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    Millipore escherichia coli e coli strain bl21
    SDS-PAGE of purified S100A9 subunit of calprotectin (S100A9). S100A9 sequences were inserted in the vector (pET15b) and expressed in <t>Escherichia</t> coli <t>BL21</t> (DE3), and they were purified using Ni-NTA affinity chromatography and verified as the right protein. Lanes 1, 2, and 3 represent S100A9 before purification and lanes 4, 5, and 6 after purification.
    Escherichia Coli E Coli Strain Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 369 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/escherichia coli e coli strain bl21/product/Millipore
    Average 99 stars, based on 369 article reviews
    Price from $9.99 to $1999.99
    escherichia coli e coli strain bl21 - by Bioz Stars, 2020-05
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    99
    Millipore e coli strains bl21 de3
    Expression and purification of rDer p 2/Der p 1 mosaic proteins. Coomassie-stained SDS-PAGE–containing protein extracts of <t>BL21</t> (DE3) expressing Der p 2/1C and Der p 2/1S (lanes 1) , purified Der p 2/1C and Der p 2/1S ( lanes 2 ; A ), and purified
    E Coli Strains Bl21 De3, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 386 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli strains bl21 de3/product/Millipore
    Average 99 stars, based on 386 article reviews
    Price from $9.99 to $1999.99
    e coli strains bl21 de3 - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

    99
    Millipore bl21 de3 strain e coli
    Expression and purification of rDer p 2/Der p 1 mosaic proteins. Coomassie-stained SDS-PAGE–containing protein extracts of <t>BL21</t> (DE3) expressing Der p 2/1C and Der p 2/1S (lanes 1) , purified Der p 2/1C and Der p 2/1S ( lanes 2 ; A ), and purified
    Bl21 De3 Strain E Coli, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bl21 de3 strain e coli/product/Millipore
    Average 99 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    bl21 de3 strain e coli - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

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    SDS-PAGE of purified S100A9 subunit of calprotectin (S100A9). S100A9 sequences were inserted in the vector (pET15b) and expressed in Escherichia coli BL21 (DE3), and they were purified using Ni-NTA affinity chromatography and verified as the right protein. Lanes 1, 2, and 3 represent S100A9 before purification and lanes 4, 5, and 6 after purification.

    Journal: Turkish Journal of Biology

    Article Title: Effect of calprotectin subunit S100A9 on the expression and methylation of OCLN in human melanoma cell line A-375

    doi: 10.3906/biy-1704-14

    Figure Lengend Snippet: SDS-PAGE of purified S100A9 subunit of calprotectin (S100A9). S100A9 sequences were inserted in the vector (pET15b) and expressed in Escherichia coli BL21 (DE3), and they were purified using Ni-NTA affinity chromatography and verified as the right protein. Lanes 1, 2, and 3 represent S100A9 before purification and lanes 4, 5, and 6 after purification.

    Article Snippet: Competent Escherichia coli strain BL21 (DE3) and the N-terminal S100A9 coding sequence were provided by Novagen.

    Techniques: SDS Page, Purification, Plasmid Preparation, Affinity Chromatography

    Expression and purification of rDer p 2/Der p 1 mosaic proteins. Coomassie-stained SDS-PAGE–containing protein extracts of BL21 (DE3) expressing Der p 2/1C and Der p 2/1S (lanes 1) , purified Der p 2/1C and Der p 2/1S ( lanes 2 ; A ), and purified

    Journal: The Journal of allergy and clinical immunology

    Article Title: Hypoallergenic Der p 1/Der p 2 combination vaccines for immunotherapy of house dust mite allergy

    doi: 10.1016/j.jaci.2012.05.035

    Figure Lengend Snippet: Expression and purification of rDer p 2/Der p 1 mosaic proteins. Coomassie-stained SDS-PAGE–containing protein extracts of BL21 (DE3) expressing Der p 2/1C and Der p 2/1S (lanes 1) , purified Der p 2/1C and Der p 2/1S ( lanes 2 ; A ), and purified

    Article Snippet: Expression plasmids containing the Der p 2/1 constructs were transformed into E coli strain BL21 (DE3; Novagen, Merck).

    Techniques: Expressing, Purification, Staining, SDS Page

    SDS-PAGE analysis of four different recombinant chitinases. (a) Intracellular recombinant chitinase inrCHI31; 1: control transformant BL21-pET52b; 2: control transformant BL21-pET52b induced by 1.0 mM IPTG; 3: protein marker; 4: transformant BL21-inCHI31; 5–8: transformant BL21-inCHI31 induced by 1.0 mM IPTG for 3, 4, 5, and 6 h. (b) Extracellular recombinant chitinase exrCHI31; 1–3: control transformant BL21-pET52b induced by 1.0 mM IPTG for 3, 6, and 0 h; 4, 9: protein marker; 5–8: transformant BL21-exCHI31 induced by IPTG for 3, 4, 5, and 6 h; 10-11: transformant BL21-exCHI31 was not induced. (c) Intracellular recombinant chitinase inrCHI32; 1–5: transformant BL21-inCHI32 induced by 1.0 mM IPTG for 6, 5, 4, 3, and 0 h; 6: control transformant BL21-pET52b induced by 1.0 mM IPTG for 5 h; 7: protein marker. (d) Extracellular recombinant chitinase exrCHI32. 1: protein marker; 2–5: transformant BL21-exCHI32 induced by 1.0 mM IPTG for 3, 4, 5, and 6 h; 6: protein marker; 7, 8: control transformant BL21-pET52b induced for 0 and 3 h at 30°C.

