escherichia coli strain bl21  (Millipore)


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    Structured Review

    Millipore escherichia coli strain bl21
    Escherichia Coli Strain Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 120 article reviews
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    escherichia coli strain bl21 - by Bioz Stars, 2020-05
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    Mutagenesis:

    Article Title: Local and non‐local topological information in the denatured state ensemble of a β‐barrel protein
    Article Snippet: .. The WT* and mutant proteins were isotopically labeled and expressed in Escherichia coli strain BL21(DE3) (Novagen) in M9 minimal media with 13 C‐ d ‐glucose (Cambridge Isotope) and 15 N‐NH4 Cl (Cambridge Isotope). .. Protein expression was induced with 0.4 m M IPTG, and the cells were allowed to grow for 4 h at 37°C.

    Transformation Assay:

    Article Title: The first crystal structure of crustacean ferritin that is a hybrid type of H and L ferritin
    Article Snippet: .. The expression plasmids were transformed into the Escherichia coli strain BL21(DE3) (Novagen). ..

    Expressing:

    Article Title: The first crystal structure of crustacean ferritin that is a hybrid type of H and L ferritin
    Article Snippet: .. The expression plasmids were transformed into the Escherichia coli strain BL21(DE3) (Novagen). ..

    Labeling:

    Article Title: Local and non‐local topological information in the denatured state ensemble of a β‐barrel protein
    Article Snippet: .. The WT* and mutant proteins were isotopically labeled and expressed in Escherichia coli strain BL21(DE3) (Novagen) in M9 minimal media with 13 C‐ d ‐glucose (Cambridge Isotope) and 15 N‐NH4 Cl (Cambridge Isotope). .. Protein expression was induced with 0.4 m M IPTG, and the cells were allowed to grow for 4 h at 37°C.

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  • 94
    Millipore gst prescission protease
    Accessible hydrophobic residues in the predicted coiled coil are critical for Rab binding. (A) Helical wheel projection of a coiled coil predicted for GCC185 residues 1579−1606. Residues in registers “a-f” were predicted by the Paircoil program. Residues at positions “a” and “d” lie in the dimer interface. Boxed residues are candidates for binding interactions with Rab GTPases. (B, C) Effect of alanine substitutions on Rab binding. Reactions contained wild type or mutant <t>GST-C-110</t> (B; 3 μM, C; 2 μM) and 35 S-GTPγS-preloaded GTPases (B; 170 pmol Rab9-His, C; 190 pmol His-Rab6). Data are mean ± SD. (D) Mass determination of untagged <t>RBD-87</t> I1588A/L1595A by multiple angle static light scattering. The gel filtration elution profile of the protein (black line) and molecular mass (grey line) are shown. Polydispersity of the peak was 1.001.
    Gst Prescission Protease, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gst prescission protease/product/Millipore
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    gst prescission protease - by Bioz Stars, 2020-05
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    99
    Millipore e coli strain bl21
    Zymographic detection of the autolytic activity in recombinant His-tagged Atl. Protein extracts from E. coli <t>BL21</t> cells grown with IPTG were used in this study. The protein extract was separated by 12.5% SDS-gel electrophoresis. The SDS gel was impregnated with autoclaved S. aureus RN450 cells. Autolytic activity was detected by renaturing the autolysins by incubation of the gel in 50 mM Tri-HCl buffer, pH 7.5, containing 0.05% Triton X-100. Lane 1: full length His-tagged Atl; lane 2: Atl-1; lane 3: Atl-2; lane 4: Atl-3; lane 5: Atl-4; lane 6: Atl-5; lane 7: Atl-6; lane 8: Atl-7; lane 9: Atl-8.
    E Coli Strain Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 284 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli strain bl21/product/Millipore
    Average 99 stars, based on 284 article reviews
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    e coli strain bl21 - by Bioz Stars, 2020-05
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    Image Search Results


    Accessible hydrophobic residues in the predicted coiled coil are critical for Rab binding. (A) Helical wheel projection of a coiled coil predicted for GCC185 residues 1579−1606. Residues in registers “a-f” were predicted by the Paircoil program. Residues at positions “a” and “d” lie in the dimer interface. Boxed residues are candidates for binding interactions with Rab GTPases. (B, C) Effect of alanine substitutions on Rab binding. Reactions contained wild type or mutant GST-C-110 (B; 3 μM, C; 2 μM) and 35 S-GTPγS-preloaded GTPases (B; 170 pmol Rab9-His, C; 190 pmol His-Rab6). Data are mean ± SD. (D) Mass determination of untagged RBD-87 I1588A/L1595A by multiple angle static light scattering. The gel filtration elution profile of the protein (black line) and molecular mass (grey line) are shown. Polydispersity of the peak was 1.001.

