ompr  (New England Biolabs)


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    Name:
    BL21 DE3 Competent E coli
    Description:
    BL21 DE3 Competent E coli 20x0 05 ml
    Catalog Number:
    c2527h
    Price:
    204
    Size:
    1 ml
    Category:
    Competent Bacteria
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    Structured Review

    New England Biolabs ompr
    BL21 DE3 Competent E coli
    BL21 DE3 Competent E coli 20x0 05 ml
    https://www.bioz.com/result/ompr/product/New England Biolabs
    Average 91 stars, based on 2138 article reviews
    Price from $9.99 to $1999.99
    ompr - by Bioz Stars, 2020-09
    91/100 stars

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    Images

    1) Product Images from "Phosphoregulated orthogonal signal transduction in mammalian cells"

    Article Title: Phosphoregulated orthogonal signal transduction in mammalian cells

    Journal: Nature Communications

    doi: 10.1038/s41467-020-16895-1

    EnvZ/OmpR and NarX/NarL POST. a Schematic of the engineered ORK/OGR proteins based on EnvZ/OmpR. In the ORK, short linkers consisting only of the two amino acids AS were used to reduce interdomain flexibility between the acV H H and the kinase domain and between the CA and DHp domains by replacing the native GQEMP linker. We hypothesize that this change results in inactive dimers. b Induction of EnvZ/OmpR POST with caffeine. The EnvZ mutant without acV H H (EnvZ 232–450;GQEMP:AS ) was included as a negative control. c Schematic of the engineered ORK/OGR proteins based on NarX/NarL. d Induction of NarX/NarL POST with caffeine. The NarX truncations without acV H H were included as negative controls. The bar charts show the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured at 24 h after induction, and the results are representative of three independent experiments. Source data are provided as a Source Data file.
    Figure Legend Snippet: EnvZ/OmpR and NarX/NarL POST. a Schematic of the engineered ORK/OGR proteins based on EnvZ/OmpR. In the ORK, short linkers consisting only of the two amino acids AS were used to reduce interdomain flexibility between the acV H H and the kinase domain and between the CA and DHp domains by replacing the native GQEMP linker. We hypothesize that this change results in inactive dimers. b Induction of EnvZ/OmpR POST with caffeine. The EnvZ mutant without acV H H (EnvZ 232–450;GQEMP:AS ) was included as a negative control. c Schematic of the engineered ORK/OGR proteins based on NarX/NarL. d Induction of NarX/NarL POST with caffeine. The NarX truncations without acV H H were included as negative controls. The bar charts show the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured at 24 h after induction, and the results are representative of three independent experiments. Source data are provided as a Source Data file.

    Techniques Used: Mutagenesis, Negative Control

    2) Product Images from "Phosphoregulated orthogonal signal transduction in mammalian cells"

    Article Title: Phosphoregulated orthogonal signal transduction in mammalian cells

    Journal: Nature Communications

    doi: 10.1038/s41467-020-16895-1

    EnvZ/OmpR and NarX/NarL POST. a Schematic of the engineered ORK/OGR proteins based on EnvZ/OmpR. In the ORK, short linkers consisting only of the two amino acids AS were used to reduce interdomain flexibility between the acV H H and the kinase domain and between the CA and DHp domains by replacing the native GQEMP linker. We hypothesize that this change results in inactive dimers. b Induction of EnvZ/OmpR POST with caffeine. The EnvZ mutant without acV H H (EnvZ 232–450;GQEMP:AS ) was included as a negative control. c Schematic of the engineered ORK/OGR proteins based on NarX/NarL. d Induction of NarX/NarL POST with caffeine. The NarX truncations without acV H H were included as negative controls. The bar charts show the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured at 24 h after induction, and the results are representative of three independent experiments. Source data are provided as a Source Data file.
    Figure Legend Snippet: EnvZ/OmpR and NarX/NarL POST. a Schematic of the engineered ORK/OGR proteins based on EnvZ/OmpR. In the ORK, short linkers consisting only of the two amino acids AS were used to reduce interdomain flexibility between the acV H H and the kinase domain and between the CA and DHp domains by replacing the native GQEMP linker. We hypothesize that this change results in inactive dimers. b Induction of EnvZ/OmpR POST with caffeine. The EnvZ mutant without acV H H (EnvZ 232–450;GQEMP:AS ) was included as a negative control. c Schematic of the engineered ORK/OGR proteins based on NarX/NarL. d Induction of NarX/NarL POST with caffeine. The NarX truncations without acV H H were included as negative controls. The bar charts show the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured at 24 h after induction, and the results are representative of three independent experiments. Source data are provided as a Source Data file.

