Structured Review

Stratagene bl21
SDS-PAGE stained with Coomassie (A) and western blot with mAb Tg621 (B). <t>BL21(pET-RPP):</t> BL21 clone transformed with pET-RPP plasmid, BL21(pET-RPP)i: induced by IPTG, Purified rRPP: purified recombinant RPP through Ni-NTA column, and TgRPP: naive RPP of tachyzoites, respectively. Numerals on the left indicate molecular mass in kDa.
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Images

1) Product Images from "Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients"

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients

Journal: The Korean Journal of Parasitology

doi: 10.3347/kjp.2003.41.2.89

SDS-PAGE stained with Coomassie (A) and western blot with mAb Tg621 (B). BL21(pET-RPP): BL21 clone transformed with pET-RPP plasmid, BL21(pET-RPP)i: induced by IPTG, Purified rRPP: purified recombinant RPP through Ni-NTA column, and TgRPP: naive RPP of tachyzoites, respectively. Numerals on the left indicate molecular mass in kDa.
Figure Legend Snippet: SDS-PAGE stained with Coomassie (A) and western blot with mAb Tg621 (B). BL21(pET-RPP): BL21 clone transformed with pET-RPP plasmid, BL21(pET-RPP)i: induced by IPTG, Purified rRPP: purified recombinant RPP through Ni-NTA column, and TgRPP: naive RPP of tachyzoites, respectively. Numerals on the left indicate molecular mass in kDa.

Techniques Used: SDS Page, Staining, Western Blot, Transformation Assay, Positron Emission Tomography, Plasmid Preparation, Purification, Recombinant

2) Product Images from "Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism"

Article Title: Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism

Journal: The EMBO Journal

doi: 10.1038/sj.emboj.7601638

Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.
Figure Legend Snippet: Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.

Techniques Used: Transformation Assay, Plasmid Preparation, Mutagenesis, Western Blot

3) Product Images from "Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism"

Article Title: Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism

Journal: The EMBO Journal

doi: 10.1038/sj.emboj.7601638

Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.
Figure Legend Snippet: Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.

Techniques Used: Transformation Assay, Plasmid Preparation, Mutagenesis, Western Blot

4) Product Images from "Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism"

Article Title: Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism

Journal: The EMBO Journal

doi: 10.1038/sj.emboj.7601638

Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.
Figure Legend Snippet: Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.

Techniques Used: Transformation Assay, Plasmid Preparation, Mutagenesis, Western Blot

5) Product Images from "Enhanced fluorescent properties of an OmpT site deleted mutant of Green Fluorescent Protein"

Article Title: Enhanced fluorescent properties of an OmpT site deleted mutant of Green Fluorescent Protein

Journal: Microbial Cell Factories

doi: 10.1186/1475-2859-9-26

SDS-PAGE of GFP expression of GFP WT and SDM II in BL21, JM109 and LE392 at 30°C and 37°C . Panels A, B and C represent GFP expression in BL21, JM109 and LE392 cells respectively. M: Medium molecular weight marker (14-97 kDa); lanes 1 and 2: GFP WT expression at 30°C and 37°C respectively; lanes 3 and 4: SDM II expression at 30°C and 37°C respectively.
Figure Legend Snippet: SDS-PAGE of GFP expression of GFP WT and SDM II in BL21, JM109 and LE392 at 30°C and 37°C . Panels A, B and C represent GFP expression in BL21, JM109 and LE392 cells respectively. M: Medium molecular weight marker (14-97 kDa); lanes 1 and 2: GFP WT expression at 30°C and 37°C respectively; lanes 3 and 4: SDM II expression at 30°C and 37°C respectively.

Techniques Used: SDS Page, Expressing, Molecular Weight, Marker

Western blot of GFP expressed from WT and SDM II clones . M: Medium molecular weight marker 97-14 kDa); lane 1: Supernatant of WT GFP expressed from JM 109; lane 2: Supernatant of GFP SDM II expressed from JM 109 cells; lanes 3 and 4: WT GFP and SDM II mutant expressed in BL21 cells respectively. The upper arrow shows the intact GFP (29 kDa) while the lower arrow shows the degraded form of GFP (of
Figure Legend Snippet: Western blot of GFP expressed from WT and SDM II clones . M: Medium molecular weight marker 97-14 kDa); lane 1: Supernatant of WT GFP expressed from JM 109; lane 2: Supernatant of GFP SDM II expressed from JM 109 cells; lanes 3 and 4: WT GFP and SDM II mutant expressed in BL21 cells respectively. The upper arrow shows the intact GFP (29 kDa) while the lower arrow shows the degraded form of GFP (of

Techniques Used: Western Blot, Clone Assay, Molecular Weight, Marker, Mutagenesis

GFP expression and activity in two different types of E. coli hosts . (A) GFP expression from pBAD24M-GFPuv clone at 37°C. Lane 1: Protein molecular weight marker (14 to 97 kDa); lane 2, GFP expression in DH5α cells; lane 3, GFP expression in BL21 cells. (B) GFP fluorescence units of pBAD24M-GFPuv at 37°C. Sample 1, pBAD24M-GFPuv in DH5α cells; Sample 2, pBAD24M-pGFPuv in BL21 cells.
Figure Legend Snippet: GFP expression and activity in two different types of E. coli hosts . (A) GFP expression from pBAD24M-GFPuv clone at 37°C. Lane 1: Protein molecular weight marker (14 to 97 kDa); lane 2, GFP expression in DH5α cells; lane 3, GFP expression in BL21 cells. (B) GFP fluorescence units of pBAD24M-GFPuv at 37°C. Sample 1, pBAD24M-GFPuv in DH5α cells; Sample 2, pBAD24M-pGFPuv in BL21 cells.

Techniques Used: Expressing, Activity Assay, Molecular Weight, Marker, Fluorescence

Fluorescence data of GFP WT and SDM II in BL21, DH5α, JM109 and LE392 at 37°C . The relative fluorescence values with ± SEM are presented with the fluorescence of GFP obtained in BL21 defined as 100 (arbitrary unit). Sample 1: BL21; sample 2: DH5α; sample 3: JM109; sample 4: LE392. Filled bars represent WT while the empty bars represent SDM II GFP mutant.
Figure Legend Snippet: Fluorescence data of GFP WT and SDM II in BL21, DH5α, JM109 and LE392 at 37°C . The relative fluorescence values with ± SEM are presented with the fluorescence of GFP obtained in BL21 defined as 100 (arbitrary unit). Sample 1: BL21; sample 2: DH5α; sample 3: JM109; sample 4: LE392. Filled bars represent WT while the empty bars represent SDM II GFP mutant.

