t7 shuffle  (New England Biolabs)


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    Structured Review

    New England Biolabs t7 shuffle
    Experiments to compare the yield of <t>T7</t> SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    T7 Shuffle, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t7 shuffle/product/New England Biolabs
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    t7 shuffle - by Bioz Stars, 2022-07
    96/100 stars

    Images

    1) Product Images from "Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds"

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    Journal: bioRxiv

    doi: 10.1101/2019.12.19.883413

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    Figure Legend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Techniques Used: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.
    Figure Legend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Techniques Used: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).
    Figure Legend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Techniques Used: Modification

    2) Product Images from "Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds"

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    Journal: bioRxiv

    doi: 10.1101/2019.12.19.883413

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    Figure Legend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Techniques Used: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.
    Figure Legend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Techniques Used: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).
    Figure Legend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Techniques Used: Modification

    3) Product Images from "Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds"

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    Journal: bioRxiv

    doi: 10.1101/2019.12.19.883413

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    Figure Legend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Techniques Used: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.
    Figure Legend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Techniques Used: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).
    Figure Legend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Techniques Used: Modification

    4) Product Images from "Expression of human ACE2 N-terminal domain, part of the receptor for SARS-CoV-2, in fusion with maltose binding protein, E. coli ribonuclease I and human RNase A"

    Article Title: Expression of human ACE2 N-terminal domain, part of the receptor for SARS-CoV-2, in fusion with maltose binding protein, E. coli ribonuclease I and human RNase A

    Journal: bioRxiv

    doi: 10.1101/2021.01.31.429007

    Expression and purification of E. coli RNase III and RNase activity assay on dsRNA. A. RNase III expression level in three E. coli T7 strains: T7 Shuffle (C3026), T7 Express with lacI q and LysY (C3013), and Nico (λDE3). B. Purified RNase III from nickel-NTA agarose column chromatography and Ni magnetic beads. C. Ribonuclease activity assay on dsRNA.
    Figure Legend Snippet: Expression and purification of E. coli RNase III and RNase activity assay on dsRNA. A. RNase III expression level in three E. coli T7 strains: T7 Shuffle (C3026), T7 Express with lacI q and LysY (C3013), and Nico (λDE3). B. Purified RNase III from nickel-NTA agarose column chromatography and Ni magnetic beads. C. Ribonuclease activity assay on dsRNA.

    Techniques Used: Expressing, Purification, Activity Assay, Column Chromatography, Magnetic Beads

    Comparison of protein expression in three E. coli strains: NEB Turbo, NEB Express, T7 SHuffle (K strain). MBP-ACE2NTD (ACE), MBP-TMPRSS2 (PRS, lacking the transmembrane domain), MBP-RNase I (RI), MBP-RNase A (RA). A. SDS-PAGE analysis of total proteins in cell lysate. B. SDS-PAGE analysis of soluble proteins (supernatant) in cell lysate. “*” indicates the expected target protein.
    Figure Legend Snippet: Comparison of protein expression in three E. coli strains: NEB Turbo, NEB Express, T7 SHuffle (K strain). MBP-ACE2NTD (ACE), MBP-TMPRSS2 (PRS, lacking the transmembrane domain), MBP-RNase I (RI), MBP-RNase A (RA). A. SDS-PAGE analysis of total proteins in cell lysate. B. SDS-PAGE analysis of soluble proteins (supernatant) in cell lysate. “*” indicates the expected target protein.

    Techniques Used: Expressing, SDS Page

    5) Product Images from "Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein, E. coli Ribonuclease I and Human RNase A"

    Article Title: Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein, E. coli Ribonuclease I and Human RNase A

    Journal: Frontiers in Microbiology

    doi: 10.3389/fmicb.2021.660149

    Expression and purification of E. coli RNase III and RNase activity assay on dsRNA. (A) RNase III expression level in three E. coli T7 strains: T7 Shuffle (C3026, K strain), T7 Express with lacI q and LysY (C3013), and Nico (λDE3). (B) Purified RNase III from nickel-NTA agarose column chromatography and Ni magnetic beads. (C) Ribonuclease activity assay on dsRNA (40 mer duplex and dsRNA ladder).
    Figure Legend Snippet: Expression and purification of E. coli RNase III and RNase activity assay on dsRNA. (A) RNase III expression level in three E. coli T7 strains: T7 Shuffle (C3026, K strain), T7 Express with lacI q and LysY (C3013), and Nico (λDE3). (B) Purified RNase III from nickel-NTA agarose column chromatography and Ni magnetic beads. (C) Ribonuclease activity assay on dsRNA (40 mer duplex and dsRNA ladder).

