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competent e coli bl21  (Fisher Scientific)

 
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    Structured Review

    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.
    Competent E Coli Bl21, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/competent e coli bl21/product/Fisher Scientific
    Average 86 stars, based on 1 article reviews
    competent e coli bl21 - by Bioz Stars, 2026-05
    86/100 stars

    Images

    1) Product Images from "Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen"

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

    Journal: Food Chemistry: Molecular Sciences

    doi: 10.1016/j.fochms.2026.100357

    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.
    Figure Legend 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.

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



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    Image Search Results


    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.

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    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