Techniques Used: Fluorescence, Mutagenesis

6) Product Images from "High yield production of pigeon circovirus capsid protein in the E. coli by evaluating the key parameters needed for protein expression"

Article Title: High yield production of pigeon circovirus capsid protein in the E. coli by evaluating the key parameters needed for protein expression

Journal: BMC Veterinary Research

doi: 10.1186/1746-6148-10-115

Effect of fusion tags, E. coli strains and rare codon replacement on recombinant PiCV capsid protein expression. The three expression plasmids containing wild-type PiCV capsid gene were expressed in E. coli strains BL21 (DE3), BL21 (DE3)-pLysS and BL21 (DE3)-CodonPlus-RIPL. Furthermore, similar plasmids but containing the codon-optimized PiCV capsid gene were also expressed in BL21 (DE3) and BL21 (DE3)-pLysS. All examined recombinant PiCV capsid proteins were analyzed by SDS-PAGE and Western-blotting. Anti-6xHis tag monoclonal antibody was used to recognize the 6xHis-tagged (A) and Trx-tagged (C) Cap proteins. Anti-GST monoclonal antibody was used for detecting GST-tagged (B) Cap proteins. Lane M, pre-stained protein marker; lane 1, 3, 5, 7 and 9, before IPTG induction; lane 2, 4, 6, 8 and 10, after IPTG induction for 4 hrs cultivation. The solid triangle pinpoints the expressed Cap protein.
Figure Legend Snippet: Effect of fusion tags, E. coli strains and rare codon replacement on recombinant PiCV capsid protein expression. The three expression plasmids containing wild-type PiCV capsid gene were expressed in E. coli strains BL21 (DE3), BL21 (DE3)-pLysS and BL21 (DE3)-CodonPlus-RIPL. Furthermore, similar plasmids but containing the codon-optimized PiCV capsid gene were also expressed in BL21 (DE3) and BL21 (DE3)-pLysS. All examined recombinant PiCV capsid proteins were analyzed by SDS-PAGE and Western-blotting. Anti-6xHis tag monoclonal antibody was used to recognize the 6xHis-tagged (A) and Trx-tagged (C) Cap proteins. Anti-GST monoclonal antibody was used for detecting GST-tagged (B) Cap proteins. Lane M, pre-stained protein marker; lane 1, 3, 5, 7 and 9, before IPTG induction; lane 2, 4, 6, 8 and 10, after IPTG induction for 4 hrs cultivation. The solid triangle pinpoints the expressed Cap protein.

Techniques Used: Recombinant, Expressing, SDS Page, Western Blot, Staining, Marker

Growth kinetics and production profiles of recombinant PiCV capsid protein (Cap) in different E. coli strains. (A) The growth and protein production profiles of the three recombinant E. coli strains expressing either the GST-Cap or GST-Cap opt protein. Two strains, BL21 (DE3) and BL21 (DE3)-pLysS expressing GST-Cap opt , and one GST-Cap expressing strain BL21 (DE3)-CodonPlus-RIPL were used in this study post-induction. (B) Growth and protein production profiles of four recombinant E. coli strains expressing Trx-His-Cap or Trx-His-Cap opt protein. Two E. coli strains, BL21 (DE3) and BL21 (DE3)-pLysS were used to express Trx-His-Cap opt , and other two recombinant E. coli strains, BL21 (DE3)-CodonPlus-RIPL and BL21 (DE3)-pLysS were used to express Trx-His-Cap. Similar tests to those described above were used to detect the time course of protein expression after IPTG induction.
Figure Legend Snippet: Growth kinetics and production profiles of recombinant PiCV capsid protein (Cap) in different E. coli strains. (A) The growth and protein production profiles of the three recombinant E. coli strains expressing either the GST-Cap or GST-Cap opt protein. Two strains, BL21 (DE3) and BL21 (DE3)-pLysS expressing GST-Cap opt , and one GST-Cap expressing strain BL21 (DE3)-CodonPlus-RIPL were used in this study post-induction. (B) Growth and protein production profiles of four recombinant E. coli strains expressing Trx-His-Cap or Trx-His-Cap opt protein. Two E. coli strains, BL21 (DE3) and BL21 (DE3)-pLysS were used to express Trx-His-Cap opt , and other two recombinant E. coli strains, BL21 (DE3)-CodonPlus-RIPL and BL21 (DE3)-pLysS were used to express Trx-His-Cap. Similar tests to those described above were used to detect the time course of protein expression after IPTG induction.

Techniques Used: Recombinant, Expressing

The solubility of recombinant GST-Cap opt and Trx-His-Cap opt protein. The two proteins were expressed by E. coli strain BL21 (DE3)-pLysS transformed pGST-Cap opt and pTrx-His-Cap opt respectively. SDS-PAGE (A) was used to analyze the protein distribution pattern of suspension fraction and the pellet fraction. The soluble percent of two recombinant proteins was determined by measuring the intensity of target protein bands on coomassie blue-strained gels (B) . Lane M, pre-stained protein marker; lane I, total protein-expressed cell lysate; lane S, suspension fraction from centrifugal protein-expressed cell lysate; lane P, pellet fraction from centrifugal protein-expressed cell lysate. The solid triangle pinpoints the expressed Cap opt protein.
Figure Legend Snippet: The solubility of recombinant GST-Cap opt and Trx-His-Cap opt protein. The two proteins were expressed by E. coli strain BL21 (DE3)-pLysS transformed pGST-Cap opt and pTrx-His-Cap opt respectively. SDS-PAGE (A) was used to analyze the protein distribution pattern of suspension fraction and the pellet fraction. The soluble percent of two recombinant proteins was determined by measuring the intensity of target protein bands on coomassie blue-strained gels (B) . Lane M, pre-stained protein marker; lane I, total protein-expressed cell lysate; lane S, suspension fraction from centrifugal protein-expressed cell lysate; lane P, pellet fraction from centrifugal protein-expressed cell lysate. The solid triangle pinpoints the expressed Cap opt protein.

Techniques Used: Solubility, Recombinant, Transformation Assay, SDS Page, Staining, Marker

7) Product Images from "Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients"

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients

Journal: The Korean Journal of Parasitology

doi: 10.3347/kjp.2003.41.2.89

SDS-PAGE stained with Coomassie (A) and western blot with mAb Tg621 (B). BL21(pET-RPP): BL21 clone transformed with pET-RPP plasmid, BL21(pET-RPP)i: induced by IPTG, Purified rRPP: purified recombinant RPP through Ni-NTA column, and TgRPP: naive RPP of tachyzoites, respectively. Numerals on the left indicate molecular mass in kDa.
Figure Legend Snippet: SDS-PAGE stained with Coomassie (A) and western blot with mAb Tg621 (B). BL21(pET-RPP): BL21 clone transformed with pET-RPP plasmid, BL21(pET-RPP)i: induced by IPTG, Purified rRPP: purified recombinant RPP through Ni-NTA column, and TgRPP: naive RPP of tachyzoites, respectively. Numerals on the left indicate molecular mass in kDa.

