ptyb21  (New England Biolabs)


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  • 94
    Name:
    pTYB21 Vector
    Description:
    pTYB21 Vector 10 ug
    Catalog Number:
    n6709s
    Price:
    133
    Size:
    10 ug
    Category:
    E coli Expression Vectors
    Buy from Supplier


    Structured Review

    New England Biolabs ptyb21
    pTYB21 Vector
    pTYB21 Vector 10 ug
    https://www.bioz.com/result/ptyb21/product/New England Biolabs
    Average 94 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    ptyb21 - by Bioz Stars, 2021-02
    94/100 stars

    Images

    1) Product Images from "Bile salts and alkaline pH reciprocally modulate the interaction between the periplasmic domains of Vibrio cholerae ToxR and ToxS"

    Article Title: Bile salts and alkaline pH reciprocally modulate the interaction between the periplasmic domains of Vibrio cholerae ToxR and ToxS

    Journal: Molecular microbiology

    doi: 10.1111/mmi.13699

    Cloning and purification of the ToxR and ToxS periplasmic domains. A. Schematic of ToxR (top) and ToxS (bottom) showing domain boundaries. ToxR contains a cytoplasmic DNA binding domain, while ToxS has a 5 amino acid cytoplasmic tail. Both proteins contain a single pass transmembrane domain along with a C-terminal periplasmic domain. DNA encoding the periplasmic domains of ToxR (T199-E294) and ToxS (S25-S173) were cloned in frame into pTYB21, which contains a N-terminal chitin binding domain intein tag. The amino acid sequences of the purified constructs are shown with the periplasmic domain sequences in bold, and the N-terminal five amino acids leftover from the intein tag after cleavage in gray. B. A Colloidal Blue stained 16% SDS-PAGE gel of 1 μg of purified ToxRp and ToxSp.
    Figure Legend Snippet: Cloning and purification of the ToxR and ToxS periplasmic domains. A. Schematic of ToxR (top) and ToxS (bottom) showing domain boundaries. ToxR contains a cytoplasmic DNA binding domain, while ToxS has a 5 amino acid cytoplasmic tail. Both proteins contain a single pass transmembrane domain along with a C-terminal periplasmic domain. DNA encoding the periplasmic domains of ToxR (T199-E294) and ToxS (S25-S173) were cloned in frame into pTYB21, which contains a N-terminal chitin binding domain intein tag. The amino acid sequences of the purified constructs are shown with the periplasmic domain sequences in bold, and the N-terminal five amino acids leftover from the intein tag after cleavage in gray. B. A Colloidal Blue stained 16% SDS-PAGE gel of 1 μg of purified ToxRp and ToxSp.

    Techniques Used: Clone Assay, Purification, Binding Assay, Construct, Staining, SDS Page

    2) Product Images from "Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity"

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    doi: 10.22037/ijpr.2019.112397.13734

    The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box
    Figure Legend Snippet: The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box

    Techniques Used: Recombinant, Plasmid Preparation, Sequencing

    3) Product Images from "Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity"

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    doi: 10.22037/ijpr.2019.112397.13734

    The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box
    Figure Legend Snippet: The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box

    Techniques Used: Recombinant, Plasmid Preparation, Sequencing

    4) Product Images from "Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity"

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    doi: 10.22037/ijpr.2019.112397.13734

    The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box
    Figure Legend Snippet: The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box

    Techniques Used: Recombinant, Plasmid Preparation, Sequencing

    5) Product Images from "Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity"

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    doi: 10.22037/ijpr.2019.112397.13734

    The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box
    Figure Legend Snippet: The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box

    Techniques Used: Recombinant, Plasmid Preparation, Sequencing

    Related Articles

    Clone Assay:

    Article Title: Crystal Structure of the Human Fatty Acid Synthase Enoyl-Acyl Carrier Protein-Reductase Domain Complexed with Triclosan Reveals Allosteric Protein-Protein Interface Inhibition *
    Article Snippet: .. The cDNA was cloned into a pTYB21 IMPACT vector (New England Biolabs, Ipswich, MA) according to the manufacturer's instructions. ..

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity
    Article Snippet: .. The P24 gene was designed with NdeI restriction site at 5’ end and EcoRI restriction site at the 3´end of the gene for directed cloning into the pTYB21. ..

    Article Title: A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development
    Article Snippet: .. 2.12 Overexpression and Purification of AdcA-NTD The coding sequence of the extracellular domain of adcA without the secretion signal sequence (amino acids 32-320) from strain MGAS10870 was amplified and cloned into Nde I and Bam HI restriction sites of E. coli overexpression vector pTYB21 (New England BioLabs). .. The details of AdcA-NTD purification is described in the Supplemental Experimental Procedures.

