escherichia coli strains  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    Name:
    BL21 Competent E coli
    Description:
    BL21 Competent E coli 20x0 05 ml
    Catalog Number:
    C2530H
    Price:
    204
    Category:
    Competent Bacteria
    Size:
    1 ml
    Buy from Supplier


    Structured Review

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

    Images

    Related Articles

    Expressing:

    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
    Article Snippet: Expression of the relevant genes sucC and sucD in about equimolar amounts in a successful purification protocol was observed to require 68 or 135 bp of the corresponding sucC upstream regions in the expression vector pBluescriptSK(−) for sucCD Am and sucCD BL21 , respectively. .. 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 . ..

    Article Title: A human monocytic NF-κB fluorescent reporter cell line for detection of microbial contaminants in biological samples
    Article Snippet: Bacterial protein expression A construct encoding human complement split product C4dg fused to a C-terminal 6xHIS Tag was cloned into the IPTG-inducible bacterial expression vector pET21a(+) (EMD Millipore, Billerica, MA). .. 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). .. Protein expression was performed in standard LB (for BL21) or LB-Miller (10 g/L NaCl, for ClearColi BL21).

    Sequencing:

    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
    Article Snippet: Expression of the relevant genes sucC and sucD in about equimolar amounts in a successful purification protocol was observed to require 68 or 135 bp of the corresponding sucC upstream regions in the expression vector pBluescriptSK(−) for sucCD Am and sucCD BL21 , respectively. .. 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 . ..

    Over Expression:

    Article Title: Amino-Terminal Processing of Helicobacter pylori Serine Protease HtrA: Role in Oligomerization and Activity Regulation
    Article Snippet: As control, E. coli BL21 without a plasmid exhibited no expression of HtrAHp or GST-tagged protein, respectively ( Figures ). .. Together, these findings confirmed the successful overexpression of HtrAHp variants in E. coli BL21, useful for further analysis of HtrA activity. .. As next, the above generated E. coli BL21 lysates were subjected to casein zymography to investigate an effect of the shortened amino-terminus of HtrAHp on the proteolytic activity.

    Article Title: HMD-ARG: hierarchical multi-task deep learning for annotating antibiotic resistance genes
    Article Snippet: After ligation using the Quick LigationTM Kit (NEB, USA) and verification by PCR and DNA sequencing (BGI, China), the resulting plasmids were transformed into E. coli BL21 for antibiotic sensitivity analysis. .. 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). .. After incubation at 37 °C with 220-rpm agitation for 90 min, bacterial cultures were transferred to a 24-well plate.

    Activity Assay:

    Article Title: Amino-Terminal Processing of Helicobacter pylori Serine Protease HtrA: Role in Oligomerization and Activity Regulation
    Article Snippet: As control, E. coli BL21 without a plasmid exhibited no expression of HtrAHp or GST-tagged protein, respectively ( Figures ). .. Together, these findings confirmed the successful overexpression of HtrAHp variants in E. coli BL21, useful for further analysis of HtrA activity. .. As next, the above generated E. coli BL21 lysates were subjected to casein zymography to investigate an effect of the shortened amino-terminus of HtrAHp on the proteolytic activity.

    Cell Culture:

    Article Title: Improve Protein Solubility and Activity based on Machine Learning Models
    Article Snippet: Plasmid construction All the plasmids used in this work were constructed by using GT DNA standard (Supplementary Table S7). .. Cell culture and SDS-PAGE analysis of protein solubility Each of constructed plasmid was introduced into E. coli BL21 (DE3) (C2530H, New England Biolabs) for SDS-PAGE analysis by using standard heat shock protocol. ..

    SDS Page:

    Article Title: Improve Protein Solubility and Activity based on Machine Learning Models
    Article Snippet: Plasmid construction All the plasmids used in this work were constructed by using GT DNA standard (Supplementary Table S7). .. Cell culture and SDS-PAGE analysis of protein solubility Each of constructed plasmid was introduced into E. coli BL21 (DE3) (C2530H, New England Biolabs) for SDS-PAGE analysis by using standard heat shock protocol. ..

    Solubility:

    Article Title: Improve Protein Solubility and Activity based on Machine Learning Models
    Article Snippet: Plasmid construction All the plasmids used in this work were constructed by using GT DNA standard (Supplementary Table S7). .. Cell culture and SDS-PAGE analysis of protein solubility Each of constructed plasmid was introduced into E. coli BL21 (DE3) (C2530H, New England Biolabs) for SDS-PAGE analysis by using standard heat shock protocol. ..

    Construct:

    Article Title: Improve Protein Solubility and Activity based on Machine Learning Models
    Article Snippet: Plasmid construction All the plasmids used in this work were constructed by using GT DNA standard (Supplementary Table S7). .. Cell culture and SDS-PAGE analysis of protein solubility Each of constructed plasmid was introduced into E. coli BL21 (DE3) (C2530H, New England Biolabs) for SDS-PAGE analysis by using standard heat shock protocol. ..