Techniques Used: SDS Page, Staining, Western Blot, Transformation Assay, Positron Emission Tomography, Plasmid Preparation, Purification, Recombinant

8) Product Images from "A New Amidohydrolase from Bordetella or Alcaligenes Strain FB188 with Similarities to Histone Deacetylases"

Article Title: A New Amidohydrolase from Bordetella or Alcaligenes Strain FB188 with Similarities to Histone Deacetylases

Journal: Journal of Bacteriology

doi: 10.1128/JB.186.8.2328-2339.2004

SDS gel electrophoretic analysis of cell lysates and purified enzyme fractions. (A) Native FB188 HDAH purified from Bordetella/Alcaligenes strain FB188 (DSM 11172). Lane 1, protein marker (purified FB188 HDAH prior to amino acid sequence analysis). (B) FB188 HDAH purified by IMAC from E. coli BL21 harboring pQEB-AH-NHis. A benchmark prestained protein ladder (Gibco-Life Science, Karlsruhe, Germany) (lane 1), crude cell extract (lane 2), and purified protein (lane 3) were fractionated on an SDS-10% polyacrylamide gel. Protein bands were visualized by Coomassie staining. (C) Western blotting using the anti-AHFB188 antibody (lanes are as described for panel B). (D) Western blot analysis of FB188 crude cell extract with anti-AHFB188 antibody. Lane 1, benchmark prestained protein ladder; lane 2, purified recombinant FB188 HDAH; lane 3, FB188 cell extract; lane 4, E. coli XL1-Blue cell extract.
Figure Legend Snippet: SDS gel electrophoretic analysis of cell lysates and purified enzyme fractions. (A) Native FB188 HDAH purified from Bordetella/Alcaligenes strain FB188 (DSM 11172). Lane 1, protein marker (purified FB188 HDAH prior to amino acid sequence analysis). (B) FB188 HDAH purified by IMAC from E. coli BL21 harboring pQEB-AH-NHis. A benchmark prestained protein ladder (Gibco-Life Science, Karlsruhe, Germany) (lane 1), crude cell extract (lane 2), and purified protein (lane 3) were fractionated on an SDS-10% polyacrylamide gel. Protein bands were visualized by Coomassie staining. (C) Western blotting using the anti-AHFB188 antibody (lanes are as described for panel B). (D) Western blot analysis of FB188 crude cell extract with anti-AHFB188 antibody. Lane 1, benchmark prestained protein ladder; lane 2, purified recombinant FB188 HDAH; lane 3, FB188 cell extract; lane 4, E. coli XL1-Blue cell extract.

Techniques Used: SDS-Gel, Purification, Marker, Sequencing, Staining, Western Blot, Recombinant

9) Product Images from "Peptide Deformylase as an Antibacterial Drug Target: Target Validation and Resistance Development"

Article Title: Peptide Deformylase as an Antibacterial Drug Target: Target Validation and Resistance Development

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.45.4.1058-1064.2001

Counteracting effect of overexpressing PDF from different species on growth inhibition by Ro 66-0376. E. coli BL21 transformed with the indicated plasmids was grown to an OD 578 of 0.05 and distributed into 96-well plates. Increasing amounts of IPTG (as indicated) were used to induce the expression of the PDFs, and increasing amounts of the inhibitor Ro 66-0376 were added. The OD 595 was measured after 5 h of incubation. The E. coli strain harboring vector pET-3a is shown as the control (noninduced). Conc., concentration.
Figure Legend Snippet: Counteracting effect of overexpressing PDF from different species on growth inhibition by Ro 66-0376. E. coli BL21 transformed with the indicated plasmids was grown to an OD 578 of 0.05 and distributed into 96-well plates. Increasing amounts of IPTG (as indicated) were used to induce the expression of the PDFs, and increasing amounts of the inhibitor Ro 66-0376 were added. The OD 595 was measured after 5 h of incubation. The E. coli strain harboring vector pET-3a is shown as the control (noninduced). Conc., concentration.

Techniques Used: Inhibition, Transformation Assay, Expressing, Incubation, Plasmid Preparation, Positron Emission Tomography, Concentration Assay

10) Product Images from "High yield production of pigeon circovirus capsid protein in the E. coli by evaluating the key parameters needed for protein expression"

Article Title: High yield production of pigeon circovirus capsid protein in the E. coli by evaluating the key parameters needed for protein expression

Journal: BMC Veterinary Research

doi: 10.1186/1746-6148-10-115

Effect of fusion tags, E. coli strains and rare codon replacement on recombinant PiCV capsid protein expression. The three expression plasmids containing wild-type PiCV capsid gene were expressed in E. coli strains BL21 (DE3), BL21 (DE3)-pLysS and BL21 (DE3)-CodonPlus-RIPL. Furthermore, similar plasmids but containing the codon-optimized PiCV capsid gene were also expressed in BL21 (DE3) and BL21 (DE3)-pLysS. All examined recombinant PiCV capsid proteins were analyzed by SDS-PAGE and Western-blotting. Anti-6xHis tag monoclonal antibody was used to recognize the 6xHis-tagged (A) and Trx-tagged (C) Cap proteins. Anti-GST monoclonal antibody was used for detecting GST-tagged (B) Cap proteins. Lane M, pre-stained protein marker; lane 1, 3, 5, 7 and 9, before IPTG induction; lane 2, 4, 6, 8 and 10, after IPTG induction for 4 hrs cultivation. The solid triangle pinpoints the expressed Cap protein.
Figure Legend Snippet: Effect of fusion tags, E. coli strains and rare codon replacement on recombinant PiCV capsid protein expression. The three expression plasmids containing wild-type PiCV capsid gene were expressed in E. coli strains BL21 (DE3), BL21 (DE3)-pLysS and BL21 (DE3)-CodonPlus-RIPL. Furthermore, similar plasmids but containing the codon-optimized PiCV capsid gene were also expressed in BL21 (DE3) and BL21 (DE3)-pLysS. All examined recombinant PiCV capsid proteins were analyzed by SDS-PAGE and Western-blotting. Anti-6xHis tag monoclonal antibody was used to recognize the 6xHis-tagged (A) and Trx-tagged (C) Cap proteins. Anti-GST monoclonal antibody was used for detecting GST-tagged (B) Cap proteins. Lane M, pre-stained protein marker; lane 1, 3, 5, 7 and 9, before IPTG induction; lane 2, 4, 6, 8 and 10, after IPTG induction for 4 hrs cultivation. The solid triangle pinpoints the expressed Cap protein.

Techniques Used: Recombinant, Expressing, SDS Page, Western Blot, Staining, Marker

Growth kinetics and production profiles of recombinant PiCV capsid protein (Cap) in different E. coli strains. (A) The growth and protein production profiles of the three recombinant E. coli strains expressing either the GST-Cap or GST-Cap opt protein. Two strains, BL21 (DE3) and BL21 (DE3)-pLysS expressing GST-Cap opt , and one GST-Cap expressing strain BL21 (DE3)-CodonPlus-RIPL were used in this study post-induction. (B) Growth and protein production profiles of four recombinant E. coli strains expressing Trx-His-Cap or Trx-His-Cap opt protein. Two E. coli strains, BL21 (DE3) and BL21 (DE3)-pLysS were used to express Trx-His-Cap opt , and other two recombinant E. coli strains, BL21 (DE3)-CodonPlus-RIPL and BL21 (DE3)-pLysS were used to express Trx-His-Cap. Similar tests to those described above were used to detect the time course of protein expression after IPTG induction.
Figure Legend Snippet: Growth kinetics and production profiles of recombinant PiCV capsid protein (Cap) in different E. coli strains. (A) The growth and protein production profiles of the three recombinant E. coli strains expressing either the GST-Cap or GST-Cap opt protein. Two strains, BL21 (DE3) and BL21 (DE3)-pLysS expressing GST-Cap opt , and one GST-Cap expressing strain BL21 (DE3)-CodonPlus-RIPL were used in this study post-induction. (B) Growth and protein production profiles of four recombinant E. coli strains expressing Trx-His-Cap or Trx-His-Cap opt protein. Two E. coli strains, BL21 (DE3) and BL21 (DE3)-pLysS were used to express Trx-His-Cap opt , and other two recombinant E. coli strains, BL21 (DE3)-CodonPlus-RIPL and BL21 (DE3)-pLysS were used to express Trx-His-Cap. Similar tests to those described above were used to detect the time course of protein expression after IPTG induction.

