vector pet22b Millipore Search Results


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  • 99
    Millipore expression vector pet22b
    Schematic depicting the construction of <t>pET22b-pelB</t> hGH (left) and pET22b-ompA hGH (right) expression vectors The gene encoding hGH was PCR amplified as described in Materials and Methods and restriction cloned into the pET22b E. coli expression vector.
    Expression Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 576 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Millipore vector pet22b
    SDS-PAG analysis of the recombinant EglC22b stained with Coomassie blue. Lane M: protein MW marker (18.9–94.4 kDa); Lane 1: IPTG-induced E. coli <t>pET22b-EglC;</t> Lane 2: E. coli pET22b-EglC; Lane 3: IPTG-induced E. coli pET22b; Lane 4: E. coli pET22b; Lane 5: purified EglC22b.
    Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 89/100, based on 438 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Merck KGaA pet22b vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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 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
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    90
    Millipore dephosphorylated vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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.
    Dephosphorylated Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Millipore vector pjm103
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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.
    Vector Pjm103, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore pet22b secretion vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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 Secretion Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore pet22b vector dna
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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 Vector Dna, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore ndei avai digested vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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: 85/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore p22b vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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.
    P22b Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore t7 expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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: 91/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore inducible expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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.
    Inducible Expression Vector Pet22b, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore gateway home adapted pet22b vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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.
    Gateway Home Adapted Pet22b Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore his6 fusion expression vector pet22b
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore iptg inducible pet22b vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore pet22b novagen derivative vector
    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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 Novagen Derivative Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Schematic depicting the construction of pET22b-pelB hGH (left) and pET22b-ompA hGH (right) expression vectors The gene encoding hGH was PCR amplified as described in Materials and Methods and restriction cloned into the pET22b E. coli expression vector.

    Journal: Protein expression and purification

    Article Title: Periplasmic production via the pET expression system of soluble, bioactive human growth hormone

    doi: 10.1016/j.pep.2012.11.002

    Figure Lengend Snippet: Schematic depicting the construction of pET22b-pelB hGH (left) and pET22b-ompA hGH (right) expression vectors The gene encoding hGH was PCR amplified as described in Materials and Methods and restriction cloned into the pET22b E. coli expression vector.

    Article Snippet: The resulting PCR product was purified and restriction cloned into the NcoI and XhoI sites of the bacterial expression vector pET22b (Novagen; San Diego, CA).

    Techniques: Expressing, Polymerase Chain Reaction, Amplification, Clone Assay, Plasmid Preparation

    SDS-PAG analysis of the recombinant EglC22b stained with Coomassie blue. Lane M: protein MW marker (18.9–94.4 kDa); Lane 1: IPTG-induced E. coli pET22b-EglC; Lane 2: E. coli pET22b-EglC; Lane 3: IPTG-induced E. coli pET22b; Lane 4: E. coli pET22b; Lane 5: purified EglC22b.

    Journal: PeerJ

    Article Title: Cloning, expression and characterization of a cold-adapted endo-1, 4-β-glucanase from Citrobacter farmeri A1, a symbiotic bacterium of Reticulitermes labralis

    doi: 10.7717/peerj.2679

    Figure Lengend Snippet: SDS-PAG analysis of the recombinant EglC22b stained with Coomassie blue. Lane M: protein MW marker (18.9–94.4 kDa); Lane 1: IPTG-induced E. coli pET22b-EglC; Lane 2: E. coli pET22b-EglC; Lane 3: IPTG-induced E. coli pET22b; Lane 4: E. coli pET22b; Lane 5: purified EglC22b.

    Article Snippet: The plasmid pMD20-T vector (TaKaRa, Dalian, China) and E. coli DH5α were used for gene cloning, whereas the pET22b vector (Novagen, Madison, WI) and E. coli BL21 (laboratory stock) were used for gene expression.

    Techniques: Recombinant, Staining, Marker, Purification

    SDS-PAGE and western blotting analysis of Epinephelus coioides interferon gamma (IFNγ). IFNγ1 (A) or IFNγ2 (B) proteins was expressed using the pET22b expression vector. (A) Lane M: protein size marker; Lane 1: the total lysates from non-induced cells; Lane 2: the total lysates from IPTG-induced cells; Lane 3: soluble IFNγ1 protein; Lane 4–7: IFNγ1 protein by washing buffer with different imidazole concentration; Lane 8: purified recombinant protein with a His-tag; (B) Lane M: protein size marker; Lane 1: the total lysates from non-induced cells; Lane 2: the total lysates from IPTG-induced cells; Lane 3: soluble IFNγ2 protein; Lane 4–8: IFNγ2 protein by washing buffer with pH6.3, pH5.9, pH5.4, pH5.0, and pH4.5. (C) Verification of recombinant IFNγ1 and IFNγ2 by Western blot. Lane 1: IFNγ1; Lane 2: IFNγ2; they were analyzed on a 15% SDS-PAGE gel, followed by western blotting analysis using a mAb against the His-tag. The molecular weight of the lane 1 IFNγ1 was the same to that of the lane 8 of Figure 5 A. Similarly, that of lane 2 IFNγ2 was also the same to the lane 8 of Figure 5 B.

    Journal: Frontiers in Endocrinology

    Article Title: Two Distinct Interferon-γ in the Orange-Spotted Grouper (Epinephelus coioides): Molecular Cloning, Functional Characterization, and Regulation in Toll-Like Receptor Pathway by Induction of miR-146a

    doi: 10.3389/fendo.2018.00041

    Figure Lengend Snippet: SDS-PAGE and western blotting analysis of Epinephelus coioides interferon gamma (IFNγ). IFNγ1 (A) or IFNγ2 (B) proteins was expressed using the pET22b expression vector. (A) Lane M: protein size marker; Lane 1: the total lysates from non-induced cells; Lane 2: the total lysates from IPTG-induced cells; Lane 3: soluble IFNγ1 protein; Lane 4–7: IFNγ1 protein by washing buffer with different imidazole concentration; Lane 8: purified recombinant protein with a His-tag; (B) Lane M: protein size marker; Lane 1: the total lysates from non-induced cells; Lane 2: the total lysates from IPTG-induced cells; Lane 3: soluble IFNγ2 protein; Lane 4–8: IFNγ2 protein by washing buffer with pH6.3, pH5.9, pH5.4, pH5.0, and pH4.5. (C) Verification of recombinant IFNγ1 and IFNγ2 by Western blot. Lane 1: IFNγ1; Lane 2: IFNγ2; they were analyzed on a 15% SDS-PAGE gel, followed by western blotting analysis using a mAb against the His-tag. The molecular weight of the lane 1 IFNγ1 was the same to that of the lane 8 of Figure 5 A. Similarly, that of lane 2 IFNγ2 was also the same to the lane 8 of Figure 5 B.

    Article Snippet: After subcloning into pTZ57R/T vector for sequencing, the fragments were digested with restriction enzymes and then inserted into the pET22b expression vector (Novagen, USA).

    Techniques: SDS Page, Western Blot, Expressing, Plasmid Preparation, Marker, Concentration Assay, Purification, Recombinant, Molecular Weight

    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

    (A) Sequence alignment of ML-005 with the uncharacterized esterase YdeN from Bacillus subtilis (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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 (UniProt accession number P96671.1 ) 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 server (blue ribbon; http://www.sbg.bio.ic.ac.uk/phyre/ ). 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