Structured Review

Millipore coli bl21
Proteomic analysis and identification of the esterase ( i . e . ALC24_4107) involved in the aliphatic polyester degradation of Alcanivorax sp. 24. A. PCA of the exoproteomes produced by Alcanivorax sp. 24 when grown in the presence of different substrates including the three aliphatic polyesters PES, PHB and PHBV as well as BHET and succinate. B. Relative abundance of the esterase ALC24_4107 in each one of the exoproteomes of Alcanivorax sp. 24 when grown in the presence of different substrates. Error bars indicate the standard deviation of three biological replicates. C. Protein domains and genomic context of ALC24_4107. D. Hydrolytic activity of the heterologously overexpressed ALC24_4107 in E . coli <t>BL21</t> assessed by a clear zone hydrolysis test on five different aliphatic polyesters. Halos surround 5 mm‐diameter wells. [Color figure can be viewed at http://wileyonlinelibrary.com ]
Coli Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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coli bl21 - by Bioz Stars, 2022-08
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1) Product Images from "Beyond oil degradation: enzymatic potential of Alcanivorax to degrade natural and synthetic polyesters"

Article Title: Beyond oil degradation: enzymatic potential of Alcanivorax to degrade natural and synthetic polyesters

Journal: Environmental Microbiology

doi: 10.1111/1462-2920.14947

Proteomic analysis and identification of the esterase ( i . e . ALC24_4107) involved in the aliphatic polyester degradation of Alcanivorax sp. 24. A. PCA of the exoproteomes produced by Alcanivorax sp. 24 when grown in the presence of different substrates including the three aliphatic polyesters PES, PHB and PHBV as well as BHET and succinate. B. Relative abundance of the esterase ALC24_4107 in each one of the exoproteomes of Alcanivorax sp. 24 when grown in the presence of different substrates. Error bars indicate the standard deviation of three biological replicates. C. Protein domains and genomic context of ALC24_4107. D. Hydrolytic activity of the heterologously overexpressed ALC24_4107 in E . coli BL21 assessed by a clear zone hydrolysis test on five different aliphatic polyesters. Halos surround 5 mm‐diameter wells. [Color figure can be viewed at http://wileyonlinelibrary.com ]
Figure Legend Snippet: Proteomic analysis and identification of the esterase ( i . e . ALC24_4107) involved in the aliphatic polyester degradation of Alcanivorax sp. 24. A. PCA of the exoproteomes produced by Alcanivorax sp. 24 when grown in the presence of different substrates including the three aliphatic polyesters PES, PHB and PHBV as well as BHET and succinate. B. Relative abundance of the esterase ALC24_4107 in each one of the exoproteomes of Alcanivorax sp. 24 when grown in the presence of different substrates. Error bars indicate the standard deviation of three biological replicates. C. Protein domains and genomic context of ALC24_4107. D. Hydrolytic activity of the heterologously overexpressed ALC24_4107 in E . coli BL21 assessed by a clear zone hydrolysis test on five different aliphatic polyesters. Halos surround 5 mm‐diameter wells. [Color figure can be viewed at http://wileyonlinelibrary.com ]

Techniques Used: Produced, Standard Deviation, Activity Assay

2) Product Images from "High-throughput mapping of the phage resistance landscape in E. coli"

Article Title: High-throughput mapping of the phage resistance landscape in E. coli