Techniques Used: Recombinant, Expressing

The solubility of recombinant GST-Cap opt and Trx-His-Cap opt protein. The two proteins were expressed by E. coli strain BL21 (DE3)-pLysS transformed pGST-Cap opt and pTrx-His-Cap opt respectively. SDS-PAGE (A) was used to analyze the protein distribution pattern of suspension fraction and the pellet fraction. The soluble percent of two recombinant proteins was determined by measuring the intensity of target protein bands on coomassie blue-strained gels (B) . Lane M, pre-stained protein marker; lane I, total protein-expressed cell lysate; lane S, suspension fraction from centrifugal protein-expressed cell lysate; lane P, pellet fraction from centrifugal protein-expressed cell lysate. The solid triangle pinpoints the expressed Cap opt protein.
Figure Legend Snippet: The solubility of recombinant GST-Cap opt and Trx-His-Cap opt protein. The two proteins were expressed by E. coli strain BL21 (DE3)-pLysS transformed pGST-Cap opt and pTrx-His-Cap opt respectively. SDS-PAGE (A) was used to analyze the protein distribution pattern of suspension fraction and the pellet fraction. The soluble percent of two recombinant proteins was determined by measuring the intensity of target protein bands on coomassie blue-strained gels (B) . Lane M, pre-stained protein marker; lane I, total protein-expressed cell lysate; lane S, suspension fraction from centrifugal protein-expressed cell lysate; lane P, pellet fraction from centrifugal protein-expressed cell lysate. The solid triangle pinpoints the expressed Cap opt protein.

Techniques Used: Solubility, Recombinant, Transformation Assay, SDS Page, Staining, Marker

11) Product Images from "Enhanced fluorescent properties of an OmpT site deleted mutant of Green Fluorescent Protein"

Article Title: Enhanced fluorescent properties of an OmpT site deleted mutant of Green Fluorescent Protein

Journal: Microbial Cell Factories

doi: 10.1186/1475-2859-9-26

SDS-PAGE of GFP expression of GFP WT and SDM II in BL21, JM109 and LE392 at 30°C and 37°C . Panels A, B and C represent GFP expression in BL21, JM109 and LE392 cells respectively. M: Medium molecular weight marker (14-97 kDa); lanes 1 and 2: GFP WT expression at 30°C and 37°C respectively; lanes 3 and 4: SDM II expression at 30°C and 37°C respectively.
Figure Legend Snippet: SDS-PAGE of GFP expression of GFP WT and SDM II in BL21, JM109 and LE392 at 30°C and 37°C . Panels A, B and C represent GFP expression in BL21, JM109 and LE392 cells respectively. M: Medium molecular weight marker (14-97 kDa); lanes 1 and 2: GFP WT expression at 30°C and 37°C respectively; lanes 3 and 4: SDM II expression at 30°C and 37°C respectively.

Techniques Used: SDS Page, Expressing, Molecular Weight, Marker

Western blot of GFP expressed from WT and SDM II clones . M: Medium molecular weight marker 97-14 kDa); lane 1: Supernatant of WT GFP expressed from JM 109; lane 2: Supernatant of GFP SDM II expressed from JM 109 cells; lanes 3 and 4: WT GFP and SDM II mutant expressed in BL21 cells respectively. The upper arrow shows the intact GFP (29 kDa) while the lower arrow shows the degraded form of GFP (of
Figure Legend Snippet: Western blot of GFP expressed from WT and SDM II clones . M: Medium molecular weight marker 97-14 kDa); lane 1: Supernatant of WT GFP expressed from JM 109; lane 2: Supernatant of GFP SDM II expressed from JM 109 cells; lanes 3 and 4: WT GFP and SDM II mutant expressed in BL21 cells respectively. The upper arrow shows the intact GFP (29 kDa) while the lower arrow shows the degraded form of GFP (of

Techniques Used: Western Blot, Clone Assay, Molecular Weight, Marker, Mutagenesis

GFP expression and activity in two different types of E. coli hosts . (A) GFP expression from pBAD24M-GFPuv clone at 37°C. Lane 1: Protein molecular weight marker (14 to 97 kDa); lane 2, GFP expression in DH5α cells; lane 3, GFP expression in BL21 cells. (B) GFP fluorescence units of pBAD24M-GFPuv at 37°C. Sample 1, pBAD24M-GFPuv in DH5α cells; Sample 2, pBAD24M-pGFPuv in BL21 cells.
Figure Legend Snippet: GFP expression and activity in two different types of E. coli hosts . (A) GFP expression from pBAD24M-GFPuv clone at 37°C. Lane 1: Protein molecular weight marker (14 to 97 kDa); lane 2, GFP expression in DH5α cells; lane 3, GFP expression in BL21 cells. (B) GFP fluorescence units of pBAD24M-GFPuv at 37°C. Sample 1, pBAD24M-GFPuv in DH5α cells; Sample 2, pBAD24M-pGFPuv in BL21 cells.

Techniques Used: Expressing, Activity Assay, Molecular Weight, Marker, Fluorescence

Fluorescence data of GFP WT and SDM II in BL21, DH5α, JM109 and LE392 at 37°C . The relative fluorescence values with ± SEM are presented with the fluorescence of GFP obtained in BL21 defined as 100 (arbitrary unit). Sample 1: BL21; sample 2: DH5α; sample 3: JM109; sample 4: LE392. Filled bars represent WT while the empty bars represent SDM II GFP mutant.
Figure Legend Snippet: Fluorescence data of GFP WT and SDM II in BL21, DH5α, JM109 and LE392 at 37°C . The relative fluorescence values with ± SEM are presented with the fluorescence of GFP obtained in BL21 defined as 100 (arbitrary unit). Sample 1: BL21; sample 2: DH5α; sample 3: JM109; sample 4: LE392. Filled bars represent WT while the empty bars represent SDM II GFP mutant.