    Techniques Used: Mutagenesis, Negative Control

    3) Product Images from "Phosphoregulated orthogonal signal transduction in mammalian cells"

    Article Title: Phosphoregulated orthogonal signal transduction in mammalian cells

    Journal: Nature Communications

    doi: 10.1038/s41467-020-16895-1

    Design of the phosphoregulated orthogonal signal transduction (POST) system. a Mechanism of the native signal cascade activated by the bacterial histidine kinase DcuS. (1) Upon activation, (2) the homodimeric histidine kinase DcuS trans-autophosphorylates a histidine residue in its kinase domain, consisting of the dimerization and histidine-containing phosphotransfer (DHp) domain and the catalytic and ATP-binding (CA) domain. (3) This phosphohistidine is the substrate for the response regulator DcuR that catalyzes the autophosphorylation of an aspartate residue in its dimerization domain. (4) Phosphorylated DcuR dimerizes and (5) binds response elements in its operator site to control (6) gene expression. b Linear schematic depiction of the N-terminal truncation constructs. The constructs start with the amino acid number indicated to the left and end with amino acid number 543 (numbered according to UniProt ID: P0AEC8). c The camelid heavy chain nanoboy acV H H dimerizes in the presence of caffeine. d Schematic illustration of the POST system design. (1) Caffeine induces dimerization of acV H H domains in the engineered orthogonal receptor kinase (ORK), causing (2) kinase trans autophosphorylation and (3) phosphotransfer to an engineered effector protein, such as the orthogonal gene expression regulator (OGR). (4) The effector dimerizes upon phosphotransfer to perform its function, i.e., DNA binding (5), leading to (6) activation of gene expression. e Detailed design of ORK and OGR proteins. The regulatory domain catalyzes the transfer of the phosphoryl group from phosphohistidine to one of its own aspartate residues and subsequently dimerizes.
    Figure Legend Snippet: Design of the phosphoregulated orthogonal signal transduction (POST) system. a Mechanism of the native signal cascade activated by the bacterial histidine kinase DcuS. (1) Upon activation, (2) the homodimeric histidine kinase DcuS trans-autophosphorylates a histidine residue in its kinase domain, consisting of the dimerization and histidine-containing phosphotransfer (DHp) domain and the catalytic and ATP-binding (CA) domain. (3) This phosphohistidine is the substrate for the response regulator DcuR that catalyzes the autophosphorylation of an aspartate residue in its dimerization domain. (4) Phosphorylated DcuR dimerizes and (5) binds response elements in its operator site to control (6) gene expression. b Linear schematic depiction of the N-terminal truncation constructs. The constructs start with the amino acid number indicated to the left and end with amino acid number 543 (numbered according to UniProt ID: P0AEC8). c The camelid heavy chain nanoboy acV H H dimerizes in the presence of caffeine. d Schematic illustration of the POST system design. (1) Caffeine induces dimerization of acV H H domains in the engineered orthogonal receptor kinase (ORK), causing (2) kinase trans autophosphorylation and (3) phosphotransfer to an engineered effector protein, such as the orthogonal gene expression regulator (OGR). (4) The effector dimerizes upon phosphotransfer to perform its function, i.e., DNA binding (5), leading to (6) activation of gene expression. e Detailed design of ORK and OGR proteins. The regulatory domain catalyzes the transfer of the phosphoryl group from phosphohistidine to one of its own aspartate residues and subsequently dimerizes.

    Techniques Used: Transduction, Activation Assay, Binding Assay, Expressing, Construct

    Reducing DcuR autodimerization by generating truncation mutants. a Schematic of DcuS truncation mutants. b Reporter gene expression in response to expression of different DcuS N-terminal truncation variants together with DcuR-VP16. The bar chart shows the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured 24 h after transfection, and the results are representative of three independent experiments. Source data are provided as a Source Data file.
    Figure Legend Snippet: Reducing DcuR autodimerization by generating truncation mutants. a Schematic of DcuS truncation mutants. b Reporter gene expression in response to expression of different DcuS N-terminal truncation variants together with DcuR-VP16. The bar chart shows the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured 24 h after transfection, and the results are representative of three independent experiments. Source data are provided as a Source Data file.