Journal: PLoS Biology

doi: 10.1371/journal.pbio.3000877

Genome-wide screens in E . coli BL21 strain. (A) Heatmap of BL21 LOF RB-TnSeq data for 12 dsDNA phages at a single MOI, and selected genes with high-confidence fitness benefits are shown. (B) Heatmap of GOF BL21 Dub-seq data for 12 dsDNA phages with high-confidence fitness benefit. Fitness scores of ≥4 in at least one phage assay are shown. These assays were performed in planktonic culture. Yellow stars indicate these data points are in agreement with RB-TnSeq, CRISPRi, and Dub-seq data for E . coli K-12. The underlying data for this figure can be found in S1 Data . CRISPRi, CRISPR interference; dsDNA, double-stranded DNA; Dub-seq, dual-barcoded shotgun expression library sequencing; GOF, gain-of-function; LOF, loss-of-function; MOI, multiplicity of infection; RB-TnSeq, random barcode transposon site sequencing.
Figure Legend Snippet: Genome-wide screens in E . coli BL21 strain. (A) Heatmap of BL21 LOF RB-TnSeq data for 12 dsDNA phages at a single MOI, and selected genes with high-confidence fitness benefits are shown. (B) Heatmap of GOF BL21 Dub-seq data for 12 dsDNA phages with high-confidence fitness benefit. Fitness scores of ≥4 in at least one phage assay are shown. These assays were performed in planktonic culture. Yellow stars indicate these data points are in agreement with RB-TnSeq, CRISPRi, and Dub-seq data for E . coli K-12. The underlying data for this figure can be found in S1 Data . CRISPRi, CRISPR interference; dsDNA, double-stranded DNA; Dub-seq, dual-barcoded shotgun expression library sequencing; GOF, gain-of-function; LOF, loss-of-function; MOI, multiplicity of infection; RB-TnSeq, random barcode transposon site sequencing.

Techniques Used: Genome Wide, CRISPR, Expressing, Sequencing, Infection

Overview of high-throughput genome-wide screens. We used barcoded LOF technologies (RB-TnSeq and CRISPRi) and a GOF technology (Dub-seq) in E . coli K-12 (BW25113 and MG1655) to screen for host factors important in phage infection and resistance. In E . coli BL21, we performed RB-TnSeq and Dub-seq (but not CRISPRi). We sourced 14 diverse E . coli phages with dsDNA genomes, belonging to Myoviridae, Podoviridae, and Siphoviridae families, and performed pooled fitness screens in both planktonic and solid agar formats. Disruption or overexpression of certain genes provide fitness to host in the presence of phages, and we monitor these changes by quantifying the abundance of the DNA barcode or sgRNA associated with each strain. The individual strain abundances are then converted to gene fitness scores (normalized log2 change in the abundance of mutants in that gene). CRISPRi, CRISPR interference; dsDNA, double-stranded DNA; Dub-seq, dual-barcoded shotgun expression library sequencing; GOF, gain-of-function; LOF, loss-of-function; MOI, multiplicity of infection; RB-TnSeq, random barcode transposon site sequencing; sgRNA, single-guide RNA.
Figure Legend Snippet: Overview of high-throughput genome-wide screens. We used barcoded LOF technologies (RB-TnSeq and CRISPRi) and a GOF technology (Dub-seq) in E . coli K-12 (BW25113 and MG1655) to screen for host factors important in phage infection and resistance. In E . coli BL21, we performed RB-TnSeq and Dub-seq (but not CRISPRi). We sourced 14 diverse E . coli phages with dsDNA genomes, belonging to Myoviridae, Podoviridae, and Siphoviridae families, and performed pooled fitness screens in both planktonic and solid agar formats. Disruption or overexpression of certain genes provide fitness to host in the presence of phages, and we monitor these changes by quantifying the abundance of the DNA barcode or sgRNA associated with each strain. The individual strain abundances are then converted to gene fitness scores (normalized log2 change in the abundance of mutants in that gene). CRISPRi, CRISPR interference; dsDNA, double-stranded DNA; Dub-seq, dual-barcoded shotgun expression library sequencing; GOF, gain-of-function; LOF, loss-of-function; MOI, multiplicity of infection; RB-TnSeq, random barcode transposon site sequencing; sgRNA, single-guide RNA.