    Journal: The Scientific World Journal

    Article Title: Chitinase Genes LbCHI31 and LbCHI32 from Limonium bicolor Were Successfully Expressed in Escherichia coli and Exhibit Recombinant Chitinase Activities

    doi: 10.1155/2013/648382

    Figure Lengend Snippet: SDS-PAGE analysis of four different recombinant chitinases. (a) Intracellular recombinant chitinase inrCHI31; 1: control transformant BL21-pET52b; 2: control transformant BL21-pET52b induced by 1.0 mM IPTG; 3: protein marker; 4: transformant BL21-inCHI31; 5–8: transformant BL21-inCHI31 induced by 1.0 mM IPTG for 3, 4, 5, and 6 h. (b) Extracellular recombinant chitinase exrCHI31; 1–3: control transformant BL21-pET52b induced by 1.0 mM IPTG for 3, 6, and 0 h; 4, 9: protein marker; 5–8: transformant BL21-exCHI31 induced by IPTG for 3, 4, 5, and 6 h; 10-11: transformant BL21-exCHI31 was not induced. (c) Intracellular recombinant chitinase inrCHI32; 1–5: transformant BL21-inCHI32 induced by 1.0 mM IPTG for 6, 5, 4, 3, and 0 h; 6: control transformant BL21-pET52b induced by 1.0 mM IPTG for 5 h; 7: protein marker. (d) Extracellular recombinant chitinase exrCHI32. 1: protein marker; 2–5: transformant BL21-exCHI32 induced by 1.0 mM IPTG for 3, 4, 5, and 6 h; 6: protein marker; 7, 8: control transformant BL21-pET52b induced for 0 and 3 h at 30°C.

    Article Snippet: Strains and Plasmids Escherichia coli strain Top10 (TaKaRa Biotechnology Co., Ltd., Dalian, China) was used for the genetic manipulation; E. coli BL21 strain and pET-52b(+) vector (Novagen, Madison, USA) were employed for the prokaryotic expression experiments.

    Techniques: SDS Page, Recombinant, Marker

    Enzymatic properties of four different recombinant chitinases. Dark blue: enzymatic properties of recombinant intracellular inrCHI31; pink: enzymatic properties of recombinant extracellular exrCHI31; purple: enzymatic properties of recombinant intracellular inrCHI32; Powder blue: enzymatic properties of recombinant intracellular exrCHI32. The precipitates of transformants BL21-inCHI31 and BL21-inCHI32 were used to measure chitinase activity. The culture supernatants of transformants BL21-exCHI31 and BL21-exCHI32 were used to measure chitinase activity. The supernatant was used as a control after being boiled at 100°C for 20 min. (a) Regulation of enzyme production of four transformants BL21-inCHI31, BL21-exCHI31, BL21-inCHI32, and BL21-exCHI32. The four transformants were induced by 1 mM IPTG at 30°C for 2 to 8 h, with 1 h intervals. The enzyme activities at different induced times were measured. (b) The effects of temperature on four recombinant activities. The chitinase activities were measured between 35°C and 80°C for 30 min at 5°C intervals (pH = 4.5). (c) The effects of temperature on the stability of four recombinases. The enzymatic solution (pH = 4.5) was incubated between 35°C and 80°C for 30 min at 5°C intervals, and the remaining activity was then measured. (d) The effects of pH on four recombinase enzymatic activities. Enzymatic activity was measured in the reaction buffer at different pH values from 3 to 12 at 1-unit intervals. All experiments were performed three times.

    Journal: The Scientific World Journal

    Article Title: Chitinase Genes LbCHI31 and LbCHI32 from Limonium bicolor Were Successfully Expressed in Escherichia coli and Exhibit Recombinant Chitinase Activities