    Techniques Used: Expressing, Purification, Activity Assay, Column Chromatography, Magnetic Beads

    6) Product Images from "Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds"

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    Journal: bioRxiv

    doi: 10.1101/2019.12.19.883413

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    Figure Legend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Techniques Used: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.
    Figure Legend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Techniques Used: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).
    Figure Legend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Techniques Used: Modification

    7) Product Images from "Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds"

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    Journal: bioRxiv

    doi: 10.1101/2019.12.19.883413

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    Figure Legend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Techniques Used: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.
    Figure Legend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Techniques Used: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).
    Figure Legend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Techniques Used: Modification

    8) Product Images from "Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds"

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    Journal: bioRxiv

    doi: 10.1101/2019.12.19.883413

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    Figure Legend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Techniques Used: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.
    Figure Legend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Techniques Used: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).
    Figure Legend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Techniques Used: Modification

    9) Product Images from "Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds"

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    Journal: bioRxiv

    doi: 10.1101/2019.12.19.883413

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    Figure Legend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Techniques Used: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.
    Figure Legend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Techniques Used: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).
    Figure Legend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Techniques Used: Modification

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  • 96
    New England Biolabs t7 shuffle
    Experiments to compare the yield of <t>T7</t> SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).
    T7 Shuffle, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t7 shuffle/product/New England Biolabs
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    t7 shuffle - by Bioz Stars, 2022-07
    96/100 stars
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    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
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    97
    New England Biolabs shuffle t7 express
    Expression systems for recombinant GF production. (A) Small-scale protein expression screening used to identify the expression vector and host strain combination capable of facilitating cytoplasmic soluble protein expression. The band corresponding to the protein of interest is marked with (*). T - total cell lysate; S - soluble fraction. (B) Expression vector and host strain combinations for successful expression and purification of soluble, bioactive growth factors. (^) denotes instances where the use of SHuffle <t>T7</t> Express was required for soluble expression of some orthologs.
    Shuffle T7 Express, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/shuffle t7 express/product/New England Biolabs
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    shuffle t7 express - by Bioz Stars, 2022-07
    97/100 stars
      Buy from Supplier

    Image Search Results


    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Journal: bioRxiv

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    doi: 10.1101/2019.12.19.883413

    Figure Lengend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Article Snippet: To investigate this, we expressed sfGFP using BL21 DE3 Star, KGK10, and T7 SHuffle.

    Techniques: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Journal: bioRxiv

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    doi: 10.1101/2019.12.19.883413

    Figure Lengend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Article Snippet: To investigate this, we expressed sfGFP using BL21 DE3 Star, KGK10, and T7 SHuffle.

    Techniques: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Journal: bioRxiv

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    doi: 10.1101/2019.12.19.883413

    Figure Lengend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Article Snippet: To investigate this, we expressed sfGFP using BL21 DE3 Star, KGK10, and T7 SHuffle.

    Techniques: Modification

    Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Journal: bioRxiv

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    doi: 10.1101/2019.12.19.883413

    Figure Lengend Snippet: Experiments to compare the yield of T7 SHuffle ® , KGK10, BL21 DE3 Star, and the PURE frex 2.1 kit. KGK10 #1 is carefully fermented KGK10 extract that was provided by the Swartz lab. KGK10 #2 is grown in-house using a shake flask. (A) Gluc signal comparisons at a gain of 100 without PURE frex data (n=3). (B) Gluc signal comparisons with an instrument gain of 80 so PURE frex data does not saturate the detector. (C) Expression of sfGFP to compare yield of proteins without disulfide bonds over 16 hr (n=3). (D) Is a ratio of oxidation potential/productivity using a YFP-mCherry fusion where a S-S bond has been introduced into a YFP variant (n=3).

    Article Snippet: To investigate this, we expressed sfGFP using BL21 DE3 Star, KGK10, and T7 SHuffle.

    Techniques: Expressing, Variant Assay

    Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Journal: bioRxiv

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    doi: 10.1101/2019.12.19.883413

    Figure Lengend Snippet: Experiments to optimize expression from T7 Shuffle extract. (A) Response surface fit to determine optimal growth conditions for sfGFP expression; z axis shows fluorescence (B) Response surface fit to determine optimal growth conditions for Gluc expression; z axis shows luminescence.

    Article Snippet: To investigate this, we expressed sfGFP using BL21 DE3 Star, KGK10, and T7 SHuffle.

    Techniques: Expressing, Fluorescence

    Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Journal: bioRxiv

    Article Title: Simple, Functional, Inexpensive Cell Extract for in vitro Prototyping of Proteins with Disulfide Bonds

    doi: 10.1101/2019.12.19.883413

    Figure Lengend Snippet: Schematic of mechanisms that affect disulfide bond formation and implications in the T7 Shuffle strain. (A) Oxidation via DsbA forms bonds between thiol groups on cysteines. (B) DsbC enzymes proofread proteins and isomerize disulfide bonds. (C) Reduction can occur via trxB and (D) gor enzymes that cleave disulfide bonds on the protein. (E) The T7 SHuffle ® strain is engineered to support disulfide bond formation by eliminating reducing enzymes and overexpressing the DsbC chaperone. This figure has been modified from a published schematic on disulfide bond formation ( Ke and Berkmen, 2014 ).