Techniques Used: Fluorescence, Mutagenesis

12) Product Images from "Enhanced fluorescent properties of an OmpT site deleted mutant of Green Fluorescent Protein"

Article Title: Enhanced fluorescent properties of an OmpT site deleted mutant of Green Fluorescent Protein

Journal: Microbial Cell Factories

doi: 10.1186/1475-2859-9-26

SDS-PAGE of GFP expression of GFP WT and SDM II in BL21, JM109 and LE392 at 30°C and 37°C . Panels A, B and C represent GFP expression in BL21, JM109 and LE392 cells respectively. M: Medium molecular weight marker (14-97 kDa); lanes 1 and 2: GFP WT expression at 30°C and 37°C respectively; lanes 3 and 4: SDM II expression at 30°C and 37°C respectively.
Figure Legend Snippet: SDS-PAGE of GFP expression of GFP WT and SDM II in BL21, JM109 and LE392 at 30°C and 37°C . Panels A, B and C represent GFP expression in BL21, JM109 and LE392 cells respectively. M: Medium molecular weight marker (14-97 kDa); lanes 1 and 2: GFP WT expression at 30°C and 37°C respectively; lanes 3 and 4: SDM II expression at 30°C and 37°C respectively.

Techniques Used: SDS Page, Expressing, Molecular Weight, Marker

Western blot of GFP expressed from WT and SDM II clones . M: Medium molecular weight marker 97-14 kDa); lane 1: Supernatant of WT GFP expressed from JM 109; lane 2: Supernatant of GFP SDM II expressed from JM 109 cells; lanes 3 and 4: WT GFP and SDM II mutant expressed in BL21 cells respectively. The upper arrow shows the intact GFP (29 kDa) while the lower arrow shows the degraded form of GFP (of
Figure Legend Snippet: Western blot of GFP expressed from WT and SDM II clones . M: Medium molecular weight marker 97-14 kDa); lane 1: Supernatant of WT GFP expressed from JM 109; lane 2: Supernatant of GFP SDM II expressed from JM 109 cells; lanes 3 and 4: WT GFP and SDM II mutant expressed in BL21 cells respectively. The upper arrow shows the intact GFP (29 kDa) while the lower arrow shows the degraded form of GFP (of

Techniques Used: Western Blot, Clone Assay, Molecular Weight, Marker, Mutagenesis

GFP expression and activity in two different types of E. coli hosts . (A) GFP expression from pBAD24M-GFPuv clone at 37°C. Lane 1: Protein molecular weight marker (14 to 97 kDa); lane 2, GFP expression in DH5α cells; lane 3, GFP expression in BL21 cells. (B) GFP fluorescence units of pBAD24M-GFPuv at 37°C. Sample 1, pBAD24M-GFPuv in DH5α cells; Sample 2, pBAD24M-pGFPuv in BL21 cells.
Figure Legend Snippet: GFP expression and activity in two different types of E. coli hosts . (A) GFP expression from pBAD24M-GFPuv clone at 37°C. Lane 1: Protein molecular weight marker (14 to 97 kDa); lane 2, GFP expression in DH5α cells; lane 3, GFP expression in BL21 cells. (B) GFP fluorescence units of pBAD24M-GFPuv at 37°C. Sample 1, pBAD24M-GFPuv in DH5α cells; Sample 2, pBAD24M-pGFPuv in BL21 cells.

Techniques Used: Expressing, Activity Assay, Molecular Weight, Marker, Fluorescence

Fluorescence data of GFP WT and SDM II in BL21, DH5α, JM109 and LE392 at 37°C . The relative fluorescence values with ± SEM are presented with the fluorescence of GFP obtained in BL21 defined as 100 (arbitrary unit). Sample 1: BL21; sample 2: DH5α; sample 3: JM109; sample 4: LE392. Filled bars represent WT while the empty bars represent SDM II GFP mutant.
Figure Legend Snippet: Fluorescence data of GFP WT and SDM II in BL21, DH5α, JM109 and LE392 at 37°C . The relative fluorescence values with ± SEM are presented with the fluorescence of GFP obtained in BL21 defined as 100 (arbitrary unit). Sample 1: BL21; sample 2: DH5α; sample 3: JM109; sample 4: LE392. Filled bars represent WT while the empty bars represent SDM II GFP mutant.

Techniques Used: Fluorescence, Mutagenesis

13) Product Images from "Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism"

Article Title: Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism

Journal: The EMBO Journal

doi: 10.1038/sj.emboj.7601638

Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.
Figure Legend Snippet: Residues that are required for EspP processing are also essential for the processing of B. pertussis autotransporters. BL21-CodonPlus(DE3)−RIL was transformed with a plasmid encoding HA-tagged Prn or the indicated mutant ( A ), or His-tagged BrkA or the indicated mutant ( B ) and grown in LB. Autotransporter synthesis was induced by incubating cultures with 100 μM IPTG for 2 h, and passenger domain cleavage was assayed by Western blot using anti-HA or anti-His tag antisera.

Techniques Used: Transformation Assay, Plasmid Preparation, Mutagenesis, Western Blot

14) Product Images from "High yield production of pigeon circovirus capsid protein in the E. coli by evaluating the key parameters needed for protein expression"

Article Title: High yield production of pigeon circovirus capsid protein in the E. coli by evaluating the key parameters needed for protein expression

Journal: BMC Veterinary Research

doi: 10.1186/1746-6148-10-115

Effect of fusion tags, E. coli strains and rare codon replacement on recombinant PiCV capsid protein expression. The three expression plasmids containing wild-type PiCV capsid gene were expressed in E. coli strains BL21 (DE3), BL21 (DE3)-pLysS and BL21 (DE3)-CodonPlus-RIPL. Furthermore, similar plasmids but containing the codon-optimized PiCV capsid gene were also expressed in BL21 (DE3) and BL21 (DE3)-pLysS. All examined recombinant PiCV capsid proteins were analyzed by SDS-PAGE and Western-blotting. Anti-6xHis tag monoclonal antibody was used to recognize the 6xHis-tagged (A) and Trx-tagged (C) Cap proteins. Anti-GST monoclonal antibody was used for detecting GST-tagged (B) Cap proteins. Lane M, pre-stained protein marker; lane 1, 3, 5, 7 and 9, before IPTG induction; lane 2, 4, 6, 8 and 10, after IPTG induction for 4 hrs cultivation. The solid triangle pinpoints the expressed Cap protein.
Figure Legend Snippet: Effect of fusion tags, E. coli strains and rare codon replacement on recombinant PiCV capsid protein expression. The three expression plasmids containing wild-type PiCV capsid gene were expressed in E. coli strains BL21 (DE3), BL21 (DE3)-pLysS and BL21 (DE3)-CodonPlus-RIPL. Furthermore, similar plasmids but containing the codon-optimized PiCV capsid gene were also expressed in BL21 (DE3) and BL21 (DE3)-pLysS. All examined recombinant PiCV capsid proteins were analyzed by SDS-PAGE and Western-blotting. Anti-6xHis tag monoclonal antibody was used to recognize the 6xHis-tagged (A) and Trx-tagged (C) Cap proteins. Anti-GST monoclonal antibody was used for detecting GST-tagged (B) Cap proteins. Lane M, pre-stained protein marker; lane 1, 3, 5, 7 and 9, before IPTG induction; lane 2, 4, 6, 8 and 10, after IPTG induction for 4 hrs cultivation. The solid triangle pinpoints the expressed Cap protein.