    Journal: Cell

    Article Title: Dual GTPase regulation of the GCC185 Golgin: Communication between adjacent Rab6 and Arl1 binding sites

    doi: 10.1016/j.cell.2007.11.048

    Figure Lengend Snippet: Accessible hydrophobic residues in the predicted coiled coil are critical for Rab binding. (A) Helical wheel projection of a coiled coil predicted for GCC185 residues 1579−1606. Residues in registers “a-f” were predicted by the Paircoil program. Residues at positions “a” and “d” lie in the dimer interface. Boxed residues are candidates for binding interactions with Rab GTPases. (B, C) Effect of alanine substitutions on Rab binding. Reactions contained wild type or mutant GST-C-110 (B; 3 μM, C; 2 μM) and 35 S-GTPγS-preloaded GTPases (B; 170 pmol Rab9-His, C; 190 pmol His-Rab6). Data are mean ± SD. (D) Mass determination of untagged RBD-87 I1588A/L1595A by multiple angle static light scattering. The gel filtration elution profile of the protein (black line) and molecular mass (grey line) are shown. Polydispersity of the peak was 1.001.

    Article Snippet: RBD-87 was then separated from GST, GST-Prescission Protease and glutathione beads over a solid support and concentrated (Amicon Ultra, 5,000 MWCO, Millipore).

    Techniques: Binding Assay, Mutagenesis, Filtration

    Identification of a GCC185 Rab-binding domain. (A) Constructs used to map Rab-GCC185 interactions; numbers represent amino acid residues. The GRIP domain and a Rab binding domain (RBD) are shown. At right: summary of binding to Rab6 or Rab9. (B) GCC185 preferentially binds Rab6-GTP via residues upstream of the GRIP domain. Reactions contained 50 pmol His-Rab6 (left) or 1.2 nmol His-Rab6, or Rab9-His (right) using 35 S-GTPγS or 3 H-GDP-preloaded GTPase and either GST-C110 or GST-RBD-87 (2.8 μM). (C) The GRIP domain is not sufficient for Rab binding. GST-C-110, C-110 Y/A , or C-72 (2 μM) was incubated with 35 S-GTPγS-preloaded GTPases (∼500 pmol) (as in B. except Rab1 and Rab9 were untagged and or ArlQ71L-His was used). Untagged Rab9/1 and His-Rab6 1−174 were employed. (D) Rab6 specifically competes with Rab9 for GCC185 binding. GST-C-110:Rab9 complexes (pair of lanes in the center) were incubated for 3 min with ten fold excess competitor. Rab9-His was detected by immunoblot using a monoclonal anti-Rab9 antibody that did not cross react with Rab6 (see pair of lanes at far left). Lower panel, same as upper panel using indicated amounts of competitor Rab9. Data are mean ± SD.

    Journal: Cell

    Article Title: Dual GTPase regulation of the GCC185 Golgin: Communication between adjacent Rab6 and Arl1 binding sites

    doi: 10.1016/j.cell.2007.11.048

    Figure Lengend Snippet: Identification of a GCC185 Rab-binding domain. (A) Constructs used to map Rab-GCC185 interactions; numbers represent amino acid residues. The GRIP domain and a Rab binding domain (RBD) are shown. At right: summary of binding to Rab6 or Rab9. (B) GCC185 preferentially binds Rab6-GTP via residues upstream of the GRIP domain. Reactions contained 50 pmol His-Rab6 (left) or 1.2 nmol His-Rab6, or Rab9-His (right) using 35 S-GTPγS or 3 H-GDP-preloaded GTPase and either GST-C110 or GST-RBD-87 (2.8 μM). (C) The GRIP domain is not sufficient for Rab binding. GST-C-110, C-110 Y/A , or C-72 (2 μM) was incubated with 35 S-GTPγS-preloaded GTPases (∼500 pmol) (as in B. except Rab1 and Rab9 were untagged and or ArlQ71L-His was used). Untagged Rab9/1 and His-Rab6 1−174 were employed. (D) Rab6 specifically competes with Rab9 for GCC185 binding. GST-C-110:Rab9 complexes (pair of lanes in the center) were incubated for 3 min with ten fold excess competitor. Rab9-His was detected by immunoblot using a monoclonal anti-Rab9 antibody that did not cross react with Rab6 (see pair of lanes at far left). Lower panel, same as upper panel using indicated amounts of competitor Rab9. Data are mean ± SD.

