shuffle strain c3030  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 93
      Buy from Supplier

    Structured Review

    New England Biolabs shuffle strain c3030
    Cytoplamic expression of proTHI-TRX fusion proteins in strain <t>C3030.</t> For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein
    Shuffle Strain C3030, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/shuffle strain c3030/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    shuffle strain c3030 - by Bioz Stars, 2022-07
    93/100 stars

    Images

    1) Product Images from "Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli"

    Article Title: Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli

    Journal: Biotechnology Letters

    doi: 10.1007/s10529-013-1180-z

    Cytoplamic expression of proTHI-TRX fusion proteins in strain C3030. For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein
    Figure Legend Snippet: Cytoplamic expression of proTHI-TRX fusion proteins in strain C3030. For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein

    Techniques Used: Expressing, Cell Culture, Marker, Lysis, Sonication

    Comparison of Ni–NTA purified proTHI-TRX fusion proteins from strain C3030. a Coomassie Brilliant Blue staining. b Western blot with anti-His tag antibody. Each well contained 3 μg protein. (M) Prestained protein marker, ( 1 ) proTHI2.1-TRX, ( 2 ) proTHI2.2-TRX, ( 3 ) proTHI2.3-TRX, ( 4 ) proTHI2.4-TRX
    Figure Legend Snippet: Comparison of Ni–NTA purified proTHI-TRX fusion proteins from strain C3030. a Coomassie Brilliant Blue staining. b Western blot with anti-His tag antibody. Each well contained 3 μg protein. (M) Prestained protein marker, ( 1 ) proTHI2.1-TRX, ( 2 ) proTHI2.2-TRX, ( 3 ) proTHI2.3-TRX, ( 4 ) proTHI2.4-TRX

    Techniques Used: Purification, Staining, Western Blot, Marker

    2) Product Images from "Evaluation of a Plasmodium-Specific Carrier Protein To Enhance Production of Recombinant Pfs25, a Leading Transmission-Blocking Vaccine Candidate"

    Article Title: Evaluation of a Plasmodium-Specific Carrier Protein To Enhance Production of Recombinant Pfs25, a Leading Transmission-Blocking Vaccine Candidate

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00486-17

    Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.
    Figure Legend Snippet: Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.

    Techniques Used: Expressing, Construct, Transformation Assay, SDS Page, Staining

    3) Product Images from "A high-throughput expression screening platform to optimize the production of antimicrobial peptides"

    Article Title: A high-throughput expression screening platform to optimize the production of antimicrobial peptides

    Journal: Microbial Cell Factories

    doi: 10.1186/s12934-017-0637-5

    Expression screening in E. coli . Expression screening was carried out in 96-well microtiter plates to identify high producers for three different target proteins. The promoter, protein fusion partner and E. coli strain were varied. a IMPI, b BR021, c AFP. Rosetta-gami 2 Rosetta-gami 2 (DE3) pLysS, Origami Origami 2, SHuffle SHuffle T7 Express lysY, BL21 BL21 (DE3), C41 OverExpress C41 (DE3) pLysS, C43 OverExpress C43 (DE3) pLysS
    Figure Legend Snippet: Expression screening in E. coli . Expression screening was carried out in 96-well microtiter plates to identify high producers for three different target proteins. The promoter, protein fusion partner and E. coli strain were varied. a IMPI, b BR021, c AFP. Rosetta-gami 2 Rosetta-gami 2 (DE3) pLysS, Origami Origami 2, SHuffle SHuffle T7 Express lysY, BL21 BL21 (DE3), C41 OverExpress C41 (DE3) pLysS, C43 OverExpress C43 (DE3) pLysS

    Techniques Used: Expressing

    4) Product Images from "Molecular and Biochemical Analysis of Duplicated Cytosolic CuZn Superoxide Dismutases of Rice and in silico Analysis in Plants"

    Article Title: Molecular and Biochemical Analysis of Duplicated Cytosolic CuZn Superoxide Dismutases of Rice and in silico Analysis in Plants