Techniques Used: High Throughput Screening Assay, Genome Wide, Infection, Over Expression, CRISPR, Expressing, Sequencing

3) Product Images from "Domain III of Bacillus thuringiensis Cry1Ie Toxin Plays an Important Role in Binding to Peritrophic Membrane of Asian Corn Borer"

Article Title: Domain III of Bacillus thuringiensis Cry1Ie Toxin Plays an Important Role in Binding to Peritrophic Membrane of Asian Corn Borer

Journal: PLoS ONE

doi: 10.1371/journal.pone.0136430

Expression and purification of IE648 and individual domains of Cry1Ie in E . coli BL21/DE3. A, B and C: Induced expression of domains I, II and III, respectively. Lane M, Protein molecular marker. Lane 1 and 2, supernatant and pellet of bacteria after ultrasonication. Bands of the expected size of 34.6 kDa for domain I, 27.3 kDa for domain II and 27.9 kDa for domain III were present in the pellet fraction. D: SDS-PAGE analysis of purified IE648. Lane M, Protein molecular marker. Lane 1, Purified IE648. E: SDS-PAGE analysis of purified domain I. Lane M, Protein molecular marker. Lane 1, Purified domain I. F: Purification of domain II by Ni-NTA affinity chromatography. Lane M, Protein molecular marker. Lane 1, Inclusion bodies solubilized by using solubilization solutions of Inclusion Body Solubilization and Refolding Kit. Lane 2, Proteins passed through Ni-NTA agarose. Lane 3, Proteins washed by Na 2 CO 3 buffer (pH 10.2). G: Analysis of purification of domain III by Ni-NTA affinity chromatography. Lane M, Protein molecular marker. Lane 1, Inclusion bodies solubilized by Na 2 CO 3 (pH 10.2). Lane 2, Proteins passed through Ni-NTA agarose. Lane 3, Proteins washed by Na 2 CO 3 buffer (pH 10.2). Lane 4~7, Proteins eluted by 20 mM, 50 mM, 100 mM and 150 mM imidazole, respectively.
Figure Legend Snippet: Expression and purification of IE648 and individual domains of Cry1Ie in E . coli BL21/DE3. A, B and C: Induced expression of domains I, II and III, respectively. Lane M, Protein molecular marker. Lane 1 and 2, supernatant and pellet of bacteria after ultrasonication. Bands of the expected size of 34.6 kDa for domain I, 27.3 kDa for domain II and 27.9 kDa for domain III were present in the pellet fraction. D: SDS-PAGE analysis of purified IE648. Lane M, Protein molecular marker. Lane 1, Purified IE648. E: SDS-PAGE analysis of purified domain I. Lane M, Protein molecular marker. Lane 1, Purified domain I. F: Purification of domain II by Ni-NTA affinity chromatography. Lane M, Protein molecular marker. Lane 1, Inclusion bodies solubilized by using solubilization solutions of Inclusion Body Solubilization and Refolding Kit. Lane 2, Proteins passed through Ni-NTA agarose. Lane 3, Proteins washed by Na 2 CO 3 buffer (pH 10.2). G: Analysis of purification of domain III by Ni-NTA affinity chromatography. Lane M, Protein molecular marker. Lane 1, Inclusion bodies solubilized by Na 2 CO 3 (pH 10.2). Lane 2, Proteins passed through Ni-NTA agarose. Lane 3, Proteins washed by Na 2 CO 3 buffer (pH 10.2). Lane 4~7, Proteins eluted by 20 mM, 50 mM, 100 mM and 150 mM imidazole, respectively.

Techniques Used: Expressing, Purification, Marker, SDS Page, Affinity Chromatography

4) Product Images from "An Endolysin LysSE24 by Bacteriophage LPSE1 Confers Specific Bactericidal Activity against Multidrug-Resistant Salmonella Strains"

Article Title: An Endolysin LysSE24 by Bacteriophage LPSE1 Confers Specific Bactericidal Activity against Multidrug-Resistant Salmonella Strains

