bl21 competent e.coli Search Results


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  • 99
    New England Biolabs bl21 t7
    Detection of chloroplast-expressed mTurquoise2 in transgenic lines of Marchantia polymorpha. (A) M. polymorpha protein extracts separated by SDS–PAGE. Protein extracts from wild type (WT) and transplastomic (CL0*b) lines of M. polymorpha were separated by 4–12% SDS–PAGE, and visualized by in-gel fluorescence (left) and subsequent Coomassie stain (right). The fluorescence image was generated using a custom imaging device described in the Materials and Methods for visualization of CFP bands (emission 486/10 nm, green) and marker (emission 540/10 nm, red). (B) Untagged and His 6 -tagged mTurquoise2 separated by SDS–PAGE. Untagged mTurquoise2 was expressed from plasmids pCS CL0*b ( psbA promoter) in <t>BL21</t> E. coli and pCRB SREI (T7 promoter) in T7 Express E. coli. His 6 -tagged mTurquoise2 was expressed from plasmid pCRB SREI 6his (T7 promoter) and purified by affinity chromatography. The rightmost lanes contain 50 ng of unboiled and boiled purified protein, respectively. Visualization by in-gel fluorescence and Coomassie stain was conducted as described above. (C) Standard curve for quantification of mTurquoise2 based on in-gel fluorescence. Serial dilutions of 1 µg purified of mTurquoise2 were separated by 4–12% SDS–PAGE and the band intensity quantified by in-gel fluorescence as described in the Materials and Methods. Levels of mTurquoise2 extracted from transplastomic (CL0*b) M. polymorpha (red cross) were estimated by linear regression analysis on densities of fluorescent target bands as shown in (A). Error bars represent the SD of average band density between three different experiments.
    Bl21 T7, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 136 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore bl21 competent e coli cells
    Detection of chloroplast-expressed mTurquoise2 in transgenic lines of Marchantia polymorpha. (A) M. polymorpha protein extracts separated by SDS–PAGE. Protein extracts from wild type (WT) and transplastomic (CL0*b) lines of M. polymorpha were separated by 4–12% SDS–PAGE, and visualized by in-gel fluorescence (left) and subsequent Coomassie stain (right). The fluorescence image was generated using a custom imaging device described in the Materials and Methods for visualization of CFP bands (emission 486/10 nm, green) and marker (emission 540/10 nm, red). (B) Untagged and His 6 -tagged mTurquoise2 separated by SDS–PAGE. Untagged mTurquoise2 was expressed from plasmids pCS CL0*b ( psbA promoter) in <t>BL21</t> E. coli and pCRB SREI (T7 promoter) in T7 Express E. coli. His 6 -tagged mTurquoise2 was expressed from plasmid pCRB SREI 6his (T7 promoter) and purified by affinity chromatography. The rightmost lanes contain 50 ng of unboiled and boiled purified protein, respectively. Visualization by in-gel fluorescence and Coomassie stain was conducted as described above. (C) Standard curve for quantification of mTurquoise2 based on in-gel fluorescence. Serial dilutions of 1 µg purified of mTurquoise2 were separated by 4–12% SDS–PAGE and the band intensity quantified by in-gel fluorescence as described in the Materials and Methods. Levels of mTurquoise2 extracted from transplastomic (CL0*b) M. polymorpha (red cross) were estimated by linear regression analysis on densities of fluorescent target bands as shown in (A). Error bars represent the SD of average band density between three different experiments.
    Bl21 Competent E Coli Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 2 article reviews
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    90
    New England Biolabs bl21 competent e coli
    Examples of the differences between the original RefSeq annotation and our reannotation. a In the reannotation, one pseudogene (RS16270) was identified as two genes, ins A and ins B, which show strong homology to the insertion element protein, IS1. b In the reannotation, two pseudogenes were re-identified as two genes ( lac Z1 and lac Z2), whereas the hypothetical protein was reannotated and shown to be highly homologous with the DNA-directed RNA polymerase gene ECBD_2906 from E. coli strain <t>BL21-DE3</t>
    Bl21 Competent E Coli, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 90/100, based on 267 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bl21 competent e coli/product/New England Biolabs
    Average 90 stars, based on 267 article reviews
    Price from $9.99 to $1999.99
    bl21 competent e coli - by Bioz Stars, 2020-08
    90/100 stars
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    99
    New England Biolabs bl21 competent escherichia coli cells
    (A) Extracted ion chromatograms performed on culture supernatant of Escherichia coli <t>BL21</t> <t>DE3</t> pET29a_ agrBD after induction with IPTG (BD+; upper panel) and the synthetic peptide R5T0 (lower panel; R5T0 molecular formula: C 31 H 41 N 5 O 5 S 2 ). (B) Mass spectrometry fragmentation spectra for chromatographic peaks with retention times of 61.2 and 63.9 min (marked with a box in A ). (C,D) Structure and assignment of fragments detected in MS/MS spectra to fragments of R5T0.
    Bl21 Competent Escherichia Coli Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 126 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bl21 competent escherichia coli cells/product/New England Biolabs
    Average 99 stars, based on 126 article reviews
    Price from $9.99 to $1999.99
    bl21 competent escherichia coli cells - by Bioz Stars, 2020-08
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    90
    Avantor bl21 competent e coli
    (A) Extracted ion chromatograms performed on culture supernatant of Escherichia coli <t>BL21</t> <t>DE3</t> pET29a_ agrBD after induction with IPTG (BD+; upper panel) and the synthetic peptide R5T0 (lower panel; R5T0 molecular formula: C 31 H 41 N 5 O 5 S 2 ). (B) Mass spectrometry fragmentation spectra for chromatographic peaks with retention times of 61.2 and 63.9 min (marked with a box in A ). (C,D) Structure and assignment of fragments detected in MS/MS spectra to fragments of R5T0.
    Bl21 Competent E Coli, supplied by Avantor, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bl21 competent e coli/product/Avantor
    Average 90 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    bl21 competent e coli - by Bioz Stars, 2020-08
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    Image Search Results