    Article Snippet: RBD-87 was then separated from GST, GST-Prescission Protease and glutathione beads over a solid support and concentrated (Amicon Ultra, 5,000 MWCO, Millipore).

    Techniques: Binding Assay, Construct, Incubation

    Zymographic detection of the autolytic activity in recombinant His-tagged Atl. Protein extracts from E. coli BL21 cells grown with IPTG were used in this study. The protein extract was separated by 12.5% SDS-gel electrophoresis. The SDS gel was impregnated with autoclaved S. aureus RN450 cells. Autolytic activity was detected by renaturing the autolysins by incubation of the gel in 50 mM Tri-HCl buffer, pH 7.5, containing 0.05% Triton X-100. Lane 1: full length His-tagged Atl; lane 2: Atl-1; lane 3: Atl-2; lane 4: Atl-3; lane 5: Atl-4; lane 6: Atl-5; lane 7: Atl-6; lane 8: Atl-7; lane 9: Atl-8.

    Journal: International Journal of Microbiology

    Article Title: High Level Expression and Purification of Atl, the Major Autolytic Protein of Staphylococcus aureus

    doi: 10.1155/2014/615965

    Figure Lengend Snippet: Zymographic detection of the autolytic activity in recombinant His-tagged Atl. Protein extracts from E. coli BL21 cells grown with IPTG were used in this study. The protein extract was separated by 12.5% SDS-gel electrophoresis. The SDS gel was impregnated with autoclaved S. aureus RN450 cells. Autolytic activity was detected by renaturing the autolysins by incubation of the gel in 50 mM Tri-HCl buffer, pH 7.5, containing 0.05% Triton X-100. Lane 1: full length His-tagged Atl; lane 2: Atl-1; lane 3: Atl-2; lane 4: Atl-3; lane 5: Atl-4; lane 6: Atl-5; lane 7: Atl-6; lane 8: Atl-7; lane 9: Atl-8.

    Article Snippet: In addition, E. coli strain BL21 (EMD Millipore) was used for all protein expression studies.

    Techniques: Activity Assay, Recombinant, SDS-Gel, Electrophoresis, Incubation

    Coomassie stained gels showing purity of recombinant His-tagged Atl. Recombinant Atl and Atl-1 proteins were overproduced in E. coli and purified as described in the Materials and Methods section. Lane M: standard protein markers; lanes 1 and 2: protein extract from E. coli BL21 cells transformed with plasmids pRSETA- atl and grown without and with IPTG, respectively; lane 3: purified His-tagged Atl; lanes 4 and 5: protein extract from E. coli BL21 cells transformed with plasmids pRSETA- atl1 and grown without and with IPTG, respectively; lane 6: purified His-tagged Atl-1.

    Journal: International Journal of Microbiology

    Article Title: High Level Expression and Purification of Atl, the Major Autolytic Protein of Staphylococcus aureus

    doi: 10.1155/2014/615965

    Figure Lengend Snippet: Coomassie stained gels showing purity of recombinant His-tagged Atl. Recombinant Atl and Atl-1 proteins were overproduced in E. coli and purified as described in the Materials and Methods section. Lane M: standard protein markers; lanes 1 and 2: protein extract from E. coli BL21 cells transformed with plasmids pRSETA- atl and grown without and with IPTG, respectively; lane 3: purified His-tagged Atl; lanes 4 and 5: protein extract from E. coli BL21 cells transformed with plasmids pRSETA- atl1 and grown without and with IPTG, respectively; lane 6: purified His-tagged Atl-1.

    Article Snippet: In addition, E. coli strain BL21 (EMD Millipore) was used for all protein expression studies.