    Journal: Frontiers in Plant Science

    doi: 10.3389/fpls.2022.864330

    Analysis of oxidative stress tolerance of E. coli SHuffle T7 Express cells overexpressing OsCSD1 and OsCSD4. (A) Comparative analysis of growth of E. coli cells (absorbance at 600 nm) containing pET28a (empty vector), pET28a-OsCSD1, and pET28a-OsCSD4 plasmids. Cells induced with IPTG were treated with increasing methyl viologen concentration (0–0.500 mM) and monitored spectrophotometrically. The experiment was repeated three times and data are represented as mean value ± SD. Statistical significance is indicated by * p
    Figure Legend Snippet: Analysis of oxidative stress tolerance of E. coli SHuffle T7 Express cells overexpressing OsCSD1 and OsCSD4. (A) Comparative analysis of growth of E. coli cells (absorbance at 600 nm) containing pET28a (empty vector), pET28a-OsCSD1, and pET28a-OsCSD4 plasmids. Cells induced with IPTG were treated with increasing methyl viologen concentration (0–0.500 mM) and monitored spectrophotometrically. The experiment was repeated three times and data are represented as mean value ± SD. Statistical significance is indicated by * p

    Techniques Used: Plasmid Preparation, Concentration Assay

    5) Product Images from "Evaluation of a Plasmodium-Specific Carrier Protein To Enhance Production of Recombinant Pfs25, a Leading Transmission-Blocking Vaccine Candidate"

    Article Title: Evaluation of a Plasmodium-Specific Carrier Protein To Enhance Production of Recombinant Pfs25, a Leading Transmission-Blocking Vaccine Candidate

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00486-17

    Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.
    Figure Legend Snippet: Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.

    Techniques Used: Expressing, Construct, Transformation Assay, SDS Page, Staining

    6) Product Images from "Creating a thermostable beta-glucuronidase switch for homogeneous immunoassay by disruption of conserved salt bridges at diagonal interfaces"

    Article Title: Creating a thermostable beta-glucuronidase switch for homogeneous immunoassay by disruption of conserved salt bridges at diagonal interfaces

    Journal: bioRxiv

    doi: 10.1101/2022.05.19.492583

    Conserved salt bridges at diagonal interfaces of GUS and the effect of Ala substitution on the switch function. (A) H514-E523 salt bridge between the diagonal subunits of wild-type GUS (PDB: 3LPF). (B) WebLogo (residue 512–525) showing the alignment of GUS or GUS-like scaffold from eleven organisms with amino acid identity > 40%. Color scheme of amino acid: polar, green; neutral, blue; basic, yellow; acidic, purple; hydrophobic, grey. (C) Residues show interactions with E523 (PDB: 3LPF). (D) Time course activity measurement of V HH -GUS TR3 -AKW. S/B was calculated according to the reaction rate from 0–15 min. (E) Time course activity measurement of V HH -GUS TR3 -AKE. All data are expressed as mean ± standard deviation (n = 3). N.A.: Not available. (F) SDS-PAGE analysis of the purified immunosensor variants. AKW: V HH -GUS TR3 -AKW; AKE: V HH -GUS TR3 -AKE. The orange arrow indicates the monomer of the immunosensors. Dash line divides the grouped lanes that are from two gels.
    Figure Legend Snippet: Conserved salt bridges at diagonal interfaces of GUS and the effect of Ala substitution on the switch function. (A) H514-E523 salt bridge between the diagonal subunits of wild-type GUS (PDB: 3LPF). (B) WebLogo (residue 512–525) showing the alignment of GUS or GUS-like scaffold from eleven organisms with amino acid identity > 40%. Color scheme of amino acid: polar, green; neutral, blue; basic, yellow; acidic, purple; hydrophobic, grey. (C) Residues show interactions with E523 (PDB: 3LPF). (D) Time course activity measurement of V HH -GUS TR3 -AKW. S/B was calculated according to the reaction rate from 0–15 min. (E) Time course activity measurement of V HH -GUS TR3 -AKE. All data are expressed as mean ± standard deviation (n = 3). N.A.: Not available. (F) SDS-PAGE analysis of the purified immunosensor variants. AKW: V HH -GUS TR3 -AKW; AKE: V HH -GUS TR3 -AKE. The orange arrow indicates the monomer of the immunosensors. Dash line divides the grouped lanes that are from two gels.

    Techniques Used: Activity Assay, Standard Deviation, SDS Page, Purification

    Thermostability profiling of V HH -GUS TR3 -DLW immunosensor and its analyte dosedependency measurement. Time course activity measurement of V HH -GUS TR3 -DLW at 25 °C (A), 37 °C (B), and 45 °C (C). S/B was calculated according to the fluorescence intensity at each time. Max.: maximum. (D) The reaction rate in the presence of 100 μM caffeine of different time ranges. (E) Caffeine dose-dependent curve. All data are expressed as mean ± standard deviation (n = 3).
    Figure Legend Snippet: Thermostability profiling of V HH -GUS TR3 -DLW immunosensor and its analyte dosedependency measurement. Time course activity measurement of V HH -GUS TR3 -DLW at 25 °C (A), 37 °C (B), and 45 °C (C). S/B was calculated according to the fluorescence intensity at each time. Max.: maximum. (D) The reaction rate in the presence of 100 μM caffeine of different time ranges. (E) Caffeine dose-dependent curve. All data are expressed as mean ± standard deviation (n = 3).

