bl21  (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 bl21
    BL21 DE3 Competent E coli
    BL21 DE3 Competent E coli 20x0 05 ml
    https://www.bioz.com/result/bl21/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bl21 - by Bioz Stars, 2021-04
    99/100 stars

    Images

    1) Product Images from "Investigation of the methylerythritol 4-phosphate pathway for microbial terpenoid production through metabolic control analysis"

    Article Title: Investigation of the methylerythritol 4-phosphate pathway for microbial terpenoid production through metabolic control analysis

    Journal: Microbial Cell Factories

    doi: 10.1186/s12934-019-1235-5

    Specific efflux rates of MEP pathway intermediates calculated from their measured concentrations in the supernatant of cultures of the E. coli Bl21 dxs RBS library expressing isp S and idi from pCOLA::IspS-idi ( \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\overline{\varvec{x}}$$\end{document} x ¯ ± SD, n = 3). The cultures were induced at OD 600 = 0.1 and the supernatant was sampled at OD 600 ≈ 0.5. The export of MEP pathway intermediates occurred after the induction of isp S expression in the dxs expression library. a Metabolite concentration in the supernatant of the cultures. b DXP and MEcPP efflux rates as a function of dxs expression relative to wild-type levels. Linear fits through zero and second-degree polynomial fits through zero are shown for DXP and MEcPP, respectively in ( a ) and ( b ). c Logarithmic plot of MEcPP efflux rate as a function of dxs expression. The data were fitted to a linear function with a slope of 2.0. The red marked data point was excluded from the fit. d The correlation of MEcPP efflux rate with its intracellular concentration, linear fitted through zero. e Combined efflux of DXP, MEcPP and isoprene in dependents of dxs expression, linear fitted
    Figure Legend Snippet: Specific efflux rates of MEP pathway intermediates calculated from their measured concentrations in the supernatant of cultures of the E. coli Bl21 dxs RBS library expressing isp S and idi from pCOLA::IspS-idi ( \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\overline{\varvec{x}}$$\end{document} x ¯ ± SD, n = 3). The cultures were induced at OD 600 = 0.1 and the supernatant was sampled at OD 600 ≈ 0.5. The export of MEP pathway intermediates occurred after the induction of isp S expression in the dxs expression library. a Metabolite concentration in the supernatant of the cultures. b DXP and MEcPP efflux rates as a function of dxs expression relative to wild-type levels. Linear fits through zero and second-degree polynomial fits through zero are shown for DXP and MEcPP, respectively in ( a ) and ( b ). c Logarithmic plot of MEcPP efflux rate as a function of dxs expression. The data were fitted to a linear function with a slope of 2.0. The red marked data point was excluded from the fit. d The correlation of MEcPP efflux rate with its intracellular concentration, linear fitted through zero. e Combined efflux of DXP, MEcPP and isoprene in dependents of dxs expression, linear fitted

    Techniques Used: Expressing, Concentration Assay

    2) Product Images from "Pyocin S5 import into Pseudomonas aeruginosa reveals a generic mode of bacteriocin transport"

    Article Title: Pyocin S5 import into Pseudomonas aeruginosa reveals a generic mode of bacteriocin transport

    Journal: bioRxiv

    doi: 10.1101/856047

    FptA and TonB1 constitute the minimal system for PyoS5-susceptibility in E. coli . (A) Susceptibility to PyoS5 (3 and 60 μM) was assessed for P. aeruginosa YHP17, (B) for E. coli BL21 (DE3) expressing FptA, (C) for E. coli BL21 (DE3) expressing TonB-B1, and (D) for E. coli BL21 (DE3) expressing FptA and TonB-B1. Zones of clearance are observed in all E. coli samples for the ColBPyoS5 (13 μM) control (B-D) and for both concentrations of PyoS5 in E. coli expressing FptA and TonB-B1 (D). In the P. aeruginosa control clearance zones were observed for PyoS5 (A).
    Figure Legend Snippet: FptA and TonB1 constitute the minimal system for PyoS5-susceptibility in E. coli . (A) Susceptibility to PyoS5 (3 and 60 μM) was assessed for P. aeruginosa YHP17, (B) for E. coli BL21 (DE3) expressing FptA, (C) for E. coli BL21 (DE3) expressing TonB-B1, and (D) for E. coli BL21 (DE3) expressing FptA and TonB-B1. Zones of clearance are observed in all E. coli samples for the ColBPyoS5 (13 μM) control (B-D) and for both concentrations of PyoS5 in E. coli expressing FptA and TonB-B1 (D). In the P. aeruginosa control clearance zones were observed for PyoS5 (A).

