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    T7 Express lysY Competent E coli High Efficiency
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    T7 Express lysY Competent E coli High Efficiency 6x0 2 ml
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    c3010i
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    New England Biolabs ompr
    T7 Express lysY Competent E coli High Efficiency
    T7 Express lysY Competent E coli High Efficiency 6x0 2 ml
    https://www.bioz.com/result/ompr/product/New England Biolabs
    Average 91 stars, based on 2135 article reviews
    Price from $9.99 to $1999.99
    ompr - by Bioz Stars, 2020-08
    91/100 stars

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    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: Enhanced uptake of potassium or glycine betaine or export of cyclic-di-AMP restores osmoresistance in a high cyclic-di-AMP Lactococcus lactis mutant
    Article Snippet: .. Wild-type or 42 amino acid deleted busR and downstream busAA promoter were cloned into pTCV-lac and introduced into E . coli T7 Express LysY (New England Biolabs) with selection using kanamycin (50 μg/ml). .. For β-galactosidase activity assays, strains were grown overnight in LB broth without NaCl (10 g/L tryptone; 5 g/L Yeast extract) and then diluted 1:100 in the same fresh LB medium and grown at 30°C, aeration 220 rpm to early log phase (OD600 ~0.25) where 0, 0.1, 0.2, 0.3 or 0.4 M NaCl was added.

    Selection:

    Article Title: Enhanced uptake of potassium or glycine betaine or export of cyclic-di-AMP restores osmoresistance in a high cyclic-di-AMP Lactococcus lactis mutant
    Article Snippet: .. Wild-type or 42 amino acid deleted busR and downstream busAA promoter were cloned into pTCV-lac and introduced into E . coli T7 Express LysY (New England Biolabs) with selection using kanamycin (50 μg/ml). .. For β-galactosidase activity assays, strains were grown overnight in LB broth without NaCl (10 g/L tryptone; 5 g/L Yeast extract) and then diluted 1:100 in the same fresh LB medium and grown at 30°C, aeration 220 rpm to early log phase (OD600 ~0.25) where 0, 0.1, 0.2, 0.3 or 0.4 M NaCl was added.

    Isolation:

    Article Title: Context-dependent function of a conserved translational regulatory module
    Article Snippet: .. GST fusion proteins were isolated from T7 Express lysY competent E. coli (New England BioLabs) and purified using the following elution buffer: 1×PBS, 0.2% Tween 20, 150 mM NaCl, 0.1% 2-mercaptoethanol, 50 mM glutathione (reduced, pH 8.0). .. Twenty femtomoles 32 P end-labeled oligoribonucleotides (Dharmacon) were combined with GST-Cbr-PUF-2 or GST-Cbr-PUF-1.2 at various concentrations as described ( ).

    Construct:

    Article Title: Comparative analysis of the end-joining activity of several DNA ligases
    Article Snippet: .. All constructs were expressed in T7 Express lysY/I q E . coli cells (NEB) using 0.5 mM IPTG for 2 hours at 30°C for induction. .. The β isoform of hLig3 was purified as described previously[ ].

    Article Title: Structure-function analysis of Methanobacterium thermoautotrophicum RNA ligase - engineering a thermostable ATP independent enzyme
    Article Snippet: .. The resulting constructs were sequenced and expressed in T7 Express lysY/I q E.coli cells (NEB) as follows. ..

    Purification:

    Article Title: Context-dependent function of a conserved translational regulatory module
    Article Snippet: .. GST fusion proteins were isolated from T7 Express lysY competent E. coli (New England BioLabs) and purified using the following elution buffer: 1×PBS, 0.2% Tween 20, 150 mM NaCl, 0.1% 2-mercaptoethanol, 50 mM glutathione (reduced, pH 8.0). .. Twenty femtomoles 32 P end-labeled oligoribonucleotides (Dharmacon) were combined with GST-Cbr-PUF-2 or GST-Cbr-PUF-1.2 at various concentrations as described ( ).

    Expressing:

    Article Title: Spy Go purification of SpyTag-proteins using pseudo-SpyCatcher to access an oligomerization toolbox
    Article Snippet: .. Bacterial protein expression pET28a-SpyTag-MBP, pET28a-SpyTag002-MBP, and pET28a-SpyTag-mClover3 were transformed into chemically competent E. coli BL21 (DE3) RIPL (Agilent Technologies). pET28a-scPvuII-SpyTag was transformed into T7 Express lysY /I q (NEB). pDEST14-SpyCatcher2.1 S49C E77A (SpyDock), pDEST14-SpyCatcher2.1 S49C E77X variants, pDEST14-SpyCatcher2.1 E77A N-term Cys, pDEST14-SpyCatcher2.1 S55C E77A and pDEST14-SpyCatcher002-coiled coil fusions were transformed into chemically-competent E. coli C41 (DE3), a kind gift from Anthony Watts (University of Oxford). pET28a-αDR5-SpyTag was transformed into E. coli BL21 (DE3) RIPL containing a gene encoding phosphogluconolactonase, to degrade 6-phosphogluconolactone, which promotes protein gluconoylation . ..

