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New England Biolabs e coli bl21 de3 competent cells
E Coli Bl21 De3 Competent Cells, 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
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Fisher Scientific competent e coli bl21
Expression and purification of Nb16-β-gal. <t>BL21</t> bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.
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Expression and purification of Nb16-β-gal. <t>BL21</t> bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.
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New England Biolabs competent bl21 de3 e coli
Expression and purification of Nb16-β-gal. <t>BL21</t> bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.
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New England Biolabs e coli bl21 de3 cells
Expression and purification of Nb16-β-gal. <t>BL21</t> bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.
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New England Biolabs bl21 bacteria
Expression and purification of Nb16-β-gal. <t>BL21</t> bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.
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New England Biolabs c2527h
Expression and purification of Nb16-β-gal. <t>BL21</t> bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.
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New England Biolabs e coli bl21 strain
FRET constructs and ratio (A) Plasmid designs of various constructs are illustrated. The sequences of three linkers and two tandem repeats (TR) proteins used in the study are shown. (B) Representative image of E. coli cultures expressing each construct. (C) Scatterplot of fluorescence intensity obtained in the green and red channels with the plate reader. The dotted and solid circles denote two biological replicates per sample with eight technical replicates each. FRET ratios measured by HyCAP are significantly higher than those determined by the plate reader, owing to differences in the excitation and emission measurement setups. FRET ratio distributions of replicates measured using plate reader (30 replicates each) (D) and HyCAP (E).
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New England Biolabs competent e coli bl21 de3 cells
FRET constructs and ratio (A) Plasmid designs of various constructs are illustrated. The sequences of three linkers and two tandem repeats (TR) proteins used in the study are shown. (B) Representative image of E. coli cultures expressing each construct. (C) Scatterplot of fluorescence intensity obtained in the green and red channels with the plate reader. The dotted and solid circles denote two biological replicates per sample with eight technical replicates each. FRET ratios measured by HyCAP are significantly higher than those determined by the plate reader, owing to differences in the excitation and emission measurement setups. FRET ratio distributions of replicates measured using plate reader (30 replicates each) (D) and HyCAP (E).
Competent E Coli Bl21 De3 Cells, 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
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Expression and purification of Nb16-β-gal. BL21 bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.

Journal: Food Chemistry: Molecular Sciences

Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen

doi: 10.1016/j.fochms.2026.100357

Figure Lengend Snippet: Expression and purification of Nb16-β-gal. BL21 bacteria carrying pRCH-Nb16-βGal were used to produce the target protein. Proteins in lysates from uninduced (lane U) and induced (lane I) bacteria, fractions containing the target protein after Ni 2+ column purification (lane 1), and the purified target protein after the second-step SEC purification (lane 2) were analyzed by SDS-PAGE on a 4–12% SDS gel. The molecular masses (in kDa) of the proteins in the protein standards (lane M) are indicated on the right side of the gel image. The horizontal arrow indicates the Nb16-β-gal band.

Article Snippet: Competent E. coli BL21 (BL21 StarTM (DE3), Fisher Scientific) was transformed with each of the plasmids described above.

Techniques: Expressing, Purification, Bacteria, SDS Page, SDS-Gel

FRET constructs and ratio (A) Plasmid designs of various constructs are illustrated. The sequences of three linkers and two tandem repeats (TR) proteins used in the study are shown. (B) Representative image of E. coli cultures expressing each construct. (C) Scatterplot of fluorescence intensity obtained in the green and red channels with the plate reader. The dotted and solid circles denote two biological replicates per sample with eight technical replicates each. FRET ratios measured by HyCAP are significantly higher than those determined by the plate reader, owing to differences in the excitation and emission measurement setups. FRET ratio distributions of replicates measured using plate reader (30 replicates each) (D) and HyCAP (E).

Journal: iScience

Article Title: High-throughput screening of FRET-based proteins using a hyperspectral microcapillary array

doi: 10.1016/j.isci.2026.115302

Figure Lengend Snippet: FRET constructs and ratio (A) Plasmid designs of various constructs are illustrated. The sequences of three linkers and two tandem repeats (TR) proteins used in the study are shown. (B) Representative image of E. coli cultures expressing each construct. (C) Scatterplot of fluorescence intensity obtained in the green and red channels with the plate reader. The dotted and solid circles denote two biological replicates per sample with eight technical replicates each. FRET ratios measured by HyCAP are significantly higher than those determined by the plate reader, owing to differences in the excitation and emission measurement setups. FRET ratio distributions of replicates measured using plate reader (30 replicates each) (D) and HyCAP (E).

Article Snippet: E. coli BL21 strain , New England Biolabs , C2527H.

Techniques: Construct, Plasmid Preparation, Expressing, Fluorescence