    Techniques Used: Expressing

    FpvAI and TonB1 constitute the minimal system for PyoS2- and PyoS4-susceptibility. Susceptibility to 1 μM PyoS2, PyoS4, PyoS5 and ColBPyoS5 was assessed for (A) P. aeruginosa YHP17, (B) E. coli BL21 (DE3) expressing FpvAI, (C) E. coli BL21(DE3) expressing TonB-B1, and (D) E. coli BL21 (DE3) expressing FpvAI and TonB-B1. Zones of clearance were observed for all E. coli conditions tested when ColBPyoS5 was applied (B-D). Similarly, E. coli expressing FpvAI and TonB-B1 was susceptible to both PyoS2 and PyoS4, as was the P. aeruginosa control (A+D). Zones of clearance for PyoS5 were only observed in P. aeruginosa .
    Figure Legend Snippet: FpvAI and TonB1 constitute the minimal system for PyoS2- and PyoS4-susceptibility. Susceptibility to 1 μM PyoS2, PyoS4, PyoS5 and ColBPyoS5 was assessed for (A) P. aeruginosa YHP17, (B) E. coli BL21 (DE3) expressing FpvAI, (C) E. coli BL21(DE3) expressing TonB-B1, and (D) E. coli BL21 (DE3) expressing FpvAI and TonB-B1. Zones of clearance were observed for all E. coli conditions tested when ColBPyoS5 was applied (B-D). Similarly, E. coli expressing FpvAI and TonB-B1 was susceptible to both PyoS2 and PyoS4, as was the P. aeruginosa control (A+D). Zones of clearance for PyoS5 were only observed in P. aeruginosa .

    Techniques Used: Expressing

    3) Product Images from "Cytoplasmic Chaperones Enhance Soluble Expression of Anti-EGFR huscFv in Escherichia coli"

    Article Title: Cytoplasmic Chaperones Enhance Soluble Expression of Anti-EGFR huscFv in Escherichia coli

    Journal: Iranian Journal of Biotechnology

    doi: 10.30498/IJB.2020.138200.2314

    Analyses of huscFv expression by BL21 (DE3). Lane A) pET22b-huscFv before inductions; Lane B) pET22b-huscFv after 4h of induction; Lane C) pET22b-huscFv, sonication supernatant fraction; Lane D) pET22b-huscFv sonication pellet fraction; Lane E) pET22b-huscFv, purified huscFv; Lane F) protein marker; Lane G) pET22b-huscFv + pG-KJE8 chaperone, before inductions; Lane H) pET22b-huscFv + pG-KJE8 chaperone, after 4h induction; Lane I) pET22b-huscFv + pG-KJE8 chaperone, sonication supernatant fraction; Lane J) pET22b-huscFv + pG-KJE8 chaperone, sonication pellet fraction; Lane K) pET22b-huscFv + pG-KJE8 chaperone , purified huscFv and Lane L) indicates BL21 (DE3) without plasmid, 4h after induction (control).
    Figure Legend Snippet: Analyses of huscFv expression by BL21 (DE3). Lane A) pET22b-huscFv before inductions; Lane B) pET22b-huscFv after 4h of induction; Lane C) pET22b-huscFv, sonication supernatant fraction; Lane D) pET22b-huscFv sonication pellet fraction; Lane E) pET22b-huscFv, purified huscFv; Lane F) protein marker; Lane G) pET22b-huscFv + pG-KJE8 chaperone, before inductions; Lane H) pET22b-huscFv + pG-KJE8 chaperone, after 4h induction; Lane I) pET22b-huscFv + pG-KJE8 chaperone, sonication supernatant fraction; Lane J) pET22b-huscFv + pG-KJE8 chaperone, sonication pellet fraction; Lane K) pET22b-huscFv + pG-KJE8 chaperone , purified huscFv and Lane L) indicates BL21 (DE3) without plasmid, 4h after induction (control).