Techniques Used: Recombinant, Expressing, SDS Page, Western Blot, Staining, Marker

Growth kinetics and production profiles of recombinant PiCV capsid protein (Cap) in different E. coli strains. (A) The growth and protein production profiles of the three recombinant E. coli strains expressing either the GST-Cap or GST-Cap opt protein. Two strains, BL21 (DE3) and BL21 (DE3)-pLysS expressing GST-Cap opt , and one GST-Cap expressing strain BL21 (DE3)-CodonPlus-RIPL were used in this study post-induction. (B) Growth and protein production profiles of four recombinant E. coli strains expressing Trx-His-Cap or Trx-His-Cap opt protein. Two E. coli strains, BL21 (DE3) and BL21 (DE3)-pLysS were used to express Trx-His-Cap opt , and other two recombinant E. coli strains, BL21 (DE3)-CodonPlus-RIPL and BL21 (DE3)-pLysS were used to express Trx-His-Cap. Similar tests to those described above were used to detect the time course of protein expression after IPTG induction.
Figure Legend Snippet: Growth kinetics and production profiles of recombinant PiCV capsid protein (Cap) in different E. coli strains. (A) The growth and protein production profiles of the three recombinant E. coli strains expressing either the GST-Cap or GST-Cap opt protein. Two strains, BL21 (DE3) and BL21 (DE3)-pLysS expressing GST-Cap opt , and one GST-Cap expressing strain BL21 (DE3)-CodonPlus-RIPL were used in this study post-induction. (B) Growth and protein production profiles of four recombinant E. coli strains expressing Trx-His-Cap or Trx-His-Cap opt protein. Two E. coli strains, BL21 (DE3) and BL21 (DE3)-pLysS were used to express Trx-His-Cap opt , and other two recombinant E. coli strains, BL21 (DE3)-CodonPlus-RIPL and BL21 (DE3)-pLysS were used to express Trx-His-Cap. Similar tests to those described above were used to detect the time course of protein expression after IPTG induction.

Techniques Used: Recombinant, Expressing

The solubility of recombinant GST-Cap opt and Trx-His-Cap opt protein. The two proteins were expressed by E. coli strain BL21 (DE3)-pLysS transformed pGST-Cap opt and pTrx-His-Cap opt respectively. SDS-PAGE (A) was used to analyze the protein distribution pattern of suspension fraction and the pellet fraction. The soluble percent of two recombinant proteins was determined by measuring the intensity of target protein bands on coomassie blue-strained gels (B) . Lane M, pre-stained protein marker; lane I, total protein-expressed cell lysate; lane S, suspension fraction from centrifugal protein-expressed cell lysate; lane P, pellet fraction from centrifugal protein-expressed cell lysate. The solid triangle pinpoints the expressed Cap opt protein.
Figure Legend Snippet: The solubility of recombinant GST-Cap opt and Trx-His-Cap opt protein. The two proteins were expressed by E. coli strain BL21 (DE3)-pLysS transformed pGST-Cap opt and pTrx-His-Cap opt respectively. SDS-PAGE (A) was used to analyze the protein distribution pattern of suspension fraction and the pellet fraction. The soluble percent of two recombinant proteins was determined by measuring the intensity of target protein bands on coomassie blue-strained gels (B) . Lane M, pre-stained protein marker; lane I, total protein-expressed cell lysate; lane S, suspension fraction from centrifugal protein-expressed cell lysate; lane P, pellet fraction from centrifugal protein-expressed cell lysate. The solid triangle pinpoints the expressed Cap opt protein.

Techniques Used: Solubility, Recombinant, Transformation Assay, SDS Page, Staining, Marker

Related Articles

Amplification:

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients
Article Snippet: .. Amplified DNA was subcloned into pET-28a vector (Novagen, Madison, WI) in Bam H I and Hin d III sites to transform BL21 (DE3, Stratagene). .. Recombinant protein was obtained by IPTG induction and purified through the Ni-NTA column.

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients
Article Snippet: .. Amplified DNA was subcloned into pET-28a vector to transform BL21 (DE3). .. Recombinant protein was obtained by IPTG induction and purified through the Ni-NTA column as 43 kDa protein containing TgRPP and 6x His Tag, thrombin, and T7 Tag in N-terminal of insert ( ).

Transformation Assay:

Article Title: Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism
Article Snippet: .. To purify His-tagged proEspPΔ1, BL21 transformed with either pTrc10HisEspPΔ1(D1120N) or pTrc10HisEspPΔ1(E1154A) was grown in 500 ml LB. .. At OD550 =0.5, expression of the plasmid-borne genes was induced by adding 10 μM IPTG.

Article Title: Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism
Article Snippet: .. BL21 transformed with p(TEV1)-p(TEV6) was grown overnight in LB, washed and diluted into 250 ml medium at OD600 =0.02. .. When the cultures reached OD600 =0.2, synthesis of the EspP derivatives was induced by the addition of 10 μM IPTG (final concentration).

other:

Article Title: A New Amidohydrolase from Bordetella or Alcaligenes Strain FB188 with Similarities to Histone Deacetylases
Article Snippet: E. coli strains XL1-Blue and BL21 were purchased from Stratagene (La Jolla, Calif.).

Plasmid Preparation:

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients
Article Snippet: .. Amplified DNA was subcloned into pET-28a vector (Novagen, Madison, WI) in Bam H I and Hin d III sites to transform BL21 (DE3, Stratagene). .. Recombinant protein was obtained by IPTG induction and purified through the Ni-NTA column.

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients
Article Snippet: .. Amplified DNA was subcloned into pET-28a vector to transform BL21 (DE3). .. Recombinant protein was obtained by IPTG induction and purified through the Ni-NTA column as 43 kDa protein containing TgRPP and 6x His Tag, thrombin, and T7 Tag in N-terminal of insert ( ).

Positron Emission Tomography:

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients
Article Snippet: .. Amplified DNA was subcloned into pET-28a vector (Novagen, Madison, WI) in Bam H I and Hin d III sites to transform BL21 (DE3, Stratagene). .. Recombinant protein was obtained by IPTG induction and purified through the Ni-NTA column.

Article Title: Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients
Article Snippet: .. Amplified DNA was subcloned into pET-28a vector to transform BL21 (DE3). .. Recombinant protein was obtained by IPTG induction and purified through the Ni-NTA column as 43 kDa protein containing TgRPP and 6x His Tag, thrombin, and T7 Tag in N-terminal of insert ( ).

