e coli bl21 de3  (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
    Category:
    Competent Bacteria
    Size:
    1 ml
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    Structured Review

    New England Biolabs e coli bl21 de3
    BL21 DE3 Competent E coli
    BL21 DE3 Competent E coli 20x0 05 ml
    https://www.bioz.com/result/e coli bl21 de3/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    e coli bl21 de3 - by Bioz Stars, 2021-06
    99/100 stars

    Images

    1) Product Images from "Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum"

    Article Title: Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum

    Journal: Scientific Reports

    doi: 10.1038/s41598-021-86000-z

    ( A ) Time course of recombinant cellulase fermentation by E. coli BL21 (DE3) in LB (□) and modified M9NG media (♦) over 16 h of shake flask fermentation. Effect of ( B ) temperature, ( C ) pH and ( D ) agitation rate on recombinant cellulase fermentation by E. coli BL21 (DE3) determined by incubating at different fermentation temperature, pH and agitation rates respectively. Wet cell weight (♦), recombinant cellulase expression (□).
    Figure Legend Snippet: ( A ) Time course of recombinant cellulase fermentation by E. coli BL21 (DE3) in LB (□) and modified M9NG media (♦) over 16 h of shake flask fermentation. Effect of ( B ) temperature, ( C ) pH and ( D ) agitation rate on recombinant cellulase fermentation by E. coli BL21 (DE3) determined by incubating at different fermentation temperature, pH and agitation rates respectively. Wet cell weight (♦), recombinant cellulase expression (□).

    Techniques Used: Recombinant, Modification, Expressing

    2) Product Images from "Identification of Active Site Residues of the Siderophore Synthesis Enzyme PvdF and Evidence for Interaction of PvdF with a Substrate-Providing Enzyme"

    Article Title: Identification of Active Site Residues of the Siderophore Synthesis Enzyme PvdF and Evidence for Interaction of PvdF with a Substrate-Providing Enzyme

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms22042211

    Co-purification of PvdF and PvdA ( A ) PvdF and His 6 PvdA were expressed from pET-DUET-1 in E. coli BL21 DE3. Following purification by nickel affinity chromatography, proteins from bacteria containing the plasmids shown were visualised by SDS-PAGE. The identities of the bands in red boxes were confirmed as His 6 PvdA and PvdF by mass spectrometry ( Table S1 ). ( B ) PvdFHis 6 and PvdA were expressed separately in E. coli BL21 DE3 and cell lysates prepared. Nickel affinity chromatography was carried out on individual lysates (PvdFHis 6 ; PvdA) and following mixture of lysates (PvdFHis6 and PvdA). The eluates were analysed using SDS-PAGE. The positions of PvdFHis 6 and PvdA proteins are indicated.
    Figure Legend Snippet: Co-purification of PvdF and PvdA ( A ) PvdF and His 6 PvdA were expressed from pET-DUET-1 in E. coli BL21 DE3. Following purification by nickel affinity chromatography, proteins from bacteria containing the plasmids shown were visualised by SDS-PAGE. The identities of the bands in red boxes were confirmed as His 6 PvdA and PvdF by mass spectrometry ( Table S1 ). ( B ) PvdFHis 6 and PvdA were expressed separately in E. coli BL21 DE3 and cell lysates prepared. Nickel affinity chromatography was carried out on individual lysates (PvdFHis 6 ; PvdA) and following mixture of lysates (PvdFHis6 and PvdA). The eluates were analysed using SDS-PAGE. The positions of PvdFHis 6 and PvdA proteins are indicated.

    Techniques Used: Copurification, Positron Emission Tomography, Purification, Affinity Chromatography, SDS Page, Mass Spectrometry

    Related Articles

    Transformation Assay:

    Article Title: Identification of the agr Peptide of Listeria monocytogenes
    Article Snippet: 180 μl aliquots were distributed in 96 well microtiter plates (each condition in triplicate) and incubated at 30°C for 2 h. At this stage, 20 μl of diluted peptides were added to obtain the indicated final concentrations (5 nM–50 μM) and plates were incubated at 30°C in a Tecan Infinite M200 plate reader with hourly OD600 and luminescence intensity measurements. .. 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. ..

    Expressing:

    Article Title: Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization
    Article Snippet: Mutations within BsHPF were introduced by overlapping PCR. .. Escherichia coli BL21(DE3) cells (NEB) carrying the expression plasmid were grown in lysogeny broth (LB) medium supplemented with ampicillin (100 μg/ml) or kanamycin (50 μg/ml) and D(+)‐lactose‐monohydrate (12.5 g/l) for 16 h at 30°C under rigorous shaking (180 rpm). .. The cells were harvested (3,500 × g , 20 min, 4°C), resuspended in lysis buffer (20 mM HEPES‐KOH, pH 8.0, 20 mM KCl, 20 mM MgCl2 , 500 mM NaCl, 40 mM imidazole) and lysed using a M‐110L Microfluidizer (Microfluidics).