Journal: Microorganisms

doi: 10.3390/microorganisms8050737

SDS-PAGE analysis of the endolysin LysSE24. ( A ) Lane 1, protein markers; Lane 2, non-induced E. coli BL21 culture (negative control); Lane 3, native protein extract (NPE) from E. coli BL21 induced for 16 h at 16 °C; Lane 4, NPE from E. coli BL21 induced for 4 h at 30 °C; Lane 5, NPE from E. coli BL21 induced for 4 h at 37 °C; Lane 6, denatured protein extract (DPE) from E. coli BL21 induced for 16 h at 16 °C; Lane 7, DPE from E. coli BL21 induced for 4 h at 30 °C; Lane 8, DPE from E. coli BL21 induced for 4 h at 37 °C; Lane 9, non-induced E. coli C41 culture (negative control); Lane 10, NPE from E. coli C41 induced for 16 h at 16 °C; Lane 11, NPE from E. coli C41 induced for 4 h at 30 °C; Lane 12, NPE from E. coli C41 induced for 4 h at 37 °C; Lane 13, DPE from E. coli C41 induced for 16 h at 16 °C; Lane 14, DPE from E. coli C41 induced for 4 h at 30 °C; Lane 15, DPE from E. coli C41 induced for 4 h at 37 °C; the arrow denotes the target protein; ( B ) Lane 1, protein markers; Lane 2, purified endolysin LysSE24 from E. coli BL21 after induction for 16 h at 16 °C; the arrow denotes the target protein.
Figure Legend Snippet: SDS-PAGE analysis of the endolysin LysSE24. ( A ) Lane 1, protein markers; Lane 2, non-induced E. coli BL21 culture (negative control); Lane 3, native protein extract (NPE) from E. coli BL21 induced for 16 h at 16 °C; Lane 4, NPE from E. coli BL21 induced for 4 h at 30 °C; Lane 5, NPE from E. coli BL21 induced for 4 h at 37 °C; Lane 6, denatured protein extract (DPE) from E. coli BL21 induced for 16 h at 16 °C; Lane 7, DPE from E. coli BL21 induced for 4 h at 30 °C; Lane 8, DPE from E. coli BL21 induced for 4 h at 37 °C; Lane 9, non-induced E. coli C41 culture (negative control); Lane 10, NPE from E. coli C41 induced for 16 h at 16 °C; Lane 11, NPE from E. coli C41 induced for 4 h at 30 °C; Lane 12, NPE from E. coli C41 induced for 4 h at 37 °C; Lane 13, DPE from E. coli C41 induced for 16 h at 16 °C; Lane 14, DPE from E. coli C41 induced for 4 h at 30 °C; Lane 15, DPE from E. coli C41 induced for 4 h at 37 °C; the arrow denotes the target protein; ( B ) Lane 1, protein markers; Lane 2, purified endolysin LysSE24 from E. coli BL21 after induction for 16 h at 16 °C; the arrow denotes the target protein.

Techniques Used: SDS Page, Negative Control, Purification

5) Product Images from "Fluorescence Resonance Energy Transfer Assay for High-Throughput Screening of ADAMTS1 Inhibitors "

Article Title: Fluorescence Resonance Energy Transfer Assay for High-Throughput Screening of ADAMTS1 Inhibitors

Journal: Molecules

doi: 10.3390/molecules161210709

Expression analysis of recombinant ADAMTS1 in E. coli BL21 (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.
Figure Legend Snippet: Expression analysis of recombinant ADAMTS1 in E. coli BL21 (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.

Techniques Used: Expressing, Recombinant, SDS Page, Purification, Staining, Western Blot

6) Product Images from "Characterization of Mycoplasma gallisepticum pyruvate dehydrogenase alpha and beta subunits and their roles in cytoadherence"

Article Title: Characterization of Mycoplasma gallisepticum pyruvate dehydrogenase alpha and beta subunits and their roles in cytoadherence