    Techniques Used: Expressing, Sonication, Purification, Marker, Plasmid Preparation

    PCR confirmation of the pET-22b-huscFv constructs transformation into the E. coli BL21 (DE3). Lane A –B) indicates the pET-22b-huscFv clones; Lane C) indicates the negative control; Lane D) indicates the DNA size marker.
    Figure Legend Snippet: PCR confirmation of the pET-22b-huscFv constructs transformation into the E. coli BL21 (DE3). Lane A –B) indicates the pET-22b-huscFv clones; Lane C) indicates the negative control; Lane D) indicates the DNA size marker.

    Techniques Used: Polymerase Chain Reaction, Positron Emission Tomography, Construct, Transformation Assay, Clone Assay, Negative Control, Marker

    SDS-PAGE analysis of the expressions of huscFv in different strains of E. coli . Lane A) BL21 (DE3) before inductions; Lane B) BL21 (DE3) after 4h induction; Lane C) BL21 (DE3) after 24h induction; Lane D) Rosetta (DE3) before induction; Lane E) Rosetta (DE3) after 4h induction; Lane F) Rosetta (DE3) after 24h induction; Lane G) SHuffle® T7 strain before inductions; Lane H) SHuffle® T7 after 4h induction; Lane I) SHuffle® T7 after 24h induction; Lane J) BL21 (Inv) before induction; Lane K) BL21 (Inv) after 4h induction; Lane L) BL21 (Inv) after 4h induction and Lane M) indicates the protein marker.
    Figure Legend Snippet: SDS-PAGE analysis of the expressions of huscFv in different strains of E. coli . Lane A) BL21 (DE3) before inductions; Lane B) BL21 (DE3) after 4h induction; Lane C) BL21 (DE3) after 24h induction; Lane D) Rosetta (DE3) before induction; Lane E) Rosetta (DE3) after 4h induction; Lane F) Rosetta (DE3) after 24h induction; Lane G) SHuffle® T7 strain before inductions; Lane H) SHuffle® T7 after 4h induction; Lane I) SHuffle® T7 after 24h induction; Lane J) BL21 (Inv) before induction; Lane K) BL21 (Inv) after 4h induction; Lane L) BL21 (Inv) after 4h induction and Lane M) indicates the protein marker.

    Techniques Used: SDS Page, Marker

    4) Product Images from "The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili from Thermus thermophilus"

    Article Title: The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili from Thermus thermophilus

    Journal: FEBS Open Bio

    doi: 10.1002/2211-5463.12548

    Purification of PilMNO, PilMN, PilM, and PilN. His 6 ‐PilMNO‐Strep (lane 1), His 6 ‐PilMN‐Strep (lane 2), His 6 ‐PilM (lane 3), and PilN‐Strep (lane 4) were purified from Escherichia coli BL21 (DE3) cells as described in Experimental procedures . PilMNO, PilMN, and PilN were isolated from membranes, whereas PilM was isolated from soluble fractions. To separate His 6 ‐PilM (44 kDa), PilN (23 kDa), and PilO‐Strep (22.5 kDa), 4–20% SDS/PAGE was performed (lane 1). All other protein preparations were separated by 14% SDS/PAGE (A). The identity of the proteins was confirmed by western blot using polyclonal antisera against PilM (B) and PilN (C) or using Strep‐Tactin HRP conjugate to detect PilO‐Strep (D). Dotted lines indicate excised lanes from different but comparable gels or blots.
    Figure Legend Snippet: Purification of PilMNO, PilMN, PilM, and PilN. His 6 ‐PilMNO‐Strep (lane 1), His 6 ‐PilMN‐Strep (lane 2), His 6 ‐PilM (lane 3), and PilN‐Strep (lane 4) were purified from Escherichia coli BL21 (DE3) cells as described in Experimental procedures . PilMNO, PilMN, and PilN were isolated from membranes, whereas PilM was isolated from soluble fractions. To separate His 6 ‐PilM (44 kDa), PilN (23 kDa), and PilO‐Strep (22.5 kDa), 4–20% SDS/PAGE was performed (lane 1). All other protein preparations were separated by 14% SDS/PAGE (A). The identity of the proteins was confirmed by western blot using polyclonal antisera against PilM (B) and PilN (C) or using Strep‐Tactin HRP conjugate to detect PilO‐Strep (D). Dotted lines indicate excised lanes from different but comparable gels or blots.

    Techniques Used: Purification, Isolation, SDS Page, Western Blot

    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. ..

