basic triad binding motif for the chelated metal

    doi: 10.1107/S2059798317015236

    Figure Lengend Snippet: Loci acclimation in vitro . E. coli expressing the Yiu transporter require a threefold greater time to acclimate under nutrient-limiting conditions than E. coli expressing the Yfe transporter. ( a , b , c ) Periplasmic fractions of E. coli constructs growing in various in vitro media conditions. Black arrows denote the positions of electrophoretic migration for YfeA ( b ) and YiuA ( c ). Lanes 1–4 represent time points 3, 5, 7 and 10 h from M9 minimal medium base conditions. Lanes 5–8 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 5 µ M Fe 2 (SO 4 ) 3 supplementation. Lanes 9–12 represent time points 3, 5, 7 and 10 h from M9 minimal medium with 1 m M EDDA supplementation. Molecular-weight markers are labeled in kDa. ( d , e , f ) Growth curves for the pET-22b construct ( d ), pYFE3 construct ( e ) and pYIU3 construct ( f ). Error bars represent the standard deviation in OD 600 from experiments performed in triplicate.

    Article Snippet: The yiuA gene was then cloned into a standard pET-22b vector (Novagen, catalog No. 69744) using NdeI and XhoI cloning sites.

    Techniques: In Vitro, Expressing, Construct, Migration, Molecular Weight, Labeling, Positron Emission Tomography, Standard Deviation

    ( a ) The architecture of gp41. FP (residues 512–527), fusion peptide; FPPR (residues 528–539), fusion peptide proximal region; NHR (residues 540–­590), N-terminal heptad-repeat region; CHR (residues 628–661), C-­terminal heptad-repeat region; MPER (residues 662–684), membrane-proximal external region; MPR (residues 647–684, hatched), membrane-proximal region; TM (residues 685–705), transmembrane domain; CTD (residues 706–856), cytoplasmic C-terminal domain. ( b , c , d ) DNA constructs for the expression in E. coli of the indicated CTB-MPR fusion proteins are based on elements of the pET-22b expression vector. P, T7 bacteriophage promoter; 5′-UTR, upstream untranslated region; pelB, the periplasmic targeting sequence of pectate lyase B of Erwinia carotovora ; CTB, cholera toxin B subunit; MPR, the membrane-proximal region of the gp41 protein of HIV-1; 3′-UTR, downstream untranslated region; T, T7 terminator. The GPGP and AAAA linkers are indicated above their respective constructs. The three constructs encode the fusion proteins CTB GPGP MPR ( b ), CTBMPR ( c ) and CTB AAAA MPR ( d ) with expected molecular masses (after the processing of the pelB leader sequence) of 16.7, 16.4 and 16.7 kDa, respectively.

    Journal: IUCrJ

    Article Title: Expression, purification and crystallization of CTB-MPR, a candidate mucosal vaccine component against HIV-1

    doi: 10.1107/S2052252514014900

    Figure Lengend Snippet: ( a ) The architecture of gp41. FP (residues 512–527), fusion peptide; FPPR (residues 528–539), fusion peptide proximal region; NHR (residues 540–­590), N-terminal heptad-repeat region; CHR (residues 628–661), C-­terminal heptad-repeat region; MPER (residues 662–684), membrane-proximal external region; MPR (residues 647–684, hatched), membrane-proximal region; TM (residues 685–705), transmembrane domain; CTD (residues 706–856), cytoplasmic C-terminal domain. ( b , c , d ) DNA constructs for the expression in E. coli of the indicated CTB-MPR fusion proteins are based on elements of the pET-22b expression vector. P, T7 bacteriophage promoter; 5′-UTR, upstream untranslated region; pelB, the periplasmic targeting sequence of pectate lyase B of Erwinia carotovora ; CTB, cholera toxin B subunit; MPR, the membrane-proximal region of the gp41 protein of HIV-1; 3′-UTR, downstream untranslated region; T, T7 terminator. The GPGP and AAAA linkers are indicated above their respective constructs. The three constructs encode the fusion proteins CTB GPGP MPR ( b ), CTBMPR ( c ) and CTB AAAA MPR ( d ) with expected molecular masses (after the processing of the pelB leader sequence) of 16.7, 16.4 and 16.7 kDa, respectively.

    Article Snippet: Vectors for bacterial expression of CTB-MPR fusion protein variants The expression vectors used in this study were all based on the Escherichia coli periplasmic targeting vector pET-22b(−) (Novagen; Figs. 1 b , 1 c and 1 d ).

    Techniques: Construct, Expressing, CtB Assay, Positron Emission Tomography, Plasmid Preparation, Sequencing