bl21 (New England Biolabs)


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

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
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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
![... the supernatant of cultures of the E. coli Bl21 dxs RBS library expressing isp S and idi ... 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](https://storage.googleapis.com/bioz_article_images/PMC6833178/12934_2019_1235_Fig7_HTML.jpg)
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

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

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

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

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

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

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
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