    Article Title: A Multiprotein DNA Translocation Complex Directs Intramycelial Plasmid Spreading during Streptomyces Conjugation
    Article Snippet: .. The resulting expression plasmid pGMT7-spdB2 was used to transform the different E. coli strains [BL21(DE3), BL21(DE3)/pLysS, Lemo21(DE3) (NEB)]. .. As a control, cells were also transformed with the empty expression plasmid pGM202T7.

    Article Title: Molecular characterization and Functional Analysis of the PilQ380-706: a Novel Secretin Domain in Pseudomonas aeruginosa
    Article Snippet: .. Bacterial strains, plasmids, and media Escherichia coli (E. coli ) strains Top10F and BL21 (DE3) were used as preservation and expression hosts. .. The P. aeruginosa laboratory strain PAO1 (that kindly provided by Dr. Abdi from Department of Microbiology, Faculty of Biological Sciences, Alzahra University, Tehran, Iran) were performed.

    Plasmid Preparation:

    Article Title: Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization
    Article Snippet: Mutations within BsHPF were introduced by overlapping PCR. .. Escherichia coli BL21(DE3) cells (NEB) carrying the expression plasmid were grown in lysogeny broth (LB) medium supplemented with ampicillin (100 μg/ml) or kanamycin (50 μg/ml) and D(+)‐lactose‐monohydrate (12.5 g/l) for 16 h at 30°C under rigorous shaking (180 rpm). .. The cells were harvested (3,500 × g , 20 min, 4°C), resuspended in lysis buffer (20 mM HEPES‐KOH, pH 8.0, 20 mM KCl, 20 mM MgCl2 , 500 mM NaCl, 40 mM imidazole) and lysed using a M‐110L Microfluidizer (Microfluidics).

    Article Title: A Multiprotein DNA Translocation Complex Directs Intramycelial Plasmid Spreading during Streptomyces Conjugation
    Article Snippet: .. The resulting expression plasmid pGMT7-spdB2 was used to transform the different E. coli strains [BL21(DE3), BL21(DE3)/pLysS, Lemo21(DE3) (NEB)]. .. As a control, cells were also transformed with the empty expression plasmid pGM202T7.

    Preserving:

    Article Title: Molecular characterization and Functional Analysis of the PilQ380-706: a Novel Secretin Domain in Pseudomonas aeruginosa
    Article Snippet: .. Bacterial strains, plasmids, and media Escherichia coli (E. coli ) strains Top10F and BL21 (DE3) were used as preservation and expression hosts. .. The P. aeruginosa laboratory strain PAO1 (that kindly provided by Dr. Abdi from Department of Microbiology, Faculty of Biological Sciences, Alzahra University, Tehran, Iran) were performed.

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    New England Biolabs e coli bl21 strains
    Functional validation of the predicted ARGs and structural investigation of conserved sites detected by HMD-ARG. a Left figure: A diagram showing the procedure of heterologous expression and functional analysis of the predicted ARGs from PA150567 in E. coli <t>BL21</t> host. Middle figure : Growth curves of E. coli hosts with expression of the predicted β -lactamases that inactivate β -lactam antibiotics in the presence of 2 μg/ml meropenem. Right figure : Growth curves of E. coli hosts with expression of the predicted acetyltransferases that inactivate aminoglycoside antibiotics in the presence of 4 μg/ml amikacin. b The HMD-ARG predicted conserved sites and the corresponding sequence logo from 319 to 393 in AXX01_04100. c After we mutated the conserved site (346) from T to N, the mutated protein’s (colored in red) local structure (predicted by RaptorX) changed significantly from the wild type (colored in light blue). Moreover, the binding affinity (predicted by AutoDock) between the mutated protein and the ligand (antibiotics) also reduced, as illustrated in the middle (wild type) and right (mutated protein) figures
    E Coli Bl21 Strains, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli bl21 strains/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
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    Functional validation of the predicted ARGs and structural investigation of conserved sites detected by HMD-ARG. a Left figure: A diagram showing the procedure of heterologous expression and functional analysis of the predicted ARGs from PA150567 in E. coli BL21 host. Middle figure : Growth curves of E. coli hosts with expression of the predicted β -lactamases that inactivate β -lactam antibiotics in the presence of 2 μg/ml meropenem. Right figure : Growth curves of E. coli hosts with expression of the predicted acetyltransferases that inactivate aminoglycoside antibiotics in the presence of 4 μg/ml amikacin. b The HMD-ARG predicted conserved sites and the corresponding sequence logo from 319 to 393 in AXX01_04100. c After we mutated the conserved site (346) from T to N, the mutated protein’s (colored in red) local structure (predicted by RaptorX) changed significantly from the wild type (colored in light blue). Moreover, the binding affinity (predicted by AutoDock) between the mutated protein and the ligand (antibiotics) also reduced, as illustrated in the middle (wild type) and right (mutated protein) figures