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    Stratagene ptd drbd expression utilized bl21 codon
    <t>PTD-DRBD</t> siRNA delivery into T cells and HUVECs ( a ) Flow cytometry analysis of dGFP RNAi knockdown decay kinetics of dividing Jurkat dGFP cells following treatment with GFP2 siRNA plus PTD-DRBD, Lipofection-2000 (Lipofection) or RNAiMAX (Lipofection 2), as indicated. ( b ) Quantitative RT-PCR analysis of endogenous GAPDH mRNA expression at 12 h post-treatment of GAPDH siRNA or GFP2 (Con) siRNA plus PTD-DRBD, GAPDH siRNA plus Lipofection-2000 (Lipofection) or RNAiMAX (Lipofection 2) in Jurkat cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock GAPDH control. ( c ) Flow cytometry histogram analysis of PTD-DRBD mediated CD4 or CD8 RNAi response at 1 day post-treatment of mouse primary T cells, as indicated. ( d ) Quantitative RT-PCR analysis of endogenous CD4, CD8 or CD90 mRNA expression at 12 and 24 h post-treatment of PTD-DRBD CD4 or CD8 siRNAs in primary T cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock control. *(P
    Ptd Drbd Expression Utilized Bl21 Codon, supplied by Stratagene, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene e coli bl21
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21, supplied by Stratagene, used in various techniques. Bioz Stars score: 93/100, based on 173 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene e coli bl21 de3 ripl cells
    A biochemical approach to dissect portal function. (a) The plasmids containing g20 variants (WT or mutants) were transformed into E. coli <t>BL21</t> (DE3) <t>RIPL</t> strain for IPTG induced expression of the respective gp20 protein (green). (b) The E. coli cells
    E Coli Bl21 De3 Ripl Cells, supplied by Stratagene, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    PTD-DRBD siRNA delivery into T cells and HUVECs ( a ) Flow cytometry analysis of dGFP RNAi knockdown decay kinetics of dividing Jurkat dGFP cells following treatment with GFP2 siRNA plus PTD-DRBD, Lipofection-2000 (Lipofection) or RNAiMAX (Lipofection 2), as indicated. ( b ) Quantitative RT-PCR analysis of endogenous GAPDH mRNA expression at 12 h post-treatment of GAPDH siRNA or GFP2 (Con) siRNA plus PTD-DRBD, GAPDH siRNA plus Lipofection-2000 (Lipofection) or RNAiMAX (Lipofection 2) in Jurkat cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock GAPDH control. ( c ) Flow cytometry histogram analysis of PTD-DRBD mediated CD4 or CD8 RNAi response at 1 day post-treatment of mouse primary T cells, as indicated. ( d ) Quantitative RT-PCR analysis of endogenous CD4, CD8 or CD90 mRNA expression at 12 and 24 h post-treatment of PTD-DRBD CD4 or CD8 siRNAs in primary T cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock control. *(P

    Journal: Nature biotechnology

    Article Title: Efficient siRNA Delivery into Primary Cells by Peptide Transduction-dsRNA Binding Domain (PTD-DRBD) Fusion Protein

    doi: 10.1038/nbt.1541

    Figure Lengend Snippet: PTD-DRBD siRNA delivery into T cells and HUVECs ( a ) Flow cytometry analysis of dGFP RNAi knockdown decay kinetics of dividing Jurkat dGFP cells following treatment with GFP2 siRNA plus PTD-DRBD, Lipofection-2000 (Lipofection) or RNAiMAX (Lipofection 2), as indicated. ( b ) Quantitative RT-PCR analysis of endogenous GAPDH mRNA expression at 12 h post-treatment of GAPDH siRNA or GFP2 (Con) siRNA plus PTD-DRBD, GAPDH siRNA plus Lipofection-2000 (Lipofection) or RNAiMAX (Lipofection 2) in Jurkat cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock GAPDH control. ( c ) Flow cytometry histogram analysis of PTD-DRBD mediated CD4 or CD8 RNAi response at 1 day post-treatment of mouse primary T cells, as indicated. ( d ) Quantitative RT-PCR analysis of endogenous CD4, CD8 or CD90 mRNA expression at 12 and 24 h post-treatment of PTD-DRBD CD4 or CD8 siRNAs in primary T cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock control. *(P

    Article Snippet: PTD-DRBD expression utilized BL21 codon plus (DH3) E.coli (Strategene) cells were transformed with pPTD-DRBD, cultured at 37°C in LB, then at 25°C for 12 h after induction with 400 μM IPTG.

    Techniques: Flow Cytometry, Cytometry, Quantitative RT-PCR, Expressing

    PTD-DRBD mediated siRNA delivery ( a ) Hypothetical cartoon of PTD-DRBD bound to siRNA. DRBD Ribbon structure derived from Ryter and Schultze 13 ( b ) Normalized RNAi knockdown of dGFP and dDsRed by PTD-DRBD:siRNA (left panel) and lipofection (right panel), as indicated, in H1299 dGFP/dDsRed cells. Mean values were normalized to percent control. ( c,d ) Single cell flow cytometry histogram analysis of dGFP RNAi response at 1 and 2 days post-treatment of H1299 dGFP/dDsRed cells, as indicated. ( e ) Flow cytometry analysis of dGFP RNAi knockdown decay kinetics following a single siRNA treatment of dividing H1299 dGFP/dDsRed cells. ( f ) Flow cytometry analysis of dGFP RNAi knockdown decay kinetics following multiple siRNA treatments of H1299 dGFP cells, as indicated. Mean values are normalized to percent control. ( g,h ) Quantitative RT-PCR analysis of endogenous GAPDH mRNA expression at 6 and 12 h post-treatment in H1299 cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock GAPDH control. **(P

    Journal: Nature biotechnology

    Article Title: Efficient siRNA Delivery into Primary Cells by Peptide Transduction-dsRNA Binding Domain (PTD-DRBD) Fusion Protein

    doi: 10.1038/nbt.1541

    Figure Lengend Snippet: PTD-DRBD mediated siRNA delivery ( a ) Hypothetical cartoon of PTD-DRBD bound to siRNA. DRBD Ribbon structure derived from Ryter and Schultze 13 ( b ) Normalized RNAi knockdown of dGFP and dDsRed by PTD-DRBD:siRNA (left panel) and lipofection (right panel), as indicated, in H1299 dGFP/dDsRed cells. Mean values were normalized to percent control. ( c,d ) Single cell flow cytometry histogram analysis of dGFP RNAi response at 1 and 2 days post-treatment of H1299 dGFP/dDsRed cells, as indicated. ( e ) Flow cytometry analysis of dGFP RNAi knockdown decay kinetics following a single siRNA treatment of dividing H1299 dGFP/dDsRed cells. ( f ) Flow cytometry analysis of dGFP RNAi knockdown decay kinetics following multiple siRNA treatments of H1299 dGFP cells, as indicated. Mean values are normalized to percent control. ( g,h ) Quantitative RT-PCR analysis of endogenous GAPDH mRNA expression at 6 and 12 h post-treatment in H1299 cells, as indicated. Mean values normalized to β2 microglobulin and reported as percent of mock GAPDH control. **(P

    Article Snippet: PTD-DRBD expression utilized BL21 codon plus (DH3) E.coli (Strategene) cells were transformed with pPTD-DRBD, cultured at 37°C in LB, then at 25°C for 12 h after induction with 400 μM IPTG.