    Techniques Used: Activity Assay, Fluorescence, Standard Deviation

    Functional and structural analysis of the immunosensors carrying the selected GUS TR3 mutants. (A) Time course activity measurement of V HH -GUS TR3 -DLW. (B) Time course activity measurement of V HH -GUS TR3 -SLE. (C) Time course activity measurement of V HH -GUS TR3 -AQY.S/B was calculated according to the reaction rate from 0–15 min. All data are expressed as mean ± standard deviation (n = 3). (D) Detailed structure around the catalytic center (residues in purple) and interface mutations. The loop from catalytic residue E504 to E523 is labeled in dark blue. (E) MD simulation result of the GUS TR3 -DLW at 15 ns. The simulated structure of GUS TR3 at 15 ns is superimposed and the H514 residues only are shown (grey) for comparison. The black arrow indicates the flip of the sidechain at residue 514. The O and N atoms in sidechains are labeled with red and blue, respectively.
    Figure Legend Snippet: Functional and structural analysis of the immunosensors carrying the selected GUS TR3 mutants. (A) Time course activity measurement of V HH -GUS TR3 -DLW. (B) Time course activity measurement of V HH -GUS TR3 -SLE. (C) Time course activity measurement of V HH -GUS TR3 -AQY.S/B was calculated according to the reaction rate from 0–15 min. All data are expressed as mean ± standard deviation (n = 3). (D) Detailed structure around the catalytic center (residues in purple) and interface mutations. The loop from catalytic residue E504 to E523 is labeled in dark blue. (E) MD simulation result of the GUS TR3 -DLW at 15 ns. The simulated structure of GUS TR3 at 15 ns is superimposed and the H514 residues only are shown (grey) for comparison. The black arrow indicates the flip of the sidechain at residue 514. The O and N atoms in sidechains are labeled with red and blue, respectively.

    Techniques Used: Functional Assay, Activity Assay, Standard Deviation, Labeling

    GUS complementation-based homogenous immunosensor. (A) Schematic illustration of the V HH -GUS immunosensor. The V HH (VSA2)-GUS TR3 monomer was modeled by AlphaFold and assembled via superimposing to the structure (PDB: 3LPG) of wild-type GUS. The linker region and the V HH were adjusted manually in PyMOL. (B) Interchain interactions between the Y517 and the counter residues in wild-type GUS (PDB: 3LPF). (C) Time course activity measurement of V HH -GUS TR3 -KW. (D) Time course activity measurement of V HH -GUS TR3 -KE. S/B was calculated according to the reaction rate from 0–5 min. (E) ELISA result showing the binding between the V HH -GUS TR3 -KE and caffeine. All data are expressed as mean ± standard deviation (n = 3).
    Figure Legend Snippet: GUS complementation-based homogenous immunosensor. (A) Schematic illustration of the V HH -GUS immunosensor. The V HH (VSA2)-GUS TR3 monomer was modeled by AlphaFold and assembled via superimposing to the structure (PDB: 3LPG) of wild-type GUS. The linker region and the V HH were adjusted manually in PyMOL. (B) Interchain interactions between the Y517 and the counter residues in wild-type GUS (PDB: 3LPF). (C) Time course activity measurement of V HH -GUS TR3 -KW. (D) Time course activity measurement of V HH -GUS TR3 -KE. S/B was calculated according to the reaction rate from 0–5 min. (E) ELISA result showing the binding between the V HH -GUS TR3 -KE and caffeine. All data are expressed as mean ± standard deviation (n = 3).