    Plasmid Preparation:

    Article Title: Improve Protein Solubility and Activity based on Machine Learning Models
    Article Snippet: Plasmid construction All the plasmids used in this work were constructed by using GT DNA standard (Supplementary Table S7). .. Cell culture and SDS-PAGE analysis of protein solubility Each of constructed plasmid was introduced into E. coli BL21 (DE3) (C2530H, New England Biolabs) for SDS-PAGE analysis by using standard heat shock protocol. ..

    Article Title: Characterization of diverse homoserine lactone synthases in Escherichia coli
    Article Snippet: Graphs and heat maps were generated in Microsoft Excel 2016. .. 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. .. Bacterial culture was subsequently spread onto LB agar supplemented with 5 ug/mL ampicillin with sterile disposable plastic micropipette tip, such that a central spot of Sender culture would evenly diffuse towards proximal Receiver and Control-EGFP positive control cultures.

    Staining:

    Article Title: Amino-Terminal Processing of Helicobacter pylori Serine Protease HtrA: Role in Oligomerization and Activity Regulation
    Article Snippet: To investigate the importance of the amino-terminus on the proteolytic activity of HtrAHp in more detail, wt HtrAHp , ΔN1 or ΔN2 were expressed as GST-tagged variants in E. coli strain BL21 (Supplementary Figure ). .. E. coli BL21 were induced for 4 h with IPTG and the resulting bacterial lysates were subjected to Coomassie staining, confirming that equal amounts of protein were present ( Figure ). .. HtrAHp wt missing only the signal peptide (ΔSP) revealed a strong overexpression of the fusion protein (p55 HtrAHp with GST-tag of ∼70 kDa) as detected by Coomassie-staining ( Figure , black asterisk).

    Transformation Assay:

    Article Title: Characterization of diverse homoserine lactone synthases in Escherichia coli
    Article Snippet: Graphs and heat maps were generated in Microsoft Excel 2016. .. 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. .. Bacterial culture was subsequently spread onto LB agar supplemented with 5 ug/mL ampicillin with sterile disposable plastic micropipette tip, such that a central spot of Sender culture would evenly diffuse towards proximal Receiver and Control-EGFP positive control cultures.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    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
    Price from $9.99 to $1999.99
    e coli bl21 strains - by Bioz Stars, 2021-06
    99/100 stars
      Buy from Supplier

    99
    New England Biolabs e coli dna
    Optimization of primers for real-time <t>DOP-PCR.</t> Amplification profiles of real-time DOP-PCR were obtained by using various degenerate primers. Serially diluted human placental <t>DNA</t> samples ranging from 80 fg to 80 ng and a no-template control (NTC) were amplified. The primers used were Tag-N6- ATGTGG (A), Tag-N6- CCGCCC (B), Tag-N6- ATTTCG (C), Tag-N4- ATGTGG (D), Tag-N8- ATGTGG (E), and a combination of Tag-N6- ATGTGG and Tag-N6- TGTTGC (F).
    E Coli Dna, 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 dna/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    e coli dna - by Bioz Stars, 2021-06
    99/100 stars
      Buy from Supplier

    Image Search Results


    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

    Small RNA binding ability of HcPro and its mutants. Electrophoretic mobility shift assay for wild-type (wt) HcPro and its mutants. A. Purified preparations of HcPro and mutant proteins on Coomassie-stained 12% SDS-PAGE purified from Escherichia coli BL21 cells. MBP-HcPro/mutants fusion protein (92.5 kDa) B. Electrophoretic mobility shift assay for HcPro and its mutants. Different concentrations (lane 2–8) of purified HcPro or its mutants were incubated with 30 pmol of synthetic double stranded small RNA (siRNA171) for 30 minutes at 25°C. Lane 1, 30 pmol of synthetic, double-stranded small RNAs (siRNA171) without any protein added; lane 9, 30 pmol of synthetic, double-stranded small RNAs (siRNA171) incubated with MBP for 30 minutes as control. C. Graphical representation of the RNA binding results for the wt HcPro and its mutants. % RNA retention (determined by band intensities) was plotted against protein:RNA molar ratios in the binding assays of HcPro and its mutants with double stranded siRNA171. The data are means ±SD of four repeat assays. The significance level of the data are shown by asterisks (* P