    Construct:

    Article Title: Cytoplasmic Chaperones Enhance Soluble Expression of Anti-EGFR huscFv in Escherichia coli
    Article Snippet: Objectives The aim of this study was to increase the expression of soluble humanized anti-EGFR scFv by co-expression with cytoplasmic chaperones under different conditions and to evaluate its activity on the EGFR-overexpressing tumor cell line A431. .. Cell lines, ScFv Construct, Chaperone Plasmids The E. coli strains, including BL21 (DE3), SHuffle® T7 Express Competent (NEB), BL21 Rosetta DE3, Inv, and the expression vector pET22b (+) were purchased from Novagen and New England Biolabs, respectively. .. The chaperone plasmid set was purchased from Takara Bio Inc. ( ). pET22b - humanized anti-EGFR ScFv construct was designed by Veisi K et al.( ) ( ).

    Expressing:

    Article Title: Cytoplasmic Chaperones Enhance Soluble Expression of Anti-EGFR huscFv in Escherichia coli
    Article Snippet: Objectives The aim of this study was to increase the expression of soluble humanized anti-EGFR scFv by co-expression with cytoplasmic chaperones under different conditions and to evaluate its activity on the EGFR-overexpressing tumor cell line A431. .. Cell lines, ScFv Construct, Chaperone Plasmids The E. coli strains, including BL21 (DE3), SHuffle® T7 Express Competent (NEB), BL21 Rosetta DE3, Inv, and the expression vector pET22b (+) were purchased from Novagen and New England Biolabs, respectively. .. The chaperone plasmid set was purchased from Takara Bio Inc. ( ). pET22b - humanized anti-EGFR ScFv construct was designed by Veisi K et al.( ) ( ).

    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: Cytoplasmic Chaperones Enhance Soluble Expression of Anti-EGFR huscFv in Escherichia coli
    Article Snippet: Objectives The aim of this study was to increase the expression of soluble humanized anti-EGFR scFv by co-expression with cytoplasmic chaperones under different conditions and to evaluate its activity on the EGFR-overexpressing tumor cell line A431. .. Cell lines, ScFv Construct, Chaperone Plasmids The E. coli strains, including BL21 (DE3), SHuffle® T7 Express Competent (NEB), BL21 Rosetta DE3, Inv, and the expression vector pET22b (+) were purchased from Novagen and New England Biolabs, respectively. .. The chaperone plasmid set was purchased from Takara Bio Inc. ( ). pET22b - humanized anti-EGFR ScFv construct was designed by Veisi K et al.( ) ( ).

    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.

    other:

    Article Title: The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili from Thermus thermophilus
    Article Snippet: Organisms and cultivation Escherichia coli DH5α, BL21 (DE3) and T7 Express cells harboring pET28a plasmids (New England Biolabs, Ipswich, MA, USA) were grown at 37 °C in LB medium or 2 × YT medium containing 20 μg·mL−1 kanamycin.

    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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  • 99
    New England Biolabs bl21 de3 plyss
    SpdB2-His promotes spheroplast formation by T7 lysozyme and forms unstable pores in planar lipid bilayers. (A) When expression of SpdB2-His was induced in <t>BL21/pLysS,</t> spheroplast (arrows) were formed. In contrast, spheroplasts were not observed in the absence of spdB2 (B) or when expressing spdB2 in BL21 lacking the T7 amidase (C). (D) When purified SpdB2-His was added to the cis side of a lipid bilayer, SpdB2-His inserted into the planar lipid bilayer, showing flickering pore structures. (E) The corresponding all-points conductance level histogram shows that there is no discrete conductance state of the open pore indicated by the long tail in the histogram.
    Bl21 De3 Plyss, 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/bl21 de3 plyss/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bl21 de3 plyss - by Bioz Stars, 2021-04
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    SpdB2-His promotes spheroplast formation by T7 lysozyme and forms unstable pores in planar lipid bilayers. (A) When expression of SpdB2-His was induced in BL21/pLysS, spheroplast (arrows) were formed. In contrast, spheroplasts were not observed in the absence of spdB2 (B) or when expressing spdB2 in BL21 lacking the T7 amidase (C). (D) When purified SpdB2-His was added to the cis side of a lipid bilayer, SpdB2-His inserted into the planar lipid bilayer, showing flickering pore structures. (E) The corresponding all-points conductance level histogram shows that there is no discrete conductance state of the open pore indicated by the long tail in the histogram.