    Detection of chloroplast-expressed mTurquoise2 in transgenic lines of Marchantia polymorpha. (A) M. polymorpha protein extracts separated by SDS–PAGE. Protein extracts from wild type (WT) and transplastomic (CL0*b) lines of M. polymorpha were separated by 4–12% SDS–PAGE, and visualized by in-gel fluorescence (left) and subsequent Coomassie stain (right). The fluorescence image was generated using a custom imaging device described in the Materials and Methods for visualization of CFP bands (emission 486/10 nm, green) and marker (emission 540/10 nm, red). (B) Untagged and His 6 -tagged mTurquoise2 separated by SDS–PAGE. Untagged mTurquoise2 was expressed from plasmids pCS CL0*b ( psbA promoter) in BL21 E. coli and pCRB SREI (T7 promoter) in T7 Express E. coli. His 6 -tagged mTurquoise2 was expressed from plasmid pCRB SREI 6his (T7 promoter) and purified by affinity chromatography. The rightmost lanes contain 50 ng of unboiled and boiled purified protein, respectively. Visualization by in-gel fluorescence and Coomassie stain was conducted as described above. (C) Standard curve for quantification of mTurquoise2 based on in-gel fluorescence. Serial dilutions of 1 µg purified of mTurquoise2 were separated by 4–12% SDS–PAGE and the band intensity quantified by in-gel fluorescence as described in the Materials and Methods. Levels of mTurquoise2 extracted from transplastomic (CL0*b) M. polymorpha (red cross) were estimated by linear regression analysis on densities of fluorescent target bands as shown in (A). Error bars represent the SD of average band density between three different experiments.

    Journal: Plant and Cell Physiology

    Article Title: A Cyan Fluorescent Reporter Expressed from the Chloroplast Genome of Marchantia polymorpha

    doi: 10.1093/pcp/pcv160

    Figure Lengend Snippet: Detection of chloroplast-expressed mTurquoise2 in transgenic lines of Marchantia polymorpha. (A) M. polymorpha protein extracts separated by SDS–PAGE. Protein extracts from wild type (WT) and transplastomic (CL0*b) lines of M. polymorpha were separated by 4–12% SDS–PAGE, and visualized by in-gel fluorescence (left) and subsequent Coomassie stain (right). The fluorescence image was generated using a custom imaging device described in the Materials and Methods for visualization of CFP bands (emission 486/10 nm, green) and marker (emission 540/10 nm, red). (B) Untagged and His 6 -tagged mTurquoise2 separated by SDS–PAGE. Untagged mTurquoise2 was expressed from plasmids pCS CL0*b ( psbA promoter) in BL21 E. coli and pCRB SREI (T7 promoter) in T7 Express E. coli. His 6 -tagged mTurquoise2 was expressed from plasmid pCRB SREI 6his (T7 promoter) and purified by affinity chromatography. The rightmost lanes contain 50 ng of unboiled and boiled purified protein, respectively. Visualization by in-gel fluorescence and Coomassie stain was conducted as described above. (C) Standard curve for quantification of mTurquoise2 based on in-gel fluorescence. Serial dilutions of 1 µg purified of mTurquoise2 were separated by 4–12% SDS–PAGE and the band intensity quantified by in-gel fluorescence as described in the Materials and Methods. Levels of mTurquoise2 extracted from transplastomic (CL0*b) M. polymorpha (red cross) were estimated by linear regression analysis on densities of fluorescent target bands as shown in (A). Error bars represent the SD of average band density between three different experiments.