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity
    Article Snippet: .. Cloning and transformation of AMP gene-containing construct The P24 gene was digested with NdeI at 5’ end and EcoRI at the 3´end of the gene for site-directed cloning into the pTYB21. .. After confirmation of the desired recombination by polymerase chain reaction (PCR) and electrophoresis on agarose gel, the recombinant vector was cloned into the E. coli TOP10F’ that had an endogenous plasmid with tetracycline resistance gene as the selection marker).

    Amplification:

    Article Title: A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development
    Article Snippet: .. 2.12 Overexpression and Purification of AdcA-NTD The coding sequence of the extracellular domain of adcA without the secretion signal sequence (amino acids 32-320) from strain MGAS10870 was amplified and cloned into Nde I and Bam HI restriction sites of E. coli overexpression vector pTYB21 (New England BioLabs). .. The details of AdcA-NTD purification is described in the Supplemental Experimental Procedures.

    Article Title: Recombinant broad-range phospholipase C from Listeriamonocytogenes exhibits optimal activity at acidic pH
    Article Snippet: .. The amplified fragment was ligated into pTYB21 with T4 DNA ligase (both obtained from New England BioLabs, Ipswich, MA). ..

    Construct:

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity
    Article Snippet: .. Cloning and transformation of AMP gene-containing construct The P24 gene was digested with NdeI at 5’ end and EcoRI at the 3´end of the gene for site-directed cloning into the pTYB21. .. After confirmation of the desired recombination by polymerase chain reaction (PCR) and electrophoresis on agarose gel, the recombinant vector was cloned into the E. coli TOP10F’ that had an endogenous plasmid with tetracycline resistance gene as the selection marker).

    Purification:

    Article Title: A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development
    Article Snippet: .. 2.12 Overexpression and Purification of AdcA-NTD The coding sequence of the extracellular domain of adcA without the secretion signal sequence (amino acids 32-320) from strain MGAS10870 was amplified and cloned into Nde I and Bam HI restriction sites of E. coli overexpression vector pTYB21 (New England BioLabs). .. The details of AdcA-NTD purification is described in the Supplemental Experimental Procedures.

    Sequencing:

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity
    Article Snippet: .. Then, according to the structure of the vector pTYB21, some modifications were applied in to the designed AMP (P19) and five amino acid residues (GRAHM) were added to the N-terminal of P19, which resulted in 24 amino acid sequence of P24. .. Physicochemical characteristics of the designed peptides were predicted by PepFold (http://bioserv.rpbs.univ-paris-diderot.fr/services/PEP-FOLD/) and Helical Wheel draw program from Raphael Zidovetzki’s lab (http://rzlab.ucr.edu/scripts/).

    Article Title: A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development
    Article Snippet: .. 2.12 Overexpression and Purification of AdcA-NTD The coding sequence of the extracellular domain of adcA without the secretion signal sequence (amino acids 32-320) from strain MGAS10870 was amplified and cloned into Nde I and Bam HI restriction sites of E. coli overexpression vector pTYB21 (New England BioLabs). .. The details of AdcA-NTD purification is described in the Supplemental Experimental Procedures.

    Transformation Assay:

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity
    Article Snippet: .. Cloning and transformation of AMP gene-containing construct The P24 gene was digested with NdeI at 5’ end and EcoRI at the 3´end of the gene for site-directed cloning into the pTYB21. .. After confirmation of the desired recombination by polymerase chain reaction (PCR) and electrophoresis on agarose gel, the recombinant vector was cloned into the E. coli TOP10F’ that had an endogenous plasmid with tetracycline resistance gene as the selection marker).

    Over Expression:

    Article Title: A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development
    Article Snippet: .. 2.12 Overexpression and Purification of AdcA-NTD The coding sequence of the extracellular domain of adcA without the secretion signal sequence (amino acids 32-320) from strain MGAS10870 was amplified and cloned into Nde I and Bam HI restriction sites of E. coli overexpression vector pTYB21 (New England BioLabs). .. The details of AdcA-NTD purification is described in the Supplemental Experimental Procedures.

    Plasmid Preparation:

    Article Title: Crystal Structure of the Human Fatty Acid Synthase Enoyl-Acyl Carrier Protein-Reductase Domain Complexed with Triclosan Reveals Allosteric Protein-Protein Interface Inhibition *
    Article Snippet: .. The cDNA was cloned into a pTYB21 IMPACT vector (New England Biolabs, Ipswich, MA) according to the manufacturer's instructions. ..

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity
    Article Snippet: .. Then, according to the structure of the vector pTYB21, some modifications were applied in to the designed AMP (P19) and five amino acid residues (GRAHM) were added to the N-terminal of P19, which resulted in 24 amino acid sequence of P24. .. Physicochemical characteristics of the designed peptides were predicted by PepFold (http://bioserv.rpbs.univ-paris-diderot.fr/services/PEP-FOLD/) and Helical Wheel draw program from Raphael Zidovetzki’s lab (http://rzlab.ucr.edu/scripts/).

