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Stratagene e coli bl21 gold
In vivo interactions of MBP-UreD with (UreABC) 3 , UreB, (UreAC) 3 , and UreBΔ1-19. (A) SDS-PAGE depicting the interactions of MBP-UreD with (UreABC) 3 , UreB, and (UreAC) 3 . E. coli <t>BL21-Gold(DE3)</t> cells were co-transformed with pCDF-MBP-UreD (encoding
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Images

1) Product Images from "The Function of UreB in Klebsiella aerogenes Urease"

Article Title: The Function of UreB in Klebsiella aerogenes Urease

Journal: Biochemistry

doi: 10.1021/bi2011064

In vivo interactions of MBP-UreD with (UreABC) 3 , UreB, (UreAC) 3 , and UreBΔ1-19. (A) SDS-PAGE depicting the interactions of MBP-UreD with (UreABC) 3 , UreB, and (UreAC) 3 . E. coli BL21-Gold(DE3) cells were co-transformed with pCDF-MBP-UreD (encoding
Figure Legend Snippet: In vivo interactions of MBP-UreD with (UreABC) 3 , UreB, (UreAC) 3 , and UreBΔ1-19. (A) SDS-PAGE depicting the interactions of MBP-UreD with (UreABC) 3 , UreB, and (UreAC) 3 . E. coli BL21-Gold(DE3) cells were co-transformed with pCDF-MBP-UreD (encoding

Techniques Used: In Vivo, SDS Page, Transformation Assay

2) Product Images from "Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein ▿"

Article Title: Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein ▿

Journal: Journal of Bacteriology

doi: 10.1128/JB.01426-09

Interactions of MBP-UreD with other urease components in vivo. E. coli BL21-Gold(DE3) cells were cotransformed with either pEC002 (encoding MBP-UreD) or pMal-c2x (encoding MBP-LacZα) along with pEC004, pEC005, pEC006, pEC007, pEC008, or pEC009 (encoding UreABC, UreFG, UreABCEFG, UreE, UreF, or UreG, respectively). Soluble cell extracts were analyzed directly by SDS-PAGE (odd-numbered lanes) or subjected to amylose resin chromatography with the proteins eluted by maltose addition and analyzed by SDS-PAGE (even-numbered lanes). (A) MBP-UreD interactions with multiple urease components. (B) MBP-UreD interactions with single urease components. M, molecular mass markers.
Figure Legend Snippet: Interactions of MBP-UreD with other urease components in vivo. E. coli BL21-Gold(DE3) cells were cotransformed with either pEC002 (encoding MBP-UreD) or pMal-c2x (encoding MBP-LacZα) along with pEC004, pEC005, pEC006, pEC007, pEC008, or pEC009 (encoding UreABC, UreFG, UreABCEFG, UreE, UreF, or UreG, respectively). Soluble cell extracts were analyzed directly by SDS-PAGE (odd-numbered lanes) or subjected to amylose resin chromatography with the proteins eluted by maltose addition and analyzed by SDS-PAGE (even-numbered lanes). (A) MBP-UreD interactions with multiple urease components. (B) MBP-UreD interactions with single urease components. M, molecular mass markers.