Journal: PLoS ONE

doi: 10.1371/journal.pone.0208745

Surface display assays. Adhesion and inhibition of E . coli BL21 (DE3) containing pIGN-PDHA or pIGN-PDHB to DF-1 cells. Adhesion of E . coli BL21 (DE3) containing pIGN-PDHA (A) or pIGN-PDHB (D) to DF-1 cells. Adhesion of E . coli BL21 (DE3) containing pIGN-PDHA to DF-1 cells inhibited by mouse anti-rPDHA (B) but not non-immunized mouse serum (C). Adhesion of E . coli BL21 (DE3) containing pIGN-PDHB to DF-1 cells inhibited by mouse anti-rPDHB (E) but not non-immunized mouse serum (F). PIGN (G) was used as the negative control. Column GFP, recombinant E . coli cells containing GFP fusion protein. Column Dil, cell membrane labelled by DilC18(3). Column DAPI, cell nuclei labelled by DAPI; Column merge, merge of fluorescent images.
Figure Legend Snippet: Surface display assays. Adhesion and inhibition of E . coli BL21 (DE3) containing pIGN-PDHA or pIGN-PDHB to DF-1 cells. Adhesion of E . coli BL21 (DE3) containing pIGN-PDHA (A) or pIGN-PDHB (D) to DF-1 cells. Adhesion of E . coli BL21 (DE3) containing pIGN-PDHA to DF-1 cells inhibited by mouse anti-rPDHA (B) but not non-immunized mouse serum (C). Adhesion of E . coli BL21 (DE3) containing pIGN-PDHB to DF-1 cells inhibited by mouse anti-rPDHB (E) but not non-immunized mouse serum (F). PIGN (G) was used as the negative control. Column GFP, recombinant E . coli cells containing GFP fusion protein. Column Dil, cell membrane labelled by DilC18(3). Column DAPI, cell nuclei labelled by DAPI; Column merge, merge of fluorescent images.

Techniques Used: Inhibition, Negative Control, Recombinant

Cloning and expression of the M . gallisepticum pdhA and pdhB genes. (A) Results of PCR amplification. Lane M: DNA marker; Lane 1: pdhA gene of M . gallisepticum ; Lane 2: pdhB gene of M . gallisepticum . (B) SDS-PAGE of rPDHA and rPDHB. Lane M: Prestained protein marker; Lane 1: E . coli BL21 (DE3) transformed with pET-28a (+) induced by IPTG (negative control); Lane 2: E . coli BL21 (DE3) containing recombinant pET28a-PDHA induced by IPTG; Lane 3: E . coli BL21 (DE3) containing recombinant pET28a-PDHB induced by IPTG; Lane 4: Purified rPDHA protein (42 kDa); Lane 5: Purified rPDHB protein (38 kDa).
Figure Legend Snippet: Cloning and expression of the M . gallisepticum pdhA and pdhB genes. (A) Results of PCR amplification. Lane M: DNA marker; Lane 1: pdhA gene of M . gallisepticum ; Lane 2: pdhB gene of M . gallisepticum . (B) SDS-PAGE of rPDHA and rPDHB. Lane M: Prestained protein marker; Lane 1: E . coli BL21 (DE3) transformed with pET-28a (+) induced by IPTG (negative control); Lane 2: E . coli BL21 (DE3) containing recombinant pET28a-PDHA induced by IPTG; Lane 3: E . coli BL21 (DE3) containing recombinant pET28a-PDHB induced by IPTG; Lane 4: Purified rPDHA protein (42 kDa); Lane 5: Purified rPDHB protein (38 kDa).

Techniques Used: Clone Assay, Expressing, Polymerase Chain Reaction, Amplification, Marker, SDS Page, Transformation Assay, Positron Emission Tomography, Negative Control, Recombinant, Purification

7) Product Images from "Screening, Expression, Purification and Functional Characterization of Novel Antimicrobial Peptide Genes from Hermetia illucens (L.)"

Article Title: Screening, Expression, Purification and Functional Characterization of Novel Antimicrobial Peptide Genes from Hermetia illucens (L.)

Journal: PLoS ONE

doi: 10.1371/journal.pone.0169582

Expression of the stomoxynZH1 gene in E . coli and purification of Trx- stomoxynZH1. 12% SDS-PAGE analysis of the recombinant protein expressed in BL21 (DE3) (A). M: protein standard molecular weight marker, lanes 1 and 2 are samples collected before induction with IPTG, lanes 3 and 4 are samples collected after induction with IPTG. Chromatography curve recorded by the Nanjing Puyang Scientific Instrument Research Institution Purifier system (B). Arrows 1, 2 and 3 are the fractions of Trx-stomoxynZH1 purified by the nickel ion metal chelating affinity chromatography. SDS-PAGE (12%) analysis of Trx-stomoxynZH1 purification (C). M, protein marker; lanes 1–3 are the purified fractions of Trx-stomoxynZH1.
Figure Legend Snippet: Expression of the stomoxynZH1 gene in E . coli and purification of Trx- stomoxynZH1. 12% SDS-PAGE analysis of the recombinant protein expressed in BL21 (DE3) (A). M: protein standard molecular weight marker, lanes 1 and 2 are samples collected before induction with IPTG, lanes 3 and 4 are samples collected after induction with IPTG. Chromatography curve recorded by the Nanjing Puyang Scientific Instrument Research Institution Purifier system (B). Arrows 1, 2 and 3 are the fractions of Trx-stomoxynZH1 purified by the nickel ion metal chelating affinity chromatography. SDS-PAGE (12%) analysis of Trx-stomoxynZH1 purification (C). M, protein marker; lanes 1–3 are the purified fractions of Trx-stomoxynZH1.