    Journal: Microbiome

    Article Title: HMD-ARG: hierarchical multi-task deep learning for annotating antibiotic resistance genes

    doi: 10.1186/s40168-021-01002-3

    Figure Lengend Snippet: Functional validation of the predicted ARGs and structural investigation of conserved sites detected by HMD-ARG. a Left figure: A diagram showing the procedure of heterologous expression and functional analysis of the predicted ARGs from PA150567 in E. coli BL21 host. Middle figure : Growth curves of E. coli hosts with expression of the predicted β -lactamases that inactivate β -lactam antibiotics in the presence of 2 μg/ml meropenem. Right figure : Growth curves of E. coli hosts with expression of the predicted acetyltransferases that inactivate aminoglycoside antibiotics in the presence of 4 μg/ml amikacin. b The HMD-ARG predicted conserved sites and the corresponding sequence logo from 319 to 393 in AXX01_04100. c After we mutated the conserved site (346) from T to N, the mutated protein’s (colored in red) local structure (predicted by RaptorX) changed significantly from the wild type (colored in light blue). Moreover, the binding affinity (predicted by AutoDock) between the mutated protein and the ligand (antibiotics) also reduced, as illustrated in the middle (wild type) and right (mutated protein) figures

    Article Snippet: Overnight culture of E. coli BL21 strains containing the plasmids for overexpression of the predicted genes were 1:100 diluted and grown in LB medium supplemented with kanamycin (20 μg/ml) and Isopropyl β-D-1-thiogalactopyranoside (IPTG) (0.5 mM).

    Techniques: Functional Assay, Expressing, Sequencing, Binding Assay

    Use of THP-1 TLR4-CD14 NF-κB-eGFP reporter cells for the detection of microbial contaminations in recombinant protein preparations. (A) THP-1 TLR4-CD14 NF-κB-eGFP reporter cells were incubated with the indicated serial dilutions of ultrapure LPS for 24 h. NF-κB-driven eGFP expression was assessed by flow cytometry. Bar graphs show geometric mean of fluorescence intensity (gMFI). eGFP expression of the parental THP-1 reporter cells treated with 300 ng/ml ultrapure LPS is shown for comparison (grey bar). (B) mRNA expression of TLR4, CD14 and MD2 was measured in parental and TLR4-CD14 THP-1 reporter cells by real-time qPCR. Data are presented as mean ± SEM of expression values normalized against the housekeeping gene GAPDH (n = 4). (C) Recombinant human split product C4dg produced in three different expression systems (HEK293-6E, standard E . coli BL21 and E . coli ClearColi BL21) was tested for TLR4-agonist contaminations using HEK293 hTLR4A-MD2-CD14 cells. Following 24 h of incubation the IL-8 content in the culture supernatants was measured by ELISA. (D) Parental and TLR4-CD14 THP-1 reporters were incubated with the protein preparations described in (C) and NF-κB-driven eGFP expression was assessed by flow cytometry 24 h later. Bar graphs show geometric mean of fluorescence intensity (gMFI). Mean and SE were calculated from duplicates of four independently performed experiments (n = 4) (E) Immature human moDCs were incubated with standard LPS, E . coli BL21 or E . coli ClearColi BL21 expressed C4dg protein at the indicated concentrations for 24 h or were left untreated. Expression of maturation markers CD83 and CD86 was assessed by flow cytometry. (F) E . coli ClearColi BL21-expressed C4dg protein was subjected to a single round of bulk chromatography using a polymyxin resin (see Material and Methods ). Samples before and after chromatography were tested using the THP-1 TLR4-CD14 reporters. Mean and SE were calculated from duplicates of four independently performed experiments (n = 4).