Techniques Used: In Vivo, SDS Page, Chromatography

Interactions of MBP-UreD with urease apoprotein. (A) In vivo complex formation. Soluble cell extracts of IPTG-induced E. coli BL21-Gold(DE3)/pEC002 (encoding MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (encoding UreABC) were mixed, incubated at room temperature for 1 h, and chromatographed on amylose resin. Bound proteins were eluted in buffer containing 10 mM maltose and visualized by SDS-PAGE. Lanes: M, molecular mass marker; 1, pEC002 cell extracts; 2, pEC004 cell extracts; 3, coelution of UreABC with MBP-UreD from the amylose resin. (B) In vitro interactions. Purified MBP-UreD (2 μM) was mixed with isolated urease apoprotein (10 μM) in TEB buffer with 25 mM NaCl and, where indicated, cell extracts of E. coli MG1655. Reaction mixtures were incubated at room temperature for 1 h before the mix was subjected to amylose resin chromatography. Bound proteins were eluted with buffer containing 10 mM maltose. Lanes: M, molecular mass marker; 1, purified urease apoprotein; 2, purified MBP-UreD; 3, MBP-UreD plus urease apoprotein; 4, MBP-UreD plus urease apoprotein along with E. coli MG1655 cell extracts; 5, eluted fraction from lane 3; 6, eluted fraction from lane 4.
Figure Legend Snippet: Interactions of MBP-UreD with urease apoprotein. (A) In vivo complex formation. Soluble cell extracts of IPTG-induced E. coli BL21-Gold(DE3)/pEC002 (encoding MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (encoding UreABC) were mixed, incubated at room temperature for 1 h, and chromatographed on amylose resin. Bound proteins were eluted in buffer containing 10 mM maltose and visualized by SDS-PAGE. Lanes: M, molecular mass marker; 1, pEC002 cell extracts; 2, pEC004 cell extracts; 3, coelution of UreABC with MBP-UreD from the amylose resin. (B) In vitro interactions. Purified MBP-UreD (2 μM) was mixed with isolated urease apoprotein (10 μM) in TEB buffer with 25 mM NaCl and, where indicated, cell extracts of E. coli MG1655. Reaction mixtures were incubated at room temperature for 1 h before the mix was subjected to amylose resin chromatography. Bound proteins were eluted with buffer containing 10 mM maltose. Lanes: M, molecular mass marker; 1, purified urease apoprotein; 2, purified MBP-UreD; 3, MBP-UreD plus urease apoprotein; 4, MBP-UreD plus urease apoprotein along with E. coli MG1655 cell extracts; 5, eluted fraction from lane 3; 6, eluted fraction from lane 4.

Techniques Used: In Vivo, Incubation, SDS Page, Marker, In Vitro, Purification, Isolation, Chromatography

3) Product Images from "Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein ▿"

Article Title: Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein ▿

Journal: Journal of Bacteriology

doi: 10.1128/JB.01426-09

Interactions of MBP-UreD with other urease components in vivo. E. coli BL21-Gold(DE3) cells were cotransformed with either pEC002 (encoding MBP-UreD) or pMal-c2x (encoding MBP-LacZα) along with pEC004, pEC005, pEC006, pEC007, pEC008, or pEC009 (encoding UreABC, UreFG, UreABCEFG, UreE, UreF, or UreG, respectively). Soluble cell extracts were analyzed directly by SDS-PAGE (odd-numbered lanes) or subjected to amylose resin chromatography with the proteins eluted by maltose addition and analyzed by SDS-PAGE (even-numbered lanes). (A) MBP-UreD interactions with multiple urease components. (B) MBP-UreD interactions with single urease components. M, molecular mass markers.
Figure Legend Snippet: Interactions of MBP-UreD with other urease components in vivo. E. coli BL21-Gold(DE3) cells were cotransformed with either pEC002 (encoding MBP-UreD) or pMal-c2x (encoding MBP-LacZα) along with pEC004, pEC005, pEC006, pEC007, pEC008, or pEC009 (encoding UreABC, UreFG, UreABCEFG, UreE, UreF, or UreG, respectively). Soluble cell extracts were analyzed directly by SDS-PAGE (odd-numbered lanes) or subjected to amylose resin chromatography with the proteins eluted by maltose addition and analyzed by SDS-PAGE (even-numbered lanes). (A) MBP-UreD interactions with multiple urease components. (B) MBP-UreD interactions with single urease components. M, molecular mass markers.