Techniques Used: Expressing, Purification, SDS Page, Recombinant, Molecular Weight, Marker, Chromatography, Affinity Chromatography

8) Product Images from "Characterization of Mycoplasma gallisepticum pyruvate dehydrogenase alpha and beta subunits and their roles in cytoadherence"

Article Title: Characterization of Mycoplasma gallisepticum pyruvate dehydrogenase alpha and beta subunits and their roles in cytoadherence

Journal: PLoS ONE

doi: 10.1371/journal.pone.0208745

Cloning and expression of the M . gallisepticum pdhA and pdhB genes. (A) Results of PCR amplification. Lane M: DNA marker; Lane 1: pdhA gene of M . gallisepticum ; Lane 2: pdhB gene of M . gallisepticum . (B) SDS-PAGE of rPDHA and rPDHB. Lane M: Prestained protein marker; Lane 1: E . coli BL21 (DE3) transformed with pET-28a (+) induced by IPTG (negative control); Lane 2: E . coli BL21 (DE3) containing recombinant pET28a-PDHA induced by IPTG; Lane 3: E . coli BL21 (DE3) containing recombinant pET28a-PDHB induced by IPTG; Lane 4: Purified rPDHA protein (42 kDa); Lane 5: Purified rPDHB protein (38 kDa).
Figure Legend Snippet: Cloning and expression of the M . gallisepticum pdhA and pdhB genes. (A) Results of PCR amplification. Lane M: DNA marker; Lane 1: pdhA gene of M . gallisepticum ; Lane 2: pdhB gene of M . gallisepticum . (B) SDS-PAGE of rPDHA and rPDHB. Lane M: Prestained protein marker; Lane 1: E . coli BL21 (DE3) transformed with pET-28a (+) induced by IPTG (negative control); Lane 2: E . coli BL21 (DE3) containing recombinant pET28a-PDHA induced by IPTG; Lane 3: E . coli BL21 (DE3) containing recombinant pET28a-PDHB induced by IPTG; Lane 4: Purified rPDHA protein (42 kDa); Lane 5: Purified rPDHB protein (38 kDa).

Techniques Used: Clone Assay, Expressing, Polymerase Chain Reaction, Amplification, Marker, SDS Page, Transformation Assay, Positron Emission Tomography, Negative Control, Recombinant, Purification

9) Product Images from "Properties of a Newly Identified Esterase from Bacillus sp. K91 and Its Novel Function in Diisobutyl Phthalate Degradation"

Article Title: Properties of a Newly Identified Esterase from Bacillus sp. K91 and Its Novel Function in Diisobutyl Phthalate Degradation

Journal: PLoS ONE

doi: 10.1371/journal.pone.0119216

Analysis of the protein expressed in E . coli BL21 cells following purification on a 12% SDS-PAGE. Lane M, protein molecular marker; Lane 1, before induction with 0.7 mM IPTG; Lane 2, after induction with IPTG and grown at 20°C for 20 h; and Lane 3, purified recombinant CarEW (∼53.76 kDa).
Figure Legend Snippet: Analysis of the protein expressed in E . coli BL21 cells following purification on a 12% SDS-PAGE. Lane M, protein molecular marker; Lane 1, before induction with 0.7 mM IPTG; Lane 2, after induction with IPTG and grown at 20°C for 20 h; and Lane 3, purified recombinant CarEW (∼53.76 kDa).