    Article Snippet: Visualization of proteins by in-gel fluorescence and coomassie staining For total protein extraction from M. polymorpha tissues, 50 mg (fresh weight) of thallus were ground by liquid nitrogen and the resulting powder vortexed in 200 µl of 2 × Tris–glycine for 30 s. For total protein extraction from BL21 or T7 Express competent E. coli (New England Biolabs), an aliquot of overnight culture containing approximately 0.5–1 × 109 cells was pelleted by centrifugation at 14,000 r.p.m. and 4°C for 1 min, resuspended in 50 µl of 2 × Tris–glycine SDS sample buffer and vortexed for 30 s. In both cases, 2-fold dilutions of crude extracts were centrifuged at 14,000 r.p.m. and 4°C for 20 min to remove cell debris, and unboiled (unless indicated otherwise) supernatants were directly loaded onto a NuPAGE Novex 4–12% Bis–Tris protein minigel (Life Technologies).

    Techniques: Transgenic Assay, SDS Page, Fluorescence, Staining, Generated, Imaging, Marker, Plasmid Preparation, Purification, Affinity Chromatography

    Examples of the differences between the original RefSeq annotation and our reannotation. a In the reannotation, one pseudogene (RS16270) was identified as two genes, ins A and ins B, which show strong homology to the insertion element protein, IS1. b In the reannotation, two pseudogenes were re-identified as two genes ( lac Z1 and lac Z2), whereas the hypothetical protein was reannotated and shown to be highly homologous with the DNA-directed RNA polymerase gene ECBD_2906 from E. coli strain BL21-DE3

    Journal: BMC Genomics

    Article Title: Genome re-sequencing and reannotation of the Escherichia coli ER2566 strain and transcriptome sequencing under overexpression conditions

    doi: 10.1186/s12864-020-06818-1

    Figure Lengend Snippet: Examples of the differences between the original RefSeq annotation and our reannotation. a In the reannotation, one pseudogene (RS16270) was identified as two genes, ins A and ins B, which show strong homology to the insertion element protein, IS1. b In the reannotation, two pseudogenes were re-identified as two genes ( lac Z1 and lac Z2), whereas the hypothetical protein was reannotated and shown to be highly homologous with the DNA-directed RNA polymerase gene ECBD_2906 from E. coli strain BL21-DE3

    Article Snippet: Background The Escherichia coli expression system is one of the most well-characterized classical expression systems for recombinant protein expression in biological science.

    Techniques:

    Recombinant c3B protein expression, purification, and detection. (A) Coomassie blue-stained polyacrylamide gel of recombinant MBP-c3B protein expressed in BL21  E. coli  and affinity purified using amylose resin. Lane M, molecular mass markers (Mark 12;

    Journal: Journal of Clinical Microbiology

    Article Title: Pan-Serotype Diagnostic for Foot-and-Mouth Disease Using the Consensus Antigen of Nonstructural Protein 3B

    doi: 10.1128/JCM.03491-14

    Figure Lengend Snippet: Recombinant c3B protein expression, purification, and detection. (A) Coomassie blue-stained polyacrylamide gel of recombinant MBP-c3B protein expressed in BL21 E. coli and affinity purified using amylose resin. Lane M, molecular mass markers (Mark 12;

    Article Snippet: Chemically competent BL21 E. coli (NEB) was transformed with 10 ng pMAL-c5e or pMAL-c3B for overexpression of recombinant MBP or MBP-c3B fusion protein, according to the manufacturer's instructions.

    Techniques: Recombinant, Expressing, Purification, Staining, Affinity Purification

    (A) Extracted ion chromatograms performed on culture supernatant of Escherichia coli BL21 DE3 pET29a_ agrBD after induction with IPTG (BD+; upper panel) and the synthetic peptide R5T0 (lower panel; R5T0 molecular formula: C 31 H 41 N 5 O 5 S 2 ). (B) Mass spectrometry fragmentation spectra for chromatographic peaks with retention times of 61.2 and 63.9 min (marked with a box in A ). (C,D) Structure and assignment of fragments detected in MS/MS spectra to fragments of R5T0.

    Journal: Frontiers in Microbiology

    Article Title: Identification of the agr Peptide of Listeria monocytogenes

    doi: 10.3389/fmicb.2016.00989

    Figure Lengend Snippet: (A) Extracted ion chromatograms performed on culture supernatant of Escherichia coli BL21 DE3 pET29a_ agrBD after induction with IPTG (BD+; upper panel) and the synthetic peptide R5T0 (lower panel; R5T0 molecular formula: C 31 H 41 N 5 O 5 S 2 ). (B) Mass spectrometry fragmentation spectra for chromatographic peaks with retention times of 61.2 and 63.9 min (marked with a box in A ). (C,D) Structure and assignment of fragments detected in MS/MS spectra to fragments of R5T0.

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

    Techniques: Mass Spectrometry