Techniques Used: In Vivo, SDS Page, Chromatography

Interactions of MBP-UreD with urease apoprotein. (A) In vivo complex formation. Soluble cell extracts of IPTG-induced E. coli BL21-Gold(DE3)/pEC002 (encoding MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (encoding UreABC) were mixed, incubated at room temperature for 1 h, and chromatographed on amylose resin. Bound proteins were eluted in buffer containing 10 mM maltose and visualized by SDS-PAGE. Lanes: M, molecular mass marker; 1, pEC002 cell extracts; 2, pEC004 cell extracts; 3, coelution of UreABC with MBP-UreD from the amylose resin. (B) In vitro interactions. Purified MBP-UreD (2 μM) was mixed with isolated urease apoprotein (10 μM) in TEB buffer with 25 mM NaCl and, where indicated, cell extracts of E. coli MG1655. Reaction mixtures were incubated at room temperature for 1 h before the mix was subjected to amylose resin chromatography. Bound proteins were eluted with buffer containing 10 mM maltose. Lanes: M, molecular mass marker; 1, purified urease apoprotein; 2, purified MBP-UreD; 3, MBP-UreD plus urease apoprotein; 4, MBP-UreD plus urease apoprotein along with E. coli MG1655 cell extracts; 5, eluted fraction from lane 3; 6, eluted fraction from lane 4.
Figure Legend Snippet: Interactions of MBP-UreD with urease apoprotein. (A) In vivo complex formation. Soluble cell extracts of IPTG-induced E. coli BL21-Gold(DE3)/pEC002 (encoding MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (encoding UreABC) were mixed, incubated at room temperature for 1 h, and chromatographed on amylose resin. Bound proteins were eluted in buffer containing 10 mM maltose and visualized by SDS-PAGE. Lanes: M, molecular mass marker; 1, pEC002 cell extracts; 2, pEC004 cell extracts; 3, coelution of UreABC with MBP-UreD from the amylose resin. (B) In vitro interactions. Purified MBP-UreD (2 μM) was mixed with isolated urease apoprotein (10 μM) in TEB buffer with 25 mM NaCl and, where indicated, cell extracts of E. coli MG1655. Reaction mixtures were incubated at room temperature for 1 h before the mix was subjected to amylose resin chromatography. Bound proteins were eluted with buffer containing 10 mM maltose. Lanes: M, molecular mass marker; 1, purified urease apoprotein; 2, purified MBP-UreD; 3, MBP-UreD plus urease apoprotein; 4, MBP-UreD plus urease apoprotein along with E. coli MG1655 cell extracts; 5, eluted fraction from lane 3; 6, eluted fraction from lane 4.

Techniques Used: In Vivo, Incubation, SDS Page, Marker, In Vitro, Purification, Isolation, Chromatography

4) Product Images from "Cofactor Specificity Engineering of Streptococcus mutans NADH Oxidase 2 for NAD(P)+ Regeneration in Biocatalytic Oxidations"

Article Title: Cofactor Specificity Engineering of Streptococcus mutans NADH Oxidase 2 for NAD(P)+ Regeneration in Biocatalytic Oxidations

Journal: Computational and Structural Biotechnology Journal

doi: 10.5936/csbj.201402005

4-12% Bis-Tris SDS-PAGE gel of cell free extracts of E. coli BL21 (DE3) Gold expressing Sm NOX.
Figure Legend Snippet: 4-12% Bis-Tris SDS-PAGE gel of cell free extracts of E. coli BL21 (DE3) Gold expressing Sm NOX.

Techniques Used: SDS Page, Expressing

Related Articles

Mutagenesis:

Article Title: Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay Pathway
Article Snippet: .. The mutant AcrB proteins were overproduced in E. coli BL21-Gold(DE3) cells (Stratagene), using a plasmid derived from pSPORT1 (Invitrogen). ..

Purification:

Article Title: PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
Article Snippet: .. For the bacterially expressed proteins, purification involved IPTG-induced expression in Escherichia coli BL21 gold (Stratagene). ..

Article Title: The Function of UreB in Klebsiella aerogenes Urease
Article Snippet: .. UreBΔ1-19 was purified from E. coli BL21-Gold(DE3) harboring pUreBΔ1-19 by a process similar to that for UreB. .. In this case, however, the cells were supplemented with 1 mM IPTG and grown for an additional 3 h prior to harvesting by centrifugation.