    Techniques Used: Expressing, Transfection

    4) Product Images from "Phosphoregulated orthogonal signal transduction in mammalian cells"

    Article Title: Phosphoregulated orthogonal signal transduction in mammalian cells

    Journal: Nature Communications

    doi: 10.1038/s41467-020-16895-1

    EnvZ/OmpR and NarX/NarL POST. a Schematic of the engineered ORK/OGR proteins based on EnvZ/OmpR. In the ORK, short linkers consisting only of the two amino acids AS were used to reduce interdomain flexibility between the acV H H and the kinase domain and between the CA and DHp domains by replacing the native GQEMP linker. We hypothesize that this change results in inactive dimers. b Induction of EnvZ/OmpR POST with caffeine. The EnvZ mutant without acV H H (EnvZ 232–450;GQEMP:AS ) was included as a negative control. c Schematic of the engineered ORK/OGR proteins based on NarX/NarL. d Induction of NarX/NarL POST with caffeine. The NarX truncations without acV H H were included as negative controls. The bar charts show the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured at 24 h after induction, and the results are representative of three independent experiments. Source data are provided as a Source Data file.
    Figure Legend Snippet: EnvZ/OmpR and NarX/NarL POST. a Schematic of the engineered ORK/OGR proteins based on EnvZ/OmpR. In the ORK, short linkers consisting only of the two amino acids AS were used to reduce interdomain flexibility between the acV H H and the kinase domain and between the CA and DHp domains by replacing the native GQEMP linker. We hypothesize that this change results in inactive dimers. b Induction of EnvZ/OmpR POST with caffeine. The EnvZ mutant without acV H H (EnvZ 232–450;GQEMP:AS ) was included as a negative control. c Schematic of the engineered ORK/OGR proteins based on NarX/NarL. d Induction of NarX/NarL POST with caffeine. The NarX truncations without acV H H were included as negative controls. The bar charts show the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured at 24 h after induction, and the results are representative of three independent experiments. Source data are provided as a Source Data file.

    Techniques Used: Mutagenesis, Negative Control

    5) Product Images from "Phosphoregulated orthogonal signal transduction in mammalian cells"

    Article Title: Phosphoregulated orthogonal signal transduction in mammalian cells

    Journal: Nature Communications

    doi: 10.1038/s41467-020-16895-1

    Design of the phosphoregulated orthogonal signal transduction (POST) system. a Mechanism of the native signal cascade activated by the bacterial histidine kinase DcuS. (1) Upon activation, (2) the homodimeric histidine kinase DcuS trans-autophosphorylates a histidine residue in its kinase domain, consisting of the dimerization and histidine-containing phosphotransfer (DHp) domain and the catalytic and ATP-binding (CA) domain. (3) This phosphohistidine is the substrate for the response regulator DcuR that catalyzes the autophosphorylation of an aspartate residue in its dimerization domain. (4) Phosphorylated DcuR dimerizes and (5) binds response elements in its operator site to control (6) gene expression. b Linear schematic depiction of the N-terminal truncation constructs. The constructs start with the amino acid number indicated to the left and end with amino acid number 543 (numbered according to UniProt ID: P0AEC8). c The camelid heavy chain nanoboy acV H H dimerizes in the presence of caffeine. d Schematic illustration of the POST system design. (1) Caffeine induces dimerization of acV H H domains in the engineered orthogonal receptor kinase (ORK), causing (2) kinase trans autophosphorylation and (3) phosphotransfer to an engineered effector protein, such as the orthogonal gene expression regulator (OGR). (4) The effector dimerizes upon phosphotransfer to perform its function, i.e., DNA binding (5), leading to (6) activation of gene expression. e Detailed design of ORK and OGR proteins. The regulatory domain catalyzes the transfer of the phosphoryl group from phosphohistidine to one of its own aspartate residues and subsequently dimerizes.
    Figure Legend Snippet: Design of the phosphoregulated orthogonal signal transduction (POST) system. a Mechanism of the native signal cascade activated by the bacterial histidine kinase DcuS. (1) Upon activation, (2) the homodimeric histidine kinase DcuS trans-autophosphorylates a histidine residue in its kinase domain, consisting of the dimerization and histidine-containing phosphotransfer (DHp) domain and the catalytic and ATP-binding (CA) domain. (3) This phosphohistidine is the substrate for the response regulator DcuR that catalyzes the autophosphorylation of an aspartate residue in its dimerization domain. (4) Phosphorylated DcuR dimerizes and (5) binds response elements in its operator site to control (6) gene expression. b Linear schematic depiction of the N-terminal truncation constructs. The constructs start with the amino acid number indicated to the left and end with amino acid number 543 (numbered according to UniProt ID: P0AEC8). c The camelid heavy chain nanoboy acV H H dimerizes in the presence of caffeine. d Schematic illustration of the POST system design. (1) Caffeine induces dimerization of acV H H domains in the engineered orthogonal receptor kinase (ORK), causing (2) kinase trans autophosphorylation and (3) phosphotransfer to an engineered effector protein, such as the orthogonal gene expression regulator (OGR). (4) The effector dimerizes upon phosphotransfer to perform its function, i.e., DNA binding (5), leading to (6) activation of gene expression. e Detailed design of ORK and OGR proteins. The regulatory domain catalyzes the transfer of the phosphoryl group from phosphohistidine to one of its own aspartate residues and subsequently dimerizes.