    Techniques: Derivative Assay, Flow Cytometry, Cytometry, Quantitative RT-PCR, Expressing

    PTD-DRBD mediated RNAi responses ( a ) Fluorescent microscopy analysis of H9 hESCs constitutively expressing GFP treated with with PTD-DRBD delivered GFP2 siRNA at 2 days post-addition. Black line outlines hESC colony on mouse feeder cell background. ( b ) Oct4 immunoblot analysis in HUES9 hESCs treated with mock (PBS), PTD-DRBD delivered Oct4 or control siRNAs at 2 days post-addition. ( c ) Cell division curve of human HUES9 embryonic stem cells treated with mock (PBS), PTD-DRBD delivered Oct4 or control siRNAs, as indicated. ( d ) Immunohistochemistry analysis of Oct4 and SSEA4 expression in HUES9 hESCs at 2 days post-treatment with mock (PBS), PTD-DRB delivered Oct4 or control siRNAs. Anti-Oct4 antibodies (red), anti-SSEA-4 antibodies (green), genomic DNA (blue). ( e ) Immuno-histochemistry analysis of GATA6 and SSEA4 expression in HUES9 hESCs at 10 days post-treatment with mock (PBS), PTD-DRB delivered Oct4 or control siRNAs. Anti-GATA6 antibodies (red), anti-SSEA-4 antibodies (green), genomic DNA (blue). ( f, g ) Analysis of IFN-α and TNF-α induction in human PBMCs at 4 or 24 h post-treatment with mock (PBS), β-gal siRNA plus PTD-DRBD or plus Lipofection, as indicated. 10 μ/ml Imiquimod Imiquimod or 10 μg/ml LPS was used as a positive control for IFN-α or TNF-α, respectively. ( h ) Nasal and tracheal expressing ROSA26R-Luciferase transgenic mice were live animal imaged on day 0. Randomized groups of luciferase expressing mice were then treated with PBS, PTD-DRBD plus Luc siRNA or control GFP (Con) siRNA and monitored daily for luciferase expression, as indicated. Scale is in photons/s/cm 2 /sr. ( i ) Graph of percent Luciferase knockdown mice from (h) above. Luciferase expression was normalized to mock each day, error bar indicates s.e.m., n = 3 for each group with two luciferase readings performed per mouse per day.

    Journal: Nature biotechnology

    Article Title: Efficient siRNA Delivery into Primary Cells by Peptide Transduction-dsRNA Binding Domain (PTD-DRBD) Fusion Protein

    doi: 10.1038/nbt.1541

    Figure Lengend Snippet: PTD-DRBD mediated RNAi responses ( a ) Fluorescent microscopy analysis of H9 hESCs constitutively expressing GFP treated with with PTD-DRBD delivered GFP2 siRNA at 2 days post-addition. Black line outlines hESC colony on mouse feeder cell background. ( b ) Oct4 immunoblot analysis in HUES9 hESCs treated with mock (PBS), PTD-DRBD delivered Oct4 or control siRNAs at 2 days post-addition. ( c ) Cell division curve of human HUES9 embryonic stem cells treated with mock (PBS), PTD-DRBD delivered Oct4 or control siRNAs, as indicated. ( d ) Immunohistochemistry analysis of Oct4 and SSEA4 expression in HUES9 hESCs at 2 days post-treatment with mock (PBS), PTD-DRB delivered Oct4 or control siRNAs. Anti-Oct4 antibodies (red), anti-SSEA-4 antibodies (green), genomic DNA (blue). ( e ) Immuno-histochemistry analysis of GATA6 and SSEA4 expression in HUES9 hESCs at 10 days post-treatment with mock (PBS), PTD-DRB delivered Oct4 or control siRNAs. Anti-GATA6 antibodies (red), anti-SSEA-4 antibodies (green), genomic DNA (blue). ( f, g ) Analysis of IFN-α and TNF-α induction in human PBMCs at 4 or 24 h post-treatment with mock (PBS), β-gal siRNA plus PTD-DRBD or plus Lipofection, as indicated. 10 μ/ml Imiquimod Imiquimod or 10 μg/ml LPS was used as a positive control for IFN-α or TNF-α, respectively. ( h ) Nasal and tracheal expressing ROSA26R-Luciferase transgenic mice were live animal imaged on day 0. Randomized groups of luciferase expressing mice were then treated with PBS, PTD-DRBD plus Luc siRNA or control GFP (Con) siRNA and monitored daily for luciferase expression, as indicated. Scale is in photons/s/cm 2 /sr. ( i ) Graph of percent Luciferase knockdown mice from (h) above. Luciferase expression was normalized to mock each day, error bar indicates s.e.m., n = 3 for each group with two luciferase readings performed per mouse per day.

    Article Snippet: PTD-DRBD expression utilized BL21 codon plus (DH3) E.coli (Strategene) cells were transformed with pPTD-DRBD, cultured at 37°C in LB, then at 25°C for 12 h after induction with 400 μM IPTG.

    Techniques: Microscopy, Expressing, Immunohistochemistry, Positive Control, Luciferase, Transgenic Assay, Mouse Assay

    SDS-PAGE analysis of purified protein recombinant SllB in E. coli BL21 cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: SDS-PAGE analysis of purified protein recombinant SllB in E. coli BL21 cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: SDS Page, Purification, Recombinant, Marker

    A transmission electron microscopic observation on the E. coli BL21 with recombinant protein. (A) Normal E. coli BL21 was treated as control. (B) The E. coli BL21 cells recombinant S-layer protein. (C) Crystal lattice structures on surface of the E. coli BL21 cells recombinant S-layer protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: A transmission electron microscopic observation on the E. coli BL21 with recombinant protein. (A) Normal E. coli BL21 was treated as control. (B) The E. coli BL21 cells recombinant S-layer protein. (C) Crystal lattice structures on surface of the E. coli BL21 cells recombinant S-layer protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: Transmission Assay, Recombinant

    Expression of sllB in E. coli BL21 cells. (A) SDS-PAGE analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; lane M represent Takara Protein Marker (Broad). (B) Western blot analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; M, Takara Protein Marker (Broad). Lane M1, Precision plus protein standards; lane M2, perfect protein marker. Note the band pointed with arrows is the recombinant S-layer protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: Expression of sllB in E. coli BL21 cells. (A) SDS-PAGE analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; lane M represent Takara Protein Marker (Broad). (B) Western blot analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; M, Takara Protein Marker (Broad). Lane M1, Precision plus protein standards; lane M2, perfect protein marker. Note the band pointed with arrows is the recombinant S-layer protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: Expressing, SDS Page, Marker, Western Blot, Recombinant

    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

    A biochemical approach to dissect portal function. (a) The plasmids containing g20 variants (WT or mutants) were transformed into E. coli BL21 (DE3) RIPL strain for IPTG induced expression of the respective gp20 protein (green). (b) The E. coli cells

    Journal: Journal of molecular biology

    Article Title: Structure-Function Analysis of the DNA Translocating Portal of the Bacteriophage T4 Packaging Machine

    doi: 10.1016/j.jmb.2013.10.011

    Figure Lengend Snippet: A biochemical approach to dissect portal function. (a) The plasmids containing g20 variants (WT or mutants) were transformed into E. coli BL21 (DE3) RIPL strain for IPTG induced expression of the respective gp20 protein (green). (b) The E. coli cells

    Article Snippet: E. coli BL21 (DE3) RIPL cells containing the gp20 recombinant plasmids was induced with isopropyl-β-D-thio-galactoside (IPTG; 1 mM) for 20 min at 37°C.

    Techniques: Transformation Assay, Expressing