Incubation:

Article Title: Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein ▿
Article Snippet: .. In order to further investigate the interaction between UreD and urease apoprotein, soluble cell extracts of E. coli BL21-Gold(DE3)/pEC002 (containing MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (containing UreABC) were mixed, incubated at room temperature for 1 h, and subjected to amylose resin pulldown analysis. ..

other:

Article Title: Apoprotein isolation and activation, and vibrational structure of the Helicobacter mustelae iron urease
Article Snippet: To determine whether E. coli BL21-Gold(DE3) cells harboring pEC004 were ureolytic, cells were grown overnight in LB containing chloramphenicol at 50 μg ml−1 with shaking at 37 °C.

Article Title: Functional role of Trp-105 of Enterococcus faecalis azoreductase (AzoA) as resolved by structural and mutational analysis
Article Snippet: E. coli BL21-Gold(DE3)pLysS cells harbouring pAZOA or pAZOA mutants grown on LB-ampicillin-chloramphenicol plate medium were inoculated into a flask containing 20 ml LB-ampicillin-chloramphenicol (50 μg ml−1 of each antibiotic) broth.

Derivative Assay:

Article Title: Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay Pathway
Article Snippet: .. The mutant AcrB proteins were overproduced in E. coli BL21-Gold(DE3) cells (Stratagene), using a plasmid derived from pSPORT1 (Invitrogen). ..

Expressing:

Article Title: PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
Article Snippet: .. For the bacterially expressed proteins, purification involved IPTG-induced expression in Escherichia coli BL21 gold (Stratagene). ..

Plasmid Preparation:

Article Title: Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay Pathway
Article Snippet: .. The mutant AcrB proteins were overproduced in E. coli BL21-Gold(DE3) cells (Stratagene), using a plasmid derived from pSPORT1 (Invitrogen). ..

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    Stratagene e coli bl21 gold
    In vivo interactions of MBP-UreD with (UreABC) 3 , UreB, (UreAC) 3 , and UreBΔ1-19. (A) SDS-PAGE depicting the interactions of MBP-UreD with (UreABC) 3 , UreB, and (UreAC) 3 . E. coli <t>BL21-Gold(DE3)</t> cells were co-transformed with pCDF-MBP-UreD (encoding
    E Coli Bl21 Gold, supplied by Stratagene, used in various techniques. Bioz Stars score: 90/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli bl21 gold/product/Stratagene
    Average 90 stars, based on 42 article reviews
    Price from $9.99 to $1999.99
    e coli bl21 gold - by Bioz Stars, 2020-09
    90/100 stars
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    In vivo interactions of MBP-UreD with (UreABC) 3 , UreB, (UreAC) 3 , and UreBΔ1-19. (A) SDS-PAGE depicting the interactions of MBP-UreD with (UreABC) 3 , UreB, and (UreAC) 3 . E. coli BL21-Gold(DE3) cells were co-transformed with pCDF-MBP-UreD (encoding

    Journal: Biochemistry

    Article Title: The Function of UreB in Klebsiella aerogenes Urease

    doi: 10.1021/bi2011064

    Figure Lengend Snippet: In vivo interactions of MBP-UreD with (UreABC) 3 , UreB, (UreAC) 3 , and UreBΔ1-19. (A) SDS-PAGE depicting the interactions of MBP-UreD with (UreABC) 3 , UreB, and (UreAC) 3 . E. coli BL21-Gold(DE3) cells were co-transformed with pCDF-MBP-UreD (encoding

    Article Snippet: UreBΔ1-19 was purified from E. coli BL21-Gold(DE3) harboring pUreBΔ1-19 by a process similar to that for UreB.