    Techniques Used: Transduction, Activation Assay, Binding Assay, Expressing, Construct

    Reducing DcuR autodimerization by generating truncation mutants. a Schematic of DcuS truncation mutants. b Reporter gene expression in response to expression of different DcuS N-terminal truncation variants together with DcuR-VP16. The bar chart shows the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured 24 h after transfection, and the results are representative of three independent experiments. Source data are provided as a Source Data file.
    Figure Legend Snippet: Reducing DcuR autodimerization by generating truncation mutants. a Schematic of DcuS truncation mutants. b Reporter gene expression in response to expression of different DcuS N-terminal truncation variants together with DcuR-VP16. The bar chart shows the mean ± s.d. of n = 3 biologically independent samples overlaid with a scatter dot plot of the original data points, measured 24 h after transfection, and the results are representative of three independent experiments. Source data are provided as a Source Data file.

    Techniques Used: Expressing, Transfection

    Related Articles

    Clone Assay:

    Article Title: Investigation of the methylerythritol 4-phosphate pathway for microbial terpenoid production through metabolic control analysis
    Article Snippet: .. Bacterial strains and culture conditions Standard cloning and metabolic engineering were carried out using E. coli strains 10β and BL21 (DE3), respectively (both supplied by New England Biolabs, Ipswich, MA, USA). .. For general cloning, the bacteria were cultivated in lysogenic broth (LB) medium, whereas for all other experiments the bacteria were cultivated in M9 medium supplemented with 0.5% (w/v) glucose and appropriate antibiotics (50 μg mL−1 kanamycin, 100 μg mL−1 ampicillin and/or 25 μg mL−1 chloramphenicol) at 37 °C [ ].

    Positron Emission Tomography:

    Article Title: In-cell NMR as a sensitive tool to monitor physiological condition of Escherichia coli
    Article Snippet: .. Protein expression The pET expression plasmid containing cDNA coding GB1 (the T2Q mutant, pI = 4.5, whose amino acid sequence is MQYKLILNGKTLKGETTTEAV DAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE), thermus thermophilus HB8 (TTHA1718) and its homologues (TTHA0227, TTHA0814), human calmodulin (hCaM), and green fluorescent protein (GFP) were individually incorporated into the E . coli BL21(DE3) strain (New England Biolabs, MA, USA). ..

    Mutagenesis:

    Article Title: In-cell NMR as a sensitive tool to monitor physiological condition of Escherichia coli
    Article Snippet: .. Protein expression The pET expression plasmid containing cDNA coding GB1 (the T2Q mutant, pI = 4.5, whose amino acid sequence is MQYKLILNGKTLKGETTTEAV DAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE), thermus thermophilus HB8 (TTHA1718) and its homologues (TTHA0227, TTHA0814), human calmodulin (hCaM), and green fluorescent protein (GFP) were individually incorporated into the E . coli BL21(DE3) strain (New England Biolabs, MA, USA). ..

    Construct:

    Article Title: OccK Channels from Pseudomonas aeruginosa Exhibit Diverse Single-channel Electrical Signatures, but Conserved Anion Selectivity
    Article Snippet: .. BL21(DE3) T1 phage-resistant cells (New England Biolabs, Ipswich, MA) were transformed with pB22-OccK constructs. .. The cells were grown to OD600 ~ 0.6 at 37°C, induced with 0.1% arabinose at 20°C overnight and harvested by centrifugation at 4500 rpm for 30 min (Beckman Coulter, J6-MC).

    other:

    Article Title: The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili from Thermus thermophilus
    Article Snippet: Organisms and cultivation Escherichia coli DH5α, BL21 (DE3) and T7 Express cells harboring pET28a plasmids (New England Biolabs, Ipswich, MA, USA) were grown at 37 °C in LB medium or 2 × YT medium containing 20 μg·mL−1 kanamycin.