    Journal: PLoS ONE

    Article Title: Inhibition of the Host Proteasome Facilitates Papaya Ringspot Virus Accumulation and Proteosomal Catalytic Activity Is Modulated by Viral Factor HcPro

    doi: 10.1371/journal.pone.0052546

    Figure Lengend Snippet: Small RNA binding ability of HcPro and its mutants. Electrophoretic mobility shift assay for wild-type (wt) HcPro and its mutants. A. Purified preparations of HcPro and mutant proteins on Coomassie-stained 12% SDS-PAGE purified from Escherichia coli BL21 cells. MBP-HcPro/mutants fusion protein (92.5 kDa) B. Electrophoretic mobility shift assay for HcPro and its mutants. Different concentrations (lane 2–8) of purified HcPro or its mutants were incubated with 30 pmol of synthetic double stranded small RNA (siRNA171) for 30 minutes at 25°C. Lane 1, 30 pmol of synthetic, double-stranded small RNAs (siRNA171) without any protein added; lane 9, 30 pmol of synthetic, double-stranded small RNAs (siRNA171) incubated with MBP for 30 minutes as control. C. Graphical representation of the RNA binding results for the wt HcPro and its mutants. % RNA retention (determined by band intensities) was plotted against protein:RNA molar ratios in the binding assays of HcPro and its mutants with double stranded siRNA171. The data are means ±SD of four repeat assays. The significance level of the data are shown by asterisks (* P

    Article Snippet: Expression of PRSV HC-Pro and its Mutants in Bacteria To investigate the role of PRSV HcPro and its mutants in the RNA silencing pathway, the corresponding genes were ligated in the vector pMAL-c2X and expressed from a ‘tac’ promoter as a MBP-HcPro fusion protein in E. coli strain BL21 (New England Biolabs, Beverly, MA), as described .

    Techniques: RNA Binding Assay, Electrophoretic Mobility Shift Assay, Purification, Mutagenesis, Staining, SDS Page, Incubation, Binding Assay

    Optimization of primers for real-time DOP-PCR. Amplification profiles of real-time DOP-PCR were obtained by using various degenerate primers. Serially diluted human placental DNA samples ranging from 80 fg to 80 ng and a no-template control (NTC) were amplified. The primers used were Tag-N6- ATGTGG (A), Tag-N6- CCGCCC (B), Tag-N6- ATTTCG (C), Tag-N4- ATGTGG (D), Tag-N8- ATGTGG (E), and a combination of Tag-N6- ATGTGG and Tag-N6- TGTTGC (F).

    Journal: PLoS ONE

    Article Title: Quantification of Trace-Level DNA by Real-Time Whole Genome Amplification

    doi: 10.1371/journal.pone.0028661

    Figure Lengend Snippet: Optimization of primers for real-time DOP-PCR. Amplification profiles of real-time DOP-PCR were obtained by using various degenerate primers. Serially diluted human placental DNA samples ranging from 80 fg to 80 ng and a no-template control (NTC) were amplified. The primers used were Tag-N6- ATGTGG (A), Tag-N6- CCGCCC (B), Tag-N6- ATTTCG (C), Tag-N4- ATGTGG (D), Tag-N8- ATGTGG (E), and a combination of Tag-N6- ATGTGG and Tag-N6- TGTTGC (F).

    Article Snippet: DNA samples Genomic DNAs from four different species were used as templates for PCR analysis: human placental DNA (HPD, Sigma), calf thymus DNA (CTD, Invitrogen), E. coli DNA (extracted from BL21 strain), and lambda phage DNA (NEB).

    Techniques: Degenerate Oligonucleotide–primed Polymerase Chain Reaction, Amplification

    Application of the real-time DOP-PCR to diverse DNA species. Amplification profiles and their standard curves were obtained from human placental DNA (HPD; A), calf thymus DNA (CTD; B), E. coli DNA (C), and lambda phage DNA (D). Standard DNA samples from 80 fg to 80 ng and a no-template control were amplified. Six independent experiments each comprising triplicate reactions were performed, and typical results of one experiment are presented. Data for 80 ng and NTC were omitted for the plotting of standard curves.

    Journal: PLoS ONE

    Article Title: Quantification of Trace-Level DNA by Real-Time Whole Genome Amplification

    doi: 10.1371/journal.pone.0028661

    Figure Lengend Snippet: Application of the real-time DOP-PCR to diverse DNA species. Amplification profiles and their standard curves were obtained from human placental DNA (HPD; A), calf thymus DNA (CTD; B), E. coli DNA (C), and lambda phage DNA (D). Standard DNA samples from 80 fg to 80 ng and a no-template control were amplified. Six independent experiments each comprising triplicate reactions were performed, and typical results of one experiment are presented. Data for 80 ng and NTC were omitted for the plotting of standard curves.

    Article Snippet: DNA samples Genomic DNAs from four different species were used as templates for PCR analysis: human placental DNA (HPD, Sigma), calf thymus DNA (CTD, Invitrogen), E. coli DNA (extracted from BL21 strain), and lambda phage DNA (NEB).

    Techniques: Degenerate Oligonucleotide–primed Polymerase Chain Reaction, Amplification