    Techniques: Staining, Recombinant, Purification, Transformation Assay

    Zymographic detection of the autolytic activity in purified recombinant His-tagged Atl. Lane 1: total protein extract from S. aureus cells. Lanes 2 and 4: purified His-tagged Atl and Atl-1, respectively; lanes 3 and 5: protein extract from E. coli BL21 cells transformed with plasmids pRSETA- atl or pRSETA- atl1 and grown with IPTG, respectively.

    Journal: International Journal of Microbiology

    Article Title: High Level Expression and Purification of Atl, the Major Autolytic Protein of Staphylococcus aureus

    doi: 10.1155/2014/615965

    Figure Lengend Snippet: Zymographic detection of the autolytic activity in purified recombinant His-tagged Atl. Lane 1: total protein extract from S. aureus cells. Lanes 2 and 4: purified His-tagged Atl and Atl-1, respectively; lanes 3 and 5: protein extract from E. coli BL21 cells transformed with plasmids pRSETA- atl or pRSETA- atl1 and grown with IPTG, respectively.

    Article Snippet: In addition, E. coli strain BL21 (EMD Millipore) was used for all protein expression studies.

    Techniques: Activity Assay, Purification, Recombinant, Transformation Assay

    Coomassie stained gels demonstrating overexpression of recombinant Atl. The 12.5% SDS-PAGE contains protein extracts of E. coli BL21 cells with pRSETA plasmids expressing either full length or truncated Atl proteins. The odd number labels are cells grown without IPTG and the even number labels are the cells grown with IPTG. Lane M: standard protein markers; lanes 1 and 2 - Atl (full length His-tagged Atl); lanes 3 and 4: Atl-1; lanes 5 and 6: Atl-2; lanes 7 and 8: Atl-3; lanes 9 and 10: Atl-4; lanes 11 and 12: Atl-6; lanes 13 and 14: Atl-5; lanes 15 and 16: Atl-7; lanes 17 and 18: Atl-8. The Atl number suffixes are indicated in Table 1 .

    Journal: International Journal of Microbiology

    Article Title: High Level Expression and Purification of Atl, the Major Autolytic Protein of Staphylococcus aureus

    doi: 10.1155/2014/615965

    Figure Lengend Snippet: Coomassie stained gels demonstrating overexpression of recombinant Atl. The 12.5% SDS-PAGE contains protein extracts of E. coli BL21 cells with pRSETA plasmids expressing either full length or truncated Atl proteins. The odd number labels are cells grown without IPTG and the even number labels are the cells grown with IPTG. Lane M: standard protein markers; lanes 1 and 2 - Atl (full length His-tagged Atl); lanes 3 and 4: Atl-1; lanes 5 and 6: Atl-2; lanes 7 and 8: Atl-3; lanes 9 and 10: Atl-4; lanes 11 and 12: Atl-6; lanes 13 and 14: Atl-5; lanes 15 and 16: Atl-7; lanes 17 and 18: Atl-8. The Atl number suffixes are indicated in Table 1 .

    Article Snippet: In addition, E. coli strain BL21 (EMD Millipore) was used for all protein expression studies.

    Techniques: Staining, Over Expression, Recombinant, SDS Page, Expressing

    Binding of LsrB to endogenous AI-2. Purified LsrB (BL21) and LsrB (BL21∆luxS) proteins (5 mg/ml) were incubated for 10 min at 37, 50 and 60 °C to release endogenous AI-2, respectively. After incubation, the LsrB proteins were removed by ultrafiltration (10,000-Da cut-off; EMD Millipore), and the filtered reaction products were tested for AI-2 activity using a V. harveyi BB170 bioassay. The extent of LsrB binding to endogenous AI-2 was evaluated using an AI-2 assay, which showed that recombinant LsrB (BL21) bound to endogenous AI-2 (produced by wild-type strain BL21) and was released from LsrB (BL21) at 50 or 60 °C, respectively ( a ). However, since the luxS mutant BL21∆luxS did not produce endogenous AI-2, no AI-2 could be released from the recombinant LsrB (BL21∆luxS) ( b ). Moreover, the recombinant LuxS protein, which was expressed in strain BL21 (pColdTF-lsrB) as a negative control, also showed no AI-2 binding activity ( c ). AI-2 (10 μM) was used as a positive control