    Techniques: In Vivo, SDS Page, Transformation Assay

    Interactions of MBP-UreD with other urease components in vivo. E. coli BL21-Gold(DE3) cells were cotransformed with either pEC002 (encoding MBP-UreD) or pMal-c2x (encoding MBP-LacZα) along with pEC004, pEC005, pEC006, pEC007, pEC008, or pEC009 (encoding UreABC, UreFG, UreABCEFG, UreE, UreF, or UreG, respectively). Soluble cell extracts were analyzed directly by SDS-PAGE (odd-numbered lanes) or subjected to amylose resin chromatography with the proteins eluted by maltose addition and analyzed by SDS-PAGE (even-numbered lanes). (A) MBP-UreD interactions with multiple urease components. (B) MBP-UreD interactions with single urease components. M, molecular mass markers.

    Journal: Journal of Bacteriology

    Article Title: Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein ▿

    doi: 10.1128/JB.01426-09

    Figure Lengend Snippet: Interactions of MBP-UreD with other urease components in vivo. E. coli BL21-Gold(DE3) cells were cotransformed with either pEC002 (encoding MBP-UreD) or pMal-c2x (encoding MBP-LacZα) along with pEC004, pEC005, pEC006, pEC007, pEC008, or pEC009 (encoding UreABC, UreFG, UreABCEFG, UreE, UreF, or UreG, respectively). Soluble cell extracts were analyzed directly by SDS-PAGE (odd-numbered lanes) or subjected to amylose resin chromatography with the proteins eluted by maltose addition and analyzed by SDS-PAGE (even-numbered lanes). (A) MBP-UreD interactions with multiple urease components. (B) MBP-UreD interactions with single urease components. M, molecular mass markers.

    Article Snippet: In order to further investigate the interaction between UreD and urease apoprotein, soluble cell extracts of E. coli BL21-Gold(DE3)/pEC002 (containing MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (containing UreABC) were mixed, incubated at room temperature for 1 h, and subjected to amylose resin pulldown analysis.

    Techniques: In Vivo, SDS Page, Chromatography

    Interactions of MBP-UreD with urease apoprotein. (A) In vivo complex formation. Soluble cell extracts of IPTG-induced E. coli BL21-Gold(DE3)/pEC002 (encoding MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (encoding UreABC) were mixed, incubated at room temperature for 1 h, and chromatographed on amylose resin. Bound proteins were eluted in buffer containing 10 mM maltose and visualized by SDS-PAGE. Lanes: M, molecular mass marker; 1, pEC002 cell extracts; 2, pEC004 cell extracts; 3, coelution of UreABC with MBP-UreD from the amylose resin. (B) In vitro interactions. Purified MBP-UreD (2 μM) was mixed with isolated urease apoprotein (10 μM) in TEB buffer with 25 mM NaCl and, where indicated, cell extracts of E. coli MG1655. Reaction mixtures were incubated at room temperature for 1 h before the mix was subjected to amylose resin chromatography. Bound proteins were eluted with buffer containing 10 mM maltose. Lanes: M, molecular mass marker; 1, purified urease apoprotein; 2, purified MBP-UreD; 3, MBP-UreD plus urease apoprotein; 4, MBP-UreD plus urease apoprotein along with E. coli MG1655 cell extracts; 5, eluted fraction from lane 3; 6, eluted fraction from lane 4.

    Journal: Journal of Bacteriology

    Article Title: Characterization of the Klebsiella aerogenes Urease Accessory Protein UreD in Fusion with the Maltose Binding Protein ▿