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity
    Article Snippet: .. Vector pTYB21 (cat# N6709S, ) was supplied from New England Biolab company (UK). .. The vector contains chitin binding domain and Sec VMA intein sequence upstream of the multiple cloning site (MCS). pTYB21 had ampicillin resistance gene as the selection marker.

    Article Title: A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development
    Article Snippet: .. 2.12 Overexpression and Purification of AdcA-NTD The coding sequence of the extracellular domain of adcA without the secretion signal sequence (amino acids 32-320) from strain MGAS10870 was amplified and cloned into Nde I and Bam HI restriction sites of E. coli overexpression vector pTYB21 (New England BioLabs). .. The details of AdcA-NTD purification is described in the Supplemental Experimental Procedures.

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  • 94
    New England Biolabs ptyb21
    Cloning and purification of the ToxR and ToxS periplasmic domains. A. Schematic of ToxR (top) and ToxS (bottom) showing domain boundaries. ToxR contains a cytoplasmic DNA binding domain, while ToxS has a 5 amino acid cytoplasmic tail. Both proteins contain a single pass transmembrane domain along with a C-terminal periplasmic domain. DNA encoding the periplasmic domains of ToxR (T199-E294) and ToxS (S25-S173) were cloned in frame into <t>pTYB21,</t> which contains a N-terminal chitin binding domain intein tag. The amino acid sequences of the purified constructs are shown with the periplasmic domain sequences in bold, and the N-terminal five amino acids leftover from the intein tag after cleavage in gray. B. A Colloidal Blue stained 16% SDS-PAGE gel of 1 μg of purified ToxRp and ToxSp.
    Ptyb21, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ptyb21/product/New England Biolabs
    Average 94 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    ptyb21 - by Bioz Stars, 2021-02
    94/100 stars
      Buy from Supplier

    Image Search Results


    Cloning and purification of the ToxR and ToxS periplasmic domains. A. Schematic of ToxR (top) and ToxS (bottom) showing domain boundaries. ToxR contains a cytoplasmic DNA binding domain, while ToxS has a 5 amino acid cytoplasmic tail. Both proteins contain a single pass transmembrane domain along with a C-terminal periplasmic domain. DNA encoding the periplasmic domains of ToxR (T199-E294) and ToxS (S25-S173) were cloned in frame into pTYB21, which contains a N-terminal chitin binding domain intein tag. The amino acid sequences of the purified constructs are shown with the periplasmic domain sequences in bold, and the N-terminal five amino acids leftover from the intein tag after cleavage in gray. B. A Colloidal Blue stained 16% SDS-PAGE gel of 1 μg of purified ToxRp and ToxSp.

    Journal: Molecular microbiology

    Article Title: Bile salts and alkaline pH reciprocally modulate the interaction between the periplasmic domains of Vibrio cholerae ToxR and ToxS

    doi: 10.1111/mmi.13699

    Figure Lengend Snippet: Cloning and purification of the ToxR and ToxS periplasmic domains. A. Schematic of ToxR (top) and ToxS (bottom) showing domain boundaries. ToxR contains a cytoplasmic DNA binding domain, while ToxS has a 5 amino acid cytoplasmic tail. Both proteins contain a single pass transmembrane domain along with a C-terminal periplasmic domain. DNA encoding the periplasmic domains of ToxR (T199-E294) and ToxS (S25-S173) were cloned in frame into pTYB21, which contains a N-terminal chitin binding domain intein tag. The amino acid sequences of the purified constructs are shown with the periplasmic domain sequences in bold, and the N-terminal five amino acids leftover from the intein tag after cleavage in gray. B. A Colloidal Blue stained 16% SDS-PAGE gel of 1 μg of purified ToxRp and ToxSp.

    Article Snippet: DNA corresponding to the amino acid sequences of V. cholerae El Tor N16961 ToxR (VC0984) T199-E294 and ToxS (VC0983) S25-S173 were ordered from DNA2.0 and inserted into pTYB21 (NEB).

    Techniques: Clone Assay, Purification, Binding Assay, Construct, Staining, SDS Page

    The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Effect of Amino Acid Substitutions on Biological Activity of Antimicrobial Peptide: Design, Recombinant Production, and Biological Activity

    doi: 10.22037/ijpr.2019.112397.13734

    Figure Lengend Snippet: The structure of recombinant vector pTYB21 for novel designed AMP (P24). (A) The structure of pTYB21; the important parts are outlined with red box. (B) The sequence of first 5 amino acids at MCS of pTYB21, was added to the N-terminal of P19, indicated in red box

    Article Snippet: Cloning and transformation of AMP gene-containing construct The P24 gene was digested with NdeI at 5’ end and EcoRI at the 3´end of the gene for site-directed cloning into the pTYB21.

    Techniques: Recombinant, Plasmid Preparation, Sequencing