    Journal: AMB Express

    Article Title: LsrB-based and temperature-dependent identification of bacterial AI-2 receptor

    doi: 10.1186/s13568-017-0486-y

    Figure Lengend Snippet: Binding of LsrB to endogenous AI-2. Purified LsrB (BL21) and LsrB (BL21∆luxS) proteins (5 mg/ml) were incubated for 10 min at 37, 50 and 60 °C to release endogenous AI-2, respectively. After incubation, the LsrB proteins were removed by ultrafiltration (10,000-Da cut-off; EMD Millipore), and the filtered reaction products were tested for AI-2 activity using a V. harveyi BB170 bioassay. The extent of LsrB binding to endogenous AI-2 was evaluated using an AI-2 assay, which showed that recombinant LsrB (BL21) bound to endogenous AI-2 (produced by wild-type strain BL21) and was released from LsrB (BL21) at 50 or 60 °C, respectively ( a ). However, since the luxS mutant BL21∆luxS did not produce endogenous AI-2, no AI-2 could be released from the recombinant LsrB (BL21∆luxS) ( b ). Moreover, the recombinant LuxS protein, which was expressed in strain BL21 (pColdTF-lsrB) as a negative control, also showed no AI-2 binding activity ( c ). AI-2 (10 μM) was used as a positive control

    Article Snippet: Cell-free culture fluid (CF) was prepared as follows: E. coli strains BL21 (DE3), BL21∆luxS and DH5a were grown in LB at 37 °C, and then pelleted by centrifugation at 12,000g at 4 °C for 10 min. Then, the resulting supernatants were filtered through a 0.22-μm filter (EMD Millipore, Bedford, MA, USA) to obtain CF samples.

    Techniques: Binding Assay, Purification, Incubation, Activity Assay, Recombinant, Produced, Mutagenesis, Negative Control, Positive Control

    Schematic chart of strategy for binding of LsrB to endogenous AI-2 or exogenous AI-2. The extent of LsrB binding to endogenous AI-2 was evaluated using an AI-2 assay, which showed that recombinant LsrB (BL21) bound to endogenous AI-2 (produced by wild-type strain BL21) and was released from LsrB (BL21) at 50 or 60 °C. However, since the luxS mutant BL21∆luxS did not produce endogenous AI-2, no AI-2 could be released from the recombinant LsrB (BL21∆luxS). The combination of endogenous AI-2 produced by BL21 (DE3), which is known to interfere with the binding of AI-2 to LsrB (BL21), resulted in the loss in the ability of LsrB (BL21) to bind to exogenous AI-2. Hence, the BL21 (DE3) luxS mutant, which was incapable of producing endogenous AI-2, but could bind to exogenous AI-2

    Journal: AMB Express

    Article Title: LsrB-based and temperature-dependent identification of bacterial AI-2 receptor

    doi: 10.1186/s13568-017-0486-y

    Figure Lengend Snippet: Schematic chart of strategy for binding of LsrB to endogenous AI-2 or exogenous AI-2. The extent of LsrB binding to endogenous AI-2 was evaluated using an AI-2 assay, which showed that recombinant LsrB (BL21) bound to endogenous AI-2 (produced by wild-type strain BL21) and was released from LsrB (BL21) at 50 or 60 °C. However, since the luxS mutant BL21∆luxS did not produce endogenous AI-2, no AI-2 could be released from the recombinant LsrB (BL21∆luxS). The combination of endogenous AI-2 produced by BL21 (DE3), which is known to interfere with the binding of AI-2 to LsrB (BL21), resulted in the loss in the ability of LsrB (BL21) to bind to exogenous AI-2. Hence, the BL21 (DE3) luxS mutant, which was incapable of producing endogenous AI-2, but could bind to exogenous AI-2

    Article Snippet: Cell-free culture fluid (CF) was prepared as follows: E. coli strains BL21 (DE3), BL21∆luxS and DH5a were grown in LB at 37 °C, and then pelleted by centrifugation at 12,000g at 4 °C for 10 min. Then, the resulting supernatants were filtered through a 0.22-μm filter (EMD Millipore, Bedford, MA, USA) to obtain CF samples.