    doi: 10.1128/JB.01426-09

    Figure Lengend Snippet: Interactions of MBP-UreD with urease apoprotein. (A) In vivo complex formation. Soluble cell extracts of IPTG-induced E. coli BL21-Gold(DE3)/pEC002 (encoding MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (encoding UreABC) were mixed, incubated at room temperature for 1 h, and chromatographed on amylose resin. Bound proteins were eluted in buffer containing 10 mM maltose and visualized by SDS-PAGE. Lanes: M, molecular mass marker; 1, pEC002 cell extracts; 2, pEC004 cell extracts; 3, coelution of UreABC with MBP-UreD from the amylose resin. (B) In vitro interactions. Purified MBP-UreD (2 μM) was mixed with isolated urease apoprotein (10 μM) in TEB buffer with 25 mM NaCl and, where indicated, cell extracts of E. coli MG1655. Reaction mixtures were incubated at room temperature for 1 h before the mix was subjected to amylose resin chromatography. Bound proteins were eluted with buffer containing 10 mM maltose. Lanes: M, molecular mass marker; 1, purified urease apoprotein; 2, purified MBP-UreD; 3, MBP-UreD plus urease apoprotein; 4, MBP-UreD plus urease apoprotein along with E. coli MG1655 cell extracts; 5, eluted fraction from lane 3; 6, eluted fraction from lane 4.

    Article Snippet: In order to further investigate the interaction between UreD and urease apoprotein, soluble cell extracts of E. coli BL21-Gold(DE3)/pEC002 (containing MBP-UreD) and E. coli BL21-Gold(DE3)/pEC004 (containing UreABC) were mixed, incubated at room temperature for 1 h, and subjected to amylose resin pulldown analysis.

    Techniques: In Vivo, Incubation, SDS Page, Marker, In Vitro, Purification, Isolation, Chromatography

    Optimization of expression conditions and screening background. (A) Colonies of E . coli BL21 transformed with TN-XXL cloned into the vector pRSETB (exposure time 4s, gain 2x, binning 1). Scale bar, 10 mm (B) Colonies of E . coli XL1 transformed with TN-XXL cloned into pRSETB and imaged under the same conditions. (C) Mean fluorescence intensities ± SD of colonies transformed with TN-XXL in either BL1 or XL1, imaged under identical conditions (n BL21 = 312, n XL1 = 558). (D) ΔR/R ± SD of E . coli colonies expressing TN-XXL cloned into BL21 or XL1 (n BL21 = 19, n XL1 = 15). (E) Auto-fluorescence of agar plate versus white blotting paper imaged under identical conditions with filters used for FRET imaging. Error bars indicate SD. (F) Basal ratio valuesR 0 ± SD of XL1 colonies transformed with the FRET sensor TN-XXL and imaged on agar plate or on filter paper. (n plate = 149 colonies, n blotting paper = 90 colonies) (G) ΔR/R ± SD of the same colonies following calcium application.

    Journal: PLoS ONE

    Article Title: Large Scale Bacterial Colony Screening of Diversified FRET Biosensors

    doi: 10.1371/journal.pone.0119860

    Figure Lengend Snippet: Optimization of expression conditions and screening background. (A) Colonies of E . coli BL21 transformed with TN-XXL cloned into the vector pRSETB (exposure time 4s, gain 2x, binning 1). Scale bar, 10 mm (B) Colonies of E . coli XL1 transformed with TN-XXL cloned into pRSETB and imaged under the same conditions. (C) Mean fluorescence intensities ± SD of colonies transformed with TN-XXL in either BL1 or XL1, imaged under identical conditions (n BL21 = 312, n XL1 = 558). (D) ΔR/R ± SD of E . coli colonies expressing TN-XXL cloned into BL21 or XL1 (n BL21 = 19, n XL1 = 15). (E) Auto-fluorescence of agar plate versus white blotting paper imaged under identical conditions with filters used for FRET imaging. Error bars indicate SD. (F) Basal ratio valuesR 0 ± SD of XL1 colonies transformed with the FRET sensor TN-XXL and imaged on agar plate or on filter paper. (n plate = 149 colonies, n blotting paper = 90 colonies) (G) ΔR/R ± SD of the same colonies following calcium application.

    Article Snippet: Bacterial plate screening Libraries were transformed into E .coli XL1-Blue cells or E .coli BL21-Gold cells (both Stratagene) and plated on LB agar plates containing ampicillin (100 μg/ml) with a desired colony density of ~700–800 colonies per plate.

    Techniques: Expressing, Transformation Assay, Clone Assay, Plasmid Preparation, Fluorescence, Imaging