    doi: 10.1155/2013/648382

    Figure Lengend Snippet: Enzymatic properties of four different recombinant chitinases. Dark blue: enzymatic properties of recombinant intracellular inrCHI31; pink: enzymatic properties of recombinant extracellular exrCHI31; purple: enzymatic properties of recombinant intracellular inrCHI32; Powder blue: enzymatic properties of recombinant intracellular exrCHI32. The precipitates of transformants BL21-inCHI31 and BL21-inCHI32 were used to measure chitinase activity. The culture supernatants of transformants BL21-exCHI31 and BL21-exCHI32 were used to measure chitinase activity. The supernatant was used as a control after being boiled at 100°C for 20 min. (a) Regulation of enzyme production of four transformants BL21-inCHI31, BL21-exCHI31, BL21-inCHI32, and BL21-exCHI32. The four transformants were induced by 1 mM IPTG at 30°C for 2 to 8 h, with 1 h intervals. The enzyme activities at different induced times were measured. (b) The effects of temperature on four recombinant activities. The chitinase activities were measured between 35°C and 80°C for 30 min at 5°C intervals (pH = 4.5). (c) The effects of temperature on the stability of four recombinases. The enzymatic solution (pH = 4.5) was incubated between 35°C and 80°C for 30 min at 5°C intervals, and the remaining activity was then measured. (d) The effects of pH on four recombinase enzymatic activities. Enzymatic activity was measured in the reaction buffer at different pH values from 3 to 12 at 1-unit intervals. All experiments were performed three times.

    Article Snippet: Strains and Plasmids Escherichia coli strain Top10 (TaKaRa Biotechnology Co., Ltd., Dalian, China) was used for the genetic manipulation; E. coli BL21 strain and pET-52b(+) vector (Novagen, Madison, USA) were employed for the prokaryotic expression experiments.

    Techniques: Recombinant, Activity Assay, Incubation

    Purification of GafD from E. coli BL21 λDE3(pKJ1) periplasm by affinity chromatography and analysis of the reactivities of fimbrial preparations with anti-G-fimbria and anti-GafD antibodies. (A) Binding of 14 C-labeled GafD to GlcNAc-agarose. Lane 1, pulse-labeled periplasmic peptides from rifampin-treated E. coli BL21 λDE3(pKJ1); lane 2, peptides not bound to GlcNAc-agarose; lane 3, peptides bound to GlcNAc-agarose. (B) Coomassie blue-stained SDS-PAGE gel of GafD peptides eluted with 5% (wt/vol) GlcNAc from the GlcNAc-agarose column. The peptides were prepared from periplasm of nonlabeled E. coli BL21 λDE3(pKJ1) (lane 1) and E. coli BL21 λDE3 expressing the truncated GafD1-178 (lane 2). (C) Western blot of fimbrial preparations. Lanes 1 to 3, reactivities of fimbrial peptides with anti-G-fimbria antibodies; lanes 4 to 6, reactivities with anti-GafD antibodies. The fimbrial preparations were the G fimbria isolated from E. coli HB101(pRR-5) (lanes 1 and 4), the mutated G fimbria without lectin activity isolated from E. coli HB101(pHUB110) (lanes 2 and 5), and the type 1 fimbria from E. coli EH826 (lanes 3 and 6). The migration distances of molecular weight markers are indicated on the left; those of the GafD and the GafA peptides are indicated on the right.

    Journal: Journal of Bacteriology

    Article Title: The gaf Fimbrial Gene Cluster of Escherichia coli Expresses a Full-Size and a Truncated Soluble Adhesin Protein

    doi: 10.1128/JB.183.2.512-519.2001

    Figure Lengend Snippet: Purification of GafD from E. coli BL21 λDE3(pKJ1) periplasm by affinity chromatography and analysis of the reactivities of fimbrial preparations with anti-G-fimbria and anti-GafD antibodies. (A) Binding of 14 C-labeled GafD to GlcNAc-agarose. Lane 1, pulse-labeled periplasmic peptides from rifampin-treated E. coli BL21 λDE3(pKJ1); lane 2, peptides not bound to GlcNAc-agarose; lane 3, peptides bound to GlcNAc-agarose. (B) Coomassie blue-stained SDS-PAGE gel of GafD peptides eluted with 5% (wt/vol) GlcNAc from the GlcNAc-agarose column. The peptides were prepared from periplasm of nonlabeled E. coli BL21 λDE3(pKJ1) (lane 1) and E. coli BL21 λDE3 expressing the truncated GafD1-178 (lane 2). (C) Western blot of fimbrial preparations. Lanes 1 to 3, reactivities of fimbrial peptides with anti-G-fimbria antibodies; lanes 4 to 6, reactivities with anti-GafD antibodies. The fimbrial preparations were the G fimbria isolated from E. coli HB101(pRR-5) (lanes 1 and 4), the mutated G fimbria without lectin activity isolated from E. coli HB101(pHUB110) (lanes 2 and 5), and the type 1 fimbria from E. coli EH826 (lanes 3 and 6). The migration distances of molecular weight markers are indicated on the left; those of the GafD and the GafA peptides are indicated on the right.

    Article Snippet: E. coli strain BL21 λDE3 ( ompT lon ) and expression vector pET-22b(+) were from Novagen Inc. (Madison, Wis.).

    Techniques: Purification, Affinity Chromatography, Binding Assay, Labeling, Staining, SDS Page, Expressing, Western Blot, Isolation, Activity Assay, Migration, Molecular Weight