Techniques Used: Purification, SDS Page, Marker, Recombinant

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    Millipore e coli bl21
    Heterologus expression of AmGAS . (A) sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the numbers indicate—1: protein marker, 2: induced recombinant strain containing pET-26b (+) plus AmGAS gene after 6 h, 3, after 4 h; 4, after 2 h; 5, non-induced and 6, E. coli <t>BL21</t> (DE3) without plasmid, and (B) western blotting, the numbers denote—1, non-induced recombinant strain containing pET-26b (+) plus AmGAS gene; 2, induced protein after 2 h; 3, after 4 h; 4, after 6 h and 5, protein marker. Arrows show the band that belongs to the recombinant protein of AmGAS.
    E Coli Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli bl21/product/Millipore
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Heterologus expression of AmGAS . (A) sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the numbers indicate—1: protein marker, 2: induced recombinant strain containing pET-26b (+) plus AmGAS gene after 6 h, 3, after 4 h; 4, after 2 h; 5, non-induced and 6, E. coli BL21 (DE3) without plasmid, and (B) western blotting, the numbers denote—1, non-induced recombinant strain containing pET-26b (+) plus AmGAS gene; 2, induced protein after 2 h; 3, after 4 h; 4, after 6 h and 5, protein marker. Arrows show the band that belongs to the recombinant protein of AmGAS.

    Journal: Frontiers in Plant Science

    Article Title: Germacrene A synthase in yarrow (Achillea millefolium) is an enzyme with mixed substrate specificity: gene cloning, functional characterization and expression analysis

    doi: 10.3389/fpls.2015.00111

    Figure Lengend Snippet: Heterologus expression of AmGAS . (A) sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the numbers indicate—1: protein marker, 2: induced recombinant strain containing pET-26b (+) plus AmGAS gene after 6 h, 3, after 4 h; 4, after 2 h; 5, non-induced and 6, E. coli BL21 (DE3) without plasmid, and (B) western blotting, the numbers denote—1, non-induced recombinant strain containing pET-26b (+) plus AmGAS gene; 2, induced protein after 2 h; 3, after 4 h; 4, after 6 h and 5, protein marker. Arrows show the band that belongs to the recombinant protein of AmGAS.

    Article Snippet: The digested fragments were gel-purified and then AmGAS fragment was cloned into pET-26b (+) expression vector and transformed to E. coli BL21 (Novagen) using the calcium chloride transformation method (Sambrook and Russell, ).

    Techniques: Expressing, Polyacrylamide Gel Electrophoresis, SDS Page, Marker, Recombinant, Positron Emission Tomography, Plasmid Preparation, Western Blot

    Proteomic analysis and identification of the esterase ( i . e . ALC24_4107) involved in the aliphatic polyester degradation of Alcanivorax sp. 24. A. PCA of the exoproteomes produced by Alcanivorax sp. 24 when grown in the presence of different substrates including the three aliphatic polyesters PES, PHB and PHBV as well as BHET and succinate. B. Relative abundance of the esterase ALC24_4107 in each one of the exoproteomes of Alcanivorax sp. 24 when grown in the presence of different substrates. Error bars indicate the standard deviation of three biological replicates. C. Protein domains and genomic context of ALC24_4107. D. Hydrolytic activity of the heterologously overexpressed ALC24_4107 in E . coli BL21 assessed by a clear zone hydrolysis test on five different aliphatic polyesters. Halos surround 5 mm‐diameter wells. [Color figure can be viewed at http://wileyonlinelibrary.com ]

    Journal: Environmental Microbiology

    Article Title: Beyond oil degradation: enzymatic potential of Alcanivorax to degrade natural and synthetic polyesters

    doi: 10.1111/1462-2920.14947

    Figure Lengend Snippet: Proteomic analysis and identification of the esterase ( i . e . ALC24_4107) involved in the aliphatic polyester degradation of Alcanivorax sp. 24. A. PCA of the exoproteomes produced by Alcanivorax sp. 24 when grown in the presence of different substrates including the three aliphatic polyesters PES, PHB and PHBV as well as BHET and succinate. B. Relative abundance of the esterase ALC24_4107 in each one of the exoproteomes of Alcanivorax sp. 24 when grown in the presence of different substrates. Error bars indicate the standard deviation of three biological replicates. C. Protein domains and genomic context of ALC24_4107. D. Hydrolytic activity of the heterologously overexpressed ALC24_4107 in E . coli BL21 assessed by a clear zone hydrolysis test on five different aliphatic polyesters. Halos surround 5 mm‐diameter wells. [Color figure can be viewed at http://wileyonlinelibrary.com ]

    Article Snippet: E . coli BL21 was grown using LB broth (Sigma‐Aldrich®).