    Journal: mBio

    Article Title: A Multiprotein DNA Translocation Complex Directs Intramycelial Plasmid Spreading during Streptomyces Conjugation

    doi: 10.1128/mBio.02559-14

    Figure Lengend Snippet: SpdB2-His promotes spheroplast formation by T7 lysozyme and forms unstable pores in planar lipid bilayers. (A) When expression of SpdB2-His was induced in BL21/pLysS, spheroplast (arrows) were formed. In contrast, spheroplasts were not observed in the absence of spdB2 (B) or when expressing spdB2 in BL21 lacking the T7 amidase (C). (D) When purified SpdB2-His was added to the cis side of a lipid bilayer, SpdB2-His inserted into the planar lipid bilayer, showing flickering pore structures. (E) The corresponding all-points conductance level histogram shows that there is no discrete conductance state of the open pore indicated by the long tail in the histogram.

    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)].

    Techniques: Expressing, Purification

    Specific efflux rates of MEP pathway intermediates calculated from their measured concentrations in the supernatant of cultures of the E. coli Bl21 dxs RBS library expressing isp S and idi from pCOLA::IspS-idi ( \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\overline{\varvec{x}}$$\end{document} x ¯ ± SD, n = 3). The cultures were induced at OD 600 = 0.1 and the supernatant was sampled at OD 600 ≈ 0.5. The export of MEP pathway intermediates occurred after the induction of isp S expression in the dxs expression library. a Metabolite concentration in the supernatant of the cultures. b DXP and MEcPP efflux rates as a function of dxs expression relative to wild-type levels. Linear fits through zero and second-degree polynomial fits through zero are shown for DXP and MEcPP, respectively in ( a ) and ( b ). c Logarithmic plot of MEcPP efflux rate as a function of dxs expression. The data were fitted to a linear function with a slope of 2.0. The red marked data point was excluded from the fit. d The correlation of MEcPP efflux rate with its intracellular concentration, linear fitted through zero. e Combined efflux of DXP, MEcPP and isoprene in dependents of dxs expression, linear fitted

    Journal: Microbial Cell Factories

    Article Title: Investigation of the methylerythritol 4-phosphate pathway for microbial terpenoid production through metabolic control analysis

    doi: 10.1186/s12934-019-1235-5

    Figure Lengend Snippet: Specific efflux rates of MEP pathway intermediates calculated from their measured concentrations in the supernatant of cultures of the E. coli Bl21 dxs RBS library expressing isp S and idi from pCOLA::IspS-idi ( \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\overline{\varvec{x}}$$\end{document} x ¯ ± SD, n = 3). The cultures were induced at OD 600 = 0.1 and the supernatant was sampled at OD 600 ≈ 0.5. The export of MEP pathway intermediates occurred after the induction of isp S expression in the dxs expression library. a Metabolite concentration in the supernatant of the cultures. b DXP and MEcPP efflux rates as a function of dxs expression relative to wild-type levels. Linear fits through zero and second-degree polynomial fits through zero are shown for DXP and MEcPP, respectively in ( a ) and ( b ). c Logarithmic plot of MEcPP efflux rate as a function of dxs expression. The data were fitted to a linear function with a slope of 2.0. The red marked data point was excluded from the fit. d The correlation of MEcPP efflux rate with its intracellular concentration, linear fitted through zero. e Combined efflux of DXP, MEcPP and isoprene in dependents of dxs expression, linear fitted

    Article Snippet: Bacterial strains and culture conditions Standard cloning and metabolic engineering were carried out using E. coli strains 10β and BL21 (DE3), respectively (both supplied by New England Biolabs, Ipswich, MA, USA).

    Techniques: Expressing, Concentration Assay

    Western blot analysis of the expressed r-PilQ 380-706 protein in E. coli BL21. After running the SDS-PAGE, the protein transferred onto PVDF membrane and detected with HRP-conjugated goat anti-rabbit IgG. (lane 1) total cell lysate of non-induced bacteria; (lane 2) total cell lysate of bacteria after 4 hr induction; (lane 3 and 4) purified r-PilQ 380-706 by Ni 2+ -affinity chromatography.