    Techniques: Binding Assay, Recombinant, Produced, Mutagenesis

    Identification of the luxS mutant BL21∆ luxS. a Schematic chart of strategy for producing the BL21 luxS deletion mutant. The luxS was deleted by replacing the partial gene sequence of luxS with kanamycin resistance cassette at Sal I cleavage sites. The primers used for the confirmation of the luxS deletion are also indicated. b Identification of the luxS mutant BL21∆ luxS. Lane M: DL 2000 DNA marker (D501A; Takara); lane 1: the wild-type strain BL21 showed a 2519-bp PCR product using primers LuxS-OutF/LuxS-OutR; lane 2: the mutant BL21∆ luxS with cure of the kanamycin resistance cassette showed a 2209-bp PCR product using primers LuxS-OutF/LuxS-OutR; lane 3: negative control; lane 4: the wild-type strain DE17 showed a 307-bp PCR product using primers LuxS-inF/LuxS-inR; lane 5: the mutant DE17∆ pfs showed no PCR products using primers LuxS-inF/LuxS-inR; lane 6: negative control

    Journal: AMB Express

    Article Title: LsrB-based and temperature-dependent identification of bacterial AI-2 receptor

    doi: 10.1186/s13568-017-0486-y

    Figure Lengend Snippet: Identification of the luxS mutant BL21∆ luxS. a Schematic chart of strategy for producing the BL21 luxS deletion mutant. The luxS was deleted by replacing the partial gene sequence of luxS with kanamycin resistance cassette at Sal I cleavage sites. The primers used for the confirmation of the luxS deletion are also indicated. b Identification of the luxS mutant BL21∆ luxS. Lane M: DL 2000 DNA marker (D501A; Takara); lane 1: the wild-type strain BL21 showed a 2519-bp PCR product using primers LuxS-OutF/LuxS-OutR; lane 2: the mutant BL21∆ luxS with cure of the kanamycin resistance cassette showed a 2209-bp PCR product using primers LuxS-OutF/LuxS-OutR; lane 3: negative control; lane 4: the wild-type strain DE17 showed a 307-bp PCR product using primers LuxS-inF/LuxS-inR; lane 5: the mutant DE17∆ pfs showed no PCR products using primers LuxS-inF/LuxS-inR; lane 6: negative control

    Article Snippet: Cell-free culture fluid (CF) was prepared as follows: E. coli strains BL21 (DE3), BL21∆luxS and DH5a were grown in LB at 37 °C, and then pelleted by centrifugation at 12,000g at 4 °C for 10 min. Then, the resulting supernatants were filtered through a 0.22-μm filter (EMD Millipore, Bedford, MA, USA) to obtain CF samples.

    Techniques: Mutagenesis, Sequencing, Marker, Polymerase Chain Reaction, Negative Control

    The AI-2 activity in BL21∆luxS. The wild strain BL21 secretes AI-2-like molecules, and can induce V . harveyi BB170 bioluminescence, whereas no bioluminescence induction was observed for the mutant BL21∆ luxS . V . harveyi BB152 served as a positive control and E. coli DH5α as a negative control. The figure represents the means of the results from three independent experiments. The error bars indicate standard deviations

    Journal: AMB Express

    Article Title: LsrB-based and temperature-dependent identification of bacterial AI-2 receptor

    doi: 10.1186/s13568-017-0486-y

    Figure Lengend Snippet: The AI-2 activity in BL21∆luxS. The wild strain BL21 secretes AI-2-like molecules, and can induce V . harveyi BB170 bioluminescence, whereas no bioluminescence induction was observed for the mutant BL21∆ luxS . V . harveyi BB152 served as a positive control and E. coli DH5α as a negative control. The figure represents the means of the results from three independent experiments. The error bars indicate standard deviations

    Article Snippet: Cell-free culture fluid (CF) was prepared as follows: E. coli strains BL21 (DE3), BL21∆luxS and DH5a were grown in LB at 37 °C, and then pelleted by centrifugation at 12,000g at 4 °C for 10 min. Then, the resulting supernatants were filtered through a 0.22-μm filter (EMD Millipore, Bedford, MA, USA) to obtain CF samples.

    Techniques: Activity Assay, Mutagenesis, Positive Control, Negative Control