    Journal: PLoS ONE

    Article Title: A human monocytic NF-κB fluorescent reporter cell line for detection of microbial contaminants in biological samples

    doi: 10.1371/journal.pone.0178220

    Figure Lengend Snippet: Use of THP-1 TLR4-CD14 NF-κB-eGFP reporter cells for the detection of microbial contaminations in recombinant protein preparations. (A) THP-1 TLR4-CD14 NF-κB-eGFP reporter cells were incubated with the indicated serial dilutions of ultrapure LPS for 24 h. NF-κB-driven eGFP expression was assessed by flow cytometry. Bar graphs show geometric mean of fluorescence intensity (gMFI). eGFP expression of the parental THP-1 reporter cells treated with 300 ng/ml ultrapure LPS is shown for comparison (grey bar). (B) mRNA expression of TLR4, CD14 and MD2 was measured in parental and TLR4-CD14 THP-1 reporter cells by real-time qPCR. Data are presented as mean ± SEM of expression values normalized against the housekeeping gene GAPDH (n = 4). (C) Recombinant human split product C4dg produced in three different expression systems (HEK293-6E, standard E . coli BL21 and E . coli ClearColi BL21) was tested for TLR4-agonist contaminations using HEK293 hTLR4A-MD2-CD14 cells. Following 24 h of incubation the IL-8 content in the culture supernatants was measured by ELISA. (D) Parental and TLR4-CD14 THP-1 reporters were incubated with the protein preparations described in (C) and NF-κB-driven eGFP expression was assessed by flow cytometry 24 h later. Bar graphs show geometric mean of fluorescence intensity (gMFI). Mean and SE were calculated from duplicates of four independently performed experiments (n = 4) (E) Immature human moDCs were incubated with standard LPS, E . coli BL21 or E . coli ClearColi BL21 expressed C4dg protein at the indicated concentrations for 24 h or were left untreated. Expression of maturation markers CD83 and CD86 was assessed by flow cytometry. (F) E . coli ClearColi BL21-expressed C4dg protein was subjected to a single round of bulk chromatography using a polymyxin resin (see Material and Methods ). Samples before and after chromatography were tested using the THP-1 TLR4-CD14 reporters. Mean and SE were calculated from duplicates of four independently performed experiments (n = 4).

    Article Snippet: The electrocompetent E. coli protein expression strain ClearColi BL21 was purchased from Lucigen (Middleton, WI) and standard E. coli BL21 were obtained from New England Biolabs (Ipswich, MA).

    Techniques: Recombinant, Incubation, Expressing, Flow Cytometry, Cytometry, Fluorescence, Real-time Polymerase Chain Reaction, Produced, Enzyme-linked Immunosorbent Assay, Chromatography

    Sender plasmids expressed in Escherichia coli BL21. (A) The modular Sender vector allows facile cloning of any EcoRI , XbaI ] glyphs (top) and a scaled circular map (bottom). (B) Optical density (OD) readings for E . coli cultures expressing each of the Sender plasmids. (C) mCherry expression is shown as end-point RFP signal normalized to OD 600 after an 8 hour growth period.

    Journal: PLoS ONE

    Article Title: Characterization of diverse homoserine lactone synthases in Escherichia coli

    doi: 10.1371/journal.pone.0202294

    Figure Lengend Snippet: Sender plasmids expressed in Escherichia coli BL21. (A) The modular Sender vector allows facile cloning of any EcoRI , XbaI ] glyphs (top) and a scaled circular map (bottom). (B) Optical density (OD) readings for E . coli cultures expressing each of the Sender plasmids. (C) mCherry expression is shown as end-point RFP signal normalized to OD 600 after an 8 hour growth period.

    Article Snippet: Cultures of E . coli BL21 (New England Biolabs) transformed with Sender plasmids, a Receiver plasmid, a negative receiver plasmid, and a GFP positive plasmid were grown in 3 mL of LB with 5 ug/mL ampicillin for 16 hours at 37°C and shaking at 220 rpm.

    Techniques: Plasmid Preparation, Clone Assay, Expressing

    Levels of acyl-CoA-forming activity (from ADP formation) of SucCD BL21 , SucCD Am , and SucCD AboHis . Activity values were normalized to the activity with succinate. Each of the various organic acids was applied to the assay mixture at 10 mM. Activity was determined in duplicate experiments. Black error bars, standard deviations.

    Journal: Applied and Environmental Microbiology

    Article Title: Novel Characteristics of Succinate Coenzyme A (Succinate-CoA) Ligases: Conversion of Malate to Malyl-CoA and CoA-Thioester Formation of Succinate Analogues In Vitro

    doi: 10.1128/AEM.03075-13

    Figure Lengend Snippet: Levels of acyl-CoA-forming activity (from ADP formation) of SucCD BL21 , SucCD Am , and SucCD AboHis . Activity values were normalized to the activity with succinate. Each of the various organic acids was applied to the assay mixture at 10 mM. Activity was determined in duplicate experiments. Black error bars, standard deviations.

    Article Snippet: During the experiments, the best expression was obtained when the sucCD genes of A. mimigardefordensis DPN7T and E. coli BL21 were each applied in one bicistronic operon that included the strain-specific Shine-Dalgarno sequence upstream of sucC .

    Techniques: Activity Assay