    Article Title: Methionine Sulfoxide Reductases Are Essential for Virulence of Salmonella Typhimurium
    Article Snippet: .. Plasmids, designated pET28c::msrA and pET28c::msrB , respectively, were transformed into E. coli T7 lysY Express (NEB) for expression of the recombinant His-tagged proteins. .. Expression of MsrA and MsrB was induced by addition of 0.5 mM IPTG at an OD600 ∼0,8, and cells were grown for another 5 h. Bacteria were harvested by centrifugation (3000×g, 25 min, 4°C) and resuspended in binding buffer containing 50 mM NaH2 PO4 , 300 mM NaCl and 10 mM imidazole (pH 8.0 for MsrA, pH 8.5 for MsrB).

    Transformation Assay:

    Article Title: Ultrahigh specificity in a network of computationally designed protein-interaction pairs
    Article Snippet: .. The genes were ligated into a linearized pET21d plasmid using Nco I and Xho I restriction sites, transformed into T7 Express lysY/I q E.coli cells (NEB), and five colonies of each design were sequenced. ..

    Article Title: Spy Go purification of SpyTag-proteins using pseudo-SpyCatcher to access an oligomerization toolbox
    Article Snippet: .. Bacterial protein expression pET28a-SpyTag-MBP, pET28a-SpyTag002-MBP, and pET28a-SpyTag-mClover3 were transformed into chemically competent E. coli BL21 (DE3) RIPL (Agilent Technologies). pET28a-scPvuII-SpyTag was transformed into T7 Express lysY /I q (NEB). pDEST14-SpyCatcher2.1 S49C E77A (SpyDock), pDEST14-SpyCatcher2.1 S49C E77X variants, pDEST14-SpyCatcher2.1 E77A N-term Cys, pDEST14-SpyCatcher2.1 S55C E77A and pDEST14-SpyCatcher002-coiled coil fusions were transformed into chemically-competent E. coli C41 (DE3), a kind gift from Anthony Watts (University of Oxford). pET28a-αDR5-SpyTag was transformed into E. coli BL21 (DE3) RIPL containing a gene encoding phosphogluconolactonase, to degrade 6-phosphogluconolactone, which promotes protein gluconoylation . ..

    Article Title: Methionine Sulfoxide Reductases Are Essential for Virulence of Salmonella Typhimurium
    Article Snippet: .. Plasmids, designated pET28c::msrA and pET28c::msrB , respectively, were transformed into E. coli T7 lysY Express (NEB) for expression of the recombinant His-tagged proteins. .. Expression of MsrA and MsrB was induced by addition of 0.5 mM IPTG at an OD600 ∼0,8, and cells were grown for another 5 h. Bacteria were harvested by centrifugation (3000×g, 25 min, 4°C) and resuspended in binding buffer containing 50 mM NaH2 PO4 , 300 mM NaCl and 10 mM imidazole (pH 8.0 for MsrA, pH 8.5 for MsrB).

    Recombinant:

    Article Title: Biosimilars: the process is the product. The example of recombinant streptokinase
    Article Snippet: .. Recombinant streptokinase variants were expressed in T7 Express lysY E. coli (NEB, Herts, UK) and cells were lysed using B-PER Direct with enzymes (Thermo Fisher Scientific, Loughborough, UK). .. Recombinant SUMO star-streptokinase fusion proteins were purified by Ni-affinity and cleaved with SUMOstar Protease I (Lifesensors) over 4 h (assessed by SDS PAGE) at 30°C in the recommended buffer.

    Article Title: Methionine Sulfoxide Reductases Are Essential for Virulence of Salmonella Typhimurium
    Article Snippet: .. Plasmids, designated pET28c::msrA and pET28c::msrB , respectively, were transformed into E. coli T7 lysY Express (NEB) for expression of the recombinant His-tagged proteins. .. Expression of MsrA and MsrB was induced by addition of 0.5 mM IPTG at an OD600 ∼0,8, and cells were grown for another 5 h. Bacteria were harvested by centrifugation (3000×g, 25 min, 4°C) and resuspended in binding buffer containing 50 mM NaH2 PO4 , 300 mM NaCl and 10 mM imidazole (pH 8.0 for MsrA, pH 8.5 for MsrB).

    Plasmid Preparation:

    Article Title: Ultrahigh specificity in a network of computationally designed protein-interaction pairs
    Article Snippet: .. The genes were ligated into a linearized pET21d plasmid using Nco I and Xho I restriction sites, transformed into T7 Express lysY/I q E.coli cells (NEB), and five colonies of each design were sequenced. ..

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    New England Biolabs t7 express lysy i
    T7 Express Lysy I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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