    Expressing:

    Article Title: In-cell NMR as a sensitive tool to monitor physiological condition of Escherichia coli
    Article Snippet: .. Protein expression The pET expression plasmid containing cDNA coding GB1 (the T2Q mutant, pI = 4.5, whose amino acid sequence is MQYKLILNGKTLKGETTTEAV DAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE), thermus thermophilus HB8 (TTHA1718) and its homologues (TTHA0227, TTHA0814), human calmodulin (hCaM), and green fluorescent protein (GFP) were individually incorporated into the E . coli BL21(DE3) strain (New England Biolabs, MA, USA). ..

    Article Title: The structure of PghL hydrolase bound to its substrate poly‐γ‐glutamate
    Article Snippet: .. Protein production Expression of PghL from B. subtilis according to the reading frame previously identified was induced from pETSL encoding the pghL gene in BL21(DE3) cells (New England Biolabs, Ipswich, MA, USA). .. A single colony from a freshly transformed Escherichia coli plate was used to inoculate 10 mL of 2xYT media supplemented with 100 μg·μL−1 of carbenicillin D sodium (Apollo Scientific Limited, Stockport, UK) incubated overnight at 37 °C and agitated at 200 r.p.m.

    Sequencing:

    Article Title: In-cell NMR as a sensitive tool to monitor physiological condition of Escherichia coli
    Article Snippet: .. Protein expression The pET expression plasmid containing cDNA coding GB1 (the T2Q mutant, pI = 4.5, whose amino acid sequence is MQYKLILNGKTLKGETTTEAV DAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE), thermus thermophilus HB8 (TTHA1718) and its homologues (TTHA0227, TTHA0814), human calmodulin (hCaM), and green fluorescent protein (GFP) were individually incorporated into the E . coli BL21(DE3) strain (New England Biolabs, MA, USA). ..

    Transformation Assay:

    Article Title: Single-molecule dynamics of the P granule scaffold MEG-3 in the Caenorhabditis elegans zygote
    Article Snippet: .. The resulting vectors, pTG91 (pGEX-KG-TEV-GFP) and pTG93 (pGEX-KG-TEV-meGFP), also included the linker GlySerGlyArgSer between TEV and meGFP/GFP. pTG91 and pTG93 were transformed into BL21(DE3) pLysS (New England Biolabs), grown in 250 ml Terrific Broth at 37°C to OD600 = 0.8 and induced with 1 mM IPTG overnight at 16°C. .. Pellets were resuspended in 20 ml extraction buffer (50 mM Tris–HCl, pH 8, 500 mM NaCl, 5 mM EDTA, 1 mM dithiothreitol [DTT], Roche complete protease inhibitors) and sonicated twice for 60 s. Extracts were pelleted at 17,000 × g for 10 min at 4°C, and supernatants were loaded onto column with glutathione resin (G Biosciences) equilibrated in glutathione S -transferase (GST) buffer (10 mM Tris–HCl, pH 8, 250 mM NaCl, 1 mM EDTA, 1 mM DTT, 0.1 % NP40).

    Article Title: Identification of the agr Peptide of Listeria monocytogenes
    Article Snippet: .. AIP Production in E. coli For heterologous AIP production, pET29a_agrB or pET29a_agrBD were transformed into E. coli BL21(DE3) (New England Biolabs) and transformants were selected on LB agar containing kanamycin. ..

    Article Title: OccK Channels from Pseudomonas aeruginosa Exhibit Diverse Single-channel Electrical Signatures, but Conserved Anion Selectivity
    Article Snippet: .. BL21(DE3) T1 phage-resistant cells (New England Biolabs, Ipswich, MA) were transformed with pB22-OccK constructs. .. The cells were grown to OD600 ~ 0.6 at 37°C, induced with 0.1% arabinose at 20°C overnight and harvested by centrifugation at 4500 rpm for 30 min (Beckman Coulter, J6-MC).

    Plasmid Preparation:

    Article Title: In-cell NMR as a sensitive tool to monitor physiological condition of Escherichia coli
    Article Snippet: .. Protein expression The pET expression plasmid containing cDNA coding GB1 (the T2Q mutant, pI = 4.5, whose amino acid sequence is MQYKLILNGKTLKGETTTEAV DAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE), thermus thermophilus HB8 (TTHA1718) and its homologues (TTHA0227, TTHA0814), human calmodulin (hCaM), and green fluorescent protein (GFP) were individually incorporated into the E . coli BL21(DE3) strain (New England Biolabs, MA, USA). ..

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    • t7 express lysy competent e coli  (New England Biolabs)
    96
    New England Biolabs t7 express lysy competent e coli
    T7 Express Lysy Competent E Coli, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t7 express lysy competent e coli/product/New England Biolabs
    Average 96 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    t7 express lysy competent e coli - by Bioz Stars, 2020-09
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