    Journal: Avicenna Journal of Medical Biotechnology

    Article Title: Molecular characterization and Functional Analysis of the PilQ380-706: a Novel Secretin Domain in Pseudomonas aeruginosa

    doi:

    Figure Lengend Snippet: Western blot analysis of the expressed r-PilQ 380-706 protein in E. coli BL21. After running the SDS-PAGE, the protein transferred onto PVDF membrane and detected with HRP-conjugated goat anti-rabbit IgG. (lane 1) total cell lysate of non-induced bacteria; (lane 2) total cell lysate of bacteria after 4 hr induction; (lane 3 and 4) purified r-PilQ 380-706 by Ni 2+ -affinity chromatography.

    Article Snippet: Bacterial strains, plasmids, and media Escherichia coli (E. coli ) strains Top10F and BL21 (DE3) were used as preservation and expression hosts.

    Techniques: Western Blot, SDS Page, Purification, Affinity Chromatography

    FptA and TonB1 constitute the minimal system for PyoS5-susceptibility in E. coli . (A) Susceptibility to PyoS5 (3 and 60 μM) was assessed for P. aeruginosa YHP17, (B) for E. coli BL21 (DE3) expressing FptA, (C) for E. coli BL21 (DE3) expressing TonB-B1, and (D) for E. coli BL21 (DE3) expressing FptA and TonB-B1. Zones of clearance are observed in all E. coli samples for the ColBPyoS5 (13 μM) control (B-D) and for both concentrations of PyoS5 in E. coli expressing FptA and TonB-B1 (D). In the P. aeruginosa control clearance zones were observed for PyoS5 (A).

    Journal: bioRxiv

    Article Title: Pyocin S5 import into Pseudomonas aeruginosa reveals a generic mode of bacteriocin transport

    doi: 10.1101/856047

    Figure Lengend Snippet: FptA and TonB1 constitute the minimal system for PyoS5-susceptibility in E. coli . (A) Susceptibility to PyoS5 (3 and 60 μM) was assessed for P. aeruginosa YHP17, (B) for E. coli BL21 (DE3) expressing FptA, (C) for E. coli BL21 (DE3) expressing TonB-B1, and (D) for E. coli BL21 (DE3) expressing FptA and TonB-B1. Zones of clearance are observed in all E. coli samples for the ColBPyoS5 (13 μM) control (B-D) and for both concentrations of PyoS5 in E. coli expressing FptA and TonB-B1 (D). In the P. aeruginosa control clearance zones were observed for PyoS5 (A).

    Article Snippet: Chemically competent E. coli NEB5α and BL21 (DE3) were purchased from NEB.

    Techniques: Expressing

    FpvAI and TonB1 constitute the minimal system for PyoS2- and PyoS4-susceptibility. Susceptibility to 1 μM PyoS2, PyoS4, PyoS5 and ColBPyoS5 was assessed for (A) P. aeruginosa YHP17, (B) E. coli BL21 (DE3) expressing FpvAI, (C) E. coli BL21(DE3) expressing TonB-B1, and (D) E. coli BL21 (DE3) expressing FpvAI and TonB-B1. Zones of clearance were observed for all E. coli conditions tested when ColBPyoS5 was applied (B-D). Similarly, E. coli expressing FpvAI and TonB-B1 was susceptible to both PyoS2 and PyoS4, as was the P. aeruginosa control (A+D). Zones of clearance for PyoS5 were only observed in P. aeruginosa .

    Journal: bioRxiv

    Article Title: Pyocin S5 import into Pseudomonas aeruginosa reveals a generic mode of bacteriocin transport

    doi: 10.1101/856047

    Figure Lengend Snippet: FpvAI and TonB1 constitute the minimal system for PyoS2- and PyoS4-susceptibility. Susceptibility to 1 μM PyoS2, PyoS4, PyoS5 and ColBPyoS5 was assessed for (A) P. aeruginosa YHP17, (B) E. coli BL21 (DE3) expressing FpvAI, (C) E. coli BL21(DE3) expressing TonB-B1, and (D) E. coli BL21 (DE3) expressing FpvAI and TonB-B1. Zones of clearance were observed for all E. coli conditions tested when ColBPyoS5 was applied (B-D). Similarly, E. coli expressing FpvAI and TonB-B1 was susceptible to both PyoS2 and PyoS4, as was the P. aeruginosa control (A+D). Zones of clearance for PyoS5 were only observed in P. aeruginosa .

    Article Snippet: Chemically competent E. coli NEB5α and BL21 (DE3) were purchased from NEB.

    Techniques: Expressing