    Techniques Used: Activity Assay, Enzyme-linked Immunosorbent Assay, Binding Assay, Standard Deviation

    7) Product Images from "Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli"

    Article Title: Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli

    Journal: Biotechnology Letters

    doi: 10.1007/s10529-013-1180-z

    Cytoplamic expression of proTHI-TRX fusion proteins in strain C3030. For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein
    Figure Legend Snippet: Cytoplamic expression of proTHI-TRX fusion proteins in strain C3030. For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein

    Techniques Used: Expressing, Cell Culture, Marker, Lysis, Sonication

    Comparison of Ni–NTA purified proTHI-TRX fusion proteins from strain C3030. a Coomassie Brilliant Blue staining. b Western blot with anti-His tag antibody. Each well contained 3 μg protein. (M) Prestained protein marker, ( 1 ) proTHI2.1-TRX, ( 2 ) proTHI2.2-TRX, ( 3 ) proTHI2.3-TRX, ( 4 ) proTHI2.4-TRX
    Figure Legend Snippet: Comparison of Ni–NTA purified proTHI-TRX fusion proteins from strain C3030. a Coomassie Brilliant Blue staining. b Western blot with anti-His tag antibody. Each well contained 3 μg protein. (M) Prestained protein marker, ( 1 ) proTHI2.1-TRX, ( 2 ) proTHI2.2-TRX, ( 3 ) proTHI2.3-TRX, ( 4 ) proTHI2.4-TRX

    Techniques Used: Purification, Staining, Western Blot, Marker

    8) Product Images from "Evaluation of a Plasmodium-Specific Carrier Protein To Enhance Production of Recombinant Pfs25, a Leading Transmission-Blocking Vaccine Candidate"

    Article Title: Evaluation of a Plasmodium-Specific Carrier Protein To Enhance Production of Recombinant Pfs25, a Leading Transmission-Blocking Vaccine Candidate

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00486-17

    Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.
    Figure Legend Snippet: Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.

    Techniques Used: Expressing, Construct, Transformation Assay, SDS Page, Staining

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • shuffle strain c3030  (New England Biolabs)
    93
    New England Biolabs shuffle strain c3030
    Cytoplamic expression of proTHI-TRX fusion proteins in strain <t>C3030.</t> For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein
    Shuffle Strain C3030, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/shuffle strain c3030/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    shuffle strain c3030 - by Bioz Stars, 2022-07
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Cytoplamic expression of proTHI-TRX fusion proteins in strain C3030. For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein

    Journal: Biotechnology Letters

    Article Title: Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli

    doi: 10.1007/s10529-013-1180-z

    Figure Lengend Snippet: Cytoplamic expression of proTHI-TRX fusion proteins in strain C3030. For all fusion proteins, 1 ml of cell culture was pelleted and dissolved in 100 μl sample buffer. 10 μl from this extract and an equivalent amount for total soluble cytoplasmic fractions were separated on Tricine/SDS gels. (M) Protein marker, ( 1 ) un-induced crude extract, ( 2 ) induced crude extract, ( 3 ) total soluble fraction taken after cell lysis by sonication, ( 4 ) insoluble fraction after sonication. Red stars indicate the 25 kDa fusion protein

    Article Snippet: The amount of fusion protein that could be produced from the SHuffle strain C3030 is shown in Table and was higher than obtained with Rosetta(DE3)pLysS.

    Techniques: Expressing, Cell Culture, Marker, Lysis, Sonication

    Comparison of Ni–NTA purified proTHI-TRX fusion proteins from strain C3030. a Coomassie Brilliant Blue staining. b Western blot with anti-His tag antibody. Each well contained 3 μg protein. (M) Prestained protein marker, ( 1 ) proTHI2.1-TRX, ( 2 ) proTHI2.2-TRX, ( 3 ) proTHI2.3-TRX, ( 4 ) proTHI2.4-TRX

    Journal: Biotechnology Letters

    Article Title: Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli

    doi: 10.1007/s10529-013-1180-z

    Figure Lengend Snippet: Comparison of Ni–NTA purified proTHI-TRX fusion proteins from strain C3030. a Coomassie Brilliant Blue staining. b Western blot with anti-His tag antibody. Each well contained 3 μg protein. (M) Prestained protein marker, ( 1 ) proTHI2.1-TRX, ( 2 ) proTHI2.2-TRX, ( 3 ) proTHI2.3-TRX, ( 4 ) proTHI2.4-TRX

    Article Snippet: The amount of fusion protein that could be produced from the SHuffle strain C3030 is shown in Table and was higher than obtained with Rosetta(DE3)pLysS.

    Techniques: Purification, Staining, Western Blot, Marker

    Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.