    Techniques: Produced, Standard Deviation, Activity Assay

    SDS-PAGE analysis of recombinant Gal308 from supernatant of E. coli BL21 (DE3) cell lysates and purified Gal308 by affinity chromatography. Lanes: M, standard protein molecular mass markers (sizes in kilodaltons are indicated on the left); 1, recombinant Gal308 from supernatant of E. coli BL21 (DE3) cell lysates; 2, recombinant Gal308 purified by His•Bind® Purification Kit. The sizes in kilodaltons of protein marker were listed as follows: porcine heart myosin (200,000 Da), E. coli β-galactosidase (116,000 Da), rabbit muscle phosphorylase B (97,200 Da), bovine serum albumin (66,409 Da), ovalbumin (44,287 Da), carbonic anhydrase (29,000 Da).

    Journal: BMC Microbiology

    Article Title: Metagenomic approach for the isolation of a thermostable ?-galactosidase with high tolerance of galactose and glucose from soil samples of Turpan Basin

    doi: 10.1186/1471-2180-13-237

    Figure Lengend Snippet: SDS-PAGE analysis of recombinant Gal308 from supernatant of E. coli BL21 (DE3) cell lysates and purified Gal308 by affinity chromatography. Lanes: M, standard protein molecular mass markers (sizes in kilodaltons are indicated on the left); 1, recombinant Gal308 from supernatant of E. coli BL21 (DE3) cell lysates; 2, recombinant Gal308 purified by His•Bind® Purification Kit. The sizes in kilodaltons of protein marker were listed as follows: porcine heart myosin (200,000 Da), E. coli β-galactosidase (116,000 Da), rabbit muscle phosphorylase B (97,200 Da), bovine serum albumin (66,409 Da), ovalbumin (44,287 Da), carbonic anhydrase (29,000 Da).

    Article Snippet: E. coli BL21 (DE3; Novagen) was used as the host for expression of gal308 gene under the control of the T7 promoter.

    Techniques: SDS Page, Recombinant, Purification, Affinity Chromatography, Marker

    SDS-PAGE [stacking gel (5%, w/v) and separating gel (10%, w/v)] analysis of CHAO YT–02 . Lanes: M, molecular standard; 1, purified recombinant CHAO YT–02 ; 2, E. coli BL21 (DE3) harboring pET-28b- chao after induction; 3, E. coli BL21 (DE3) harboring pET-28b- chao without induction; 4, E. coli BL21 (DE3) harboring pET-28b without induction; 5, E. coli BL21 (DE3) harboring pET-28b after induction.

    Journal: Frontiers in Microbiology

    Article Title: Characterization of a New Cyclohexylamine Oxidase From Acinetobacter sp. YT-02

    doi: 10.3389/fmicb.2018.02848

    Figure Lengend Snippet: SDS-PAGE [stacking gel (5%, w/v) and separating gel (10%, w/v)] analysis of CHAO YT–02 . Lanes: M, molecular standard; 1, purified recombinant CHAO YT–02 ; 2, E. coli BL21 (DE3) harboring pET-28b- chao after induction; 3, E. coli BL21 (DE3) harboring pET-28b- chao without induction; 4, E. coli BL21 (DE3) harboring pET-28b without induction; 5, E. coli BL21 (DE3) harboring pET-28b after induction.

    Article Snippet: E. coli BL21 (DE3) and pET-28b (Novagen, Wisconsin, United States) were used as the host strain and expression vector for gene expression, respectively.

    Techniques: SDS Page, Purification, Recombinant, Positron Emission Tomography