    Journal: Infection and Immunity

    Article Title: Evaluation of a Plasmodium-Specific Carrier Protein To Enhance Production of Recombinant Pfs25, a Leading Transmission-Blocking Vaccine Candidate

    doi: 10.1128/IAI.00486-17

    Figure Lengend Snippet: Expression of chimeric r Pf s25/8(CΔS) and unfused r Pf s25. (A) Schematic depiction of expression constructs for the production of r Pf s25/8(CΔS) and r Pf s25. Expression plasmids for chimeric r Pf s25/8(CΔS) or unfused r Pf s25 were transformed into E. coli SHuffle T7 Express lysY cells. (B and C) r Pf s25/8(CΔS) lysates harvested before ( T 0 ) or 3 h after ( T 3 ) induction were separated by SDS-PAGE (10% gel) under reducing conditions, followed by Coomassie blue staining (B) or immunoblot analysis (C) using rabbit-anti-r Pf MSP8 IgG. The asterisk highlights r Pf s25/8(CΔS) at the predicted size. (D and E) The expression of unfused r Pf s25 was assessed as described above, on 12% polyacrylamide gels under reducing conditions, followed by Coomassie blue staining (D) or immunoblot analysis (E) using an anti-His MAb. The asterisk highlights r Pf s25 at the predicted size.

    Article Snippet: The r Pf s25 expression construct was transformed into SHuffle T7 Express lysY competent E. coli cells (New England BioLabs).

    Techniques: Expressing, Construct, Transformation Assay, SDS Page, Staining

    Expression screening in E. coli . Expression screening was carried out in 96-well microtiter plates to identify high producers for three different target proteins. The promoter, protein fusion partner and E. coli strain were varied. a IMPI, b BR021, c AFP. Rosetta-gami 2 Rosetta-gami 2 (DE3) pLysS, Origami Origami 2, SHuffle SHuffle T7 Express lysY, BL21 BL21 (DE3), C41 OverExpress C41 (DE3) pLysS, C43 OverExpress C43 (DE3) pLysS

    Journal: Microbial Cell Factories

    Article Title: A high-throughput expression screening platform to optimize the production of antimicrobial peptides

    doi: 10.1186/s12934-017-0637-5

    Figure Lengend Snippet: Expression screening in E. coli . Expression screening was carried out in 96-well microtiter plates to identify high producers for three different target proteins. The promoter, protein fusion partner and E. coli strain were varied. a IMPI, b BR021, c AFP. Rosetta-gami 2 Rosetta-gami 2 (DE3) pLysS, Origami Origami 2, SHuffle SHuffle T7 Express lysY, BL21 BL21 (DE3), C41 OverExpress C41 (DE3) pLysS, C43 OverExpress C43 (DE3) pLysS

    Article Snippet: Transformation of E. coli expression strains Six different E. coli strains were used for expression screening: Rosetta-gami 2 (DE3) pLysS (Merck Millipore), Origami 2 (Merck Millipore), BL21 (DE3) (NEB), SHuffle T7 Express lysY (NEB), OverExpress C41 (DE3) pLysS (Sigma-Aldrich), OverExpress C43 (DE3) pLysS (Sigma-Aldrich).

    Techniques: Expressing

    Analysis of oxidative stress tolerance of E. coli SHuffle T7 Express cells overexpressing OsCSD1 and OsCSD4. (A) Comparative analysis of growth of E. coli cells (absorbance at 600 nm) containing pET28a (empty vector), pET28a-OsCSD1, and pET28a-OsCSD4 plasmids. Cells induced with IPTG were treated with increasing methyl viologen concentration (0–0.500 mM) and monitored spectrophotometrically. The experiment was repeated three times and data are represented as mean value ± SD. Statistical significance is indicated by * p

    Journal: Frontiers in Plant Science

    Article Title: Molecular and Biochemical Analysis of Duplicated Cytosolic CuZn Superoxide Dismutases of Rice and in silico Analysis in Plants

    doi: 10.3389/fpls.2022.864330

    Figure Lengend Snippet: Analysis of oxidative stress tolerance of E. coli SHuffle T7 Express cells overexpressing OsCSD1 and OsCSD4. (A) Comparative analysis of growth of E. coli cells (absorbance at 600 nm) containing pET28a (empty vector), pET28a-OsCSD1, and pET28a-OsCSD4 plasmids. Cells induced with IPTG were treated with increasing methyl viologen concentration (0–0.500 mM) and monitored spectrophotometrically. The experiment was repeated three times and data are represented as mean value ± SD. Statistical significance is indicated by * p

    Article Snippet: Briefly, E. coli SHuffle T7 Express cells containing recombinant pET28a-OsCSD1 or pE28a-OsCSD4 plasmid were grown overnight at 30°C in LB medium containing kanamycin (25 μg ml–1 , LB-Kan+ ).

    Techniques: Plasmid Preparation, Concentration Assay