    Article Snippet: To investigate this, we expressed sfGFP using BL21 DE3 Star, KGK10, and T7 SHuffle.

    Techniques: Modification

    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 systems for recombinant GF production. (A) Small-scale protein expression screening used to identify the expression vector and host strain combination capable of facilitating cytoplasmic soluble protein expression. The band corresponding to the protein of interest is marked with (*). T - total cell lysate; S - soluble fraction. (B) Expression vector and host strain combinations for successful expression and purification of soluble, bioactive growth factors. (^) denotes instances where the use of SHuffle T7 Express was required for soluble expression of some orthologs.

    Journal: bioRxiv

    Article Title: Recombinant production of growth factors for application in cell culture

    doi: 10.1101/2022.02.15.480596

    Figure Lengend Snippet: Expression systems for recombinant GF production. (A) Small-scale protein expression screening used to identify the expression vector and host strain combination capable of facilitating cytoplasmic soluble protein expression. The band corresponding to the protein of interest is marked with (*). T - total cell lysate; S - soluble fraction. (B) Expression vector and host strain combinations for successful expression and purification of soluble, bioactive growth factors. (^) denotes instances where the use of SHuffle T7 Express was required for soluble expression of some orthologs.

    Article Snippet: For protein expression, BL21 (DE3) Gold, Shuffle T7 express (NEB), Origami B (DE3), Rosetta Gami B (DE3) (EMD-Millipore) competent cells were used.

    Techniques: Expressing, Recombinant, Plasmid Preparation, Purification

    Recombinant GF production. Scale up of protein expressions for (A) FGF-2 AND FGF-1 cloned in pMCSG53 vector with N-terminal His6x tag and expressed in BL21(DE3) Gold cells. Targets include F1 (FGF2_Atlantic salmon); F2 (FGF2_Pufferfish); F3 (FGF1_Sheep); F4 (FGF1_Bovine) (B) PDGF-BB expressed in SHuffle T7 express cells. Target shown is P1 (PDGFBB_Cormorant) (C) IGF-1/IGF-2 cloned in pMCSG53-His6x-DsbC /pMCSG53-His6x-SUMO and expressed in SHuffle T7 express cells. Targets include ( K1 ) IGF1_Bovine (SUMO-His6x tag); ( K2 ) IGF1_Bovine (DsbC-His6x tag); (K3 ) IGF1_Goose; (K4 ) IGF1_Frog; ( J1 ) IGF2_Human; ( J2 ) IGF2_Bovine; ( J3 ) IGF2_Nile tilapia (D) TGFβ-1 cloned in pMCSG53-His6x-DsbC and expressed in SHuffle T7 express cells. Targets shown are TGFβ1_human ( T1 ); TGFβ−1_bovine ( T2 ); TGFβ−1_chicken ( T3 ); TGFβ−1_little egret ( T4 ). UC =uncut before TEV digest; C =48h post-TEV digest; TEV protease runs at 25 kDa (marked with ^). After the TEV digest and a second Ni-NTA affinity chromatography step, the concentrated, purified FGF-2/FGF-1 runs at 15 kDa on an SDS-PAGE (marked with ) shown in (A) . PDGF-BB runs at 15 kDa corresponding to the monomer (marked with ⊇) shown in (B) . DsbC fusion IGF-1/IGF-2 runs at 35 kDa (marked with *). IGF1-SUMO runs at 20 kDa (marked with **), as seen in (C) . DsbC-TGFβ-1 runs at 40 kDa (marked with # ).

    Journal: bioRxiv

    Article Title: Recombinant production of growth factors for application in cell culture

    doi: 10.1101/2022.02.15.480596

    Figure Lengend Snippet: Recombinant GF production. Scale up of protein expressions for (A) FGF-2 AND FGF-1 cloned in pMCSG53 vector with N-terminal His6x tag and expressed in BL21(DE3) Gold cells. Targets include F1 (FGF2_Atlantic salmon); F2 (FGF2_Pufferfish); F3 (FGF1_Sheep); F4 (FGF1_Bovine) (B) PDGF-BB expressed in SHuffle T7 express cells. Target shown is P1 (PDGFBB_Cormorant) (C) IGF-1/IGF-2 cloned in pMCSG53-His6x-DsbC /pMCSG53-His6x-SUMO and expressed in SHuffle T7 express cells. Targets include ( K1 ) IGF1_Bovine (SUMO-His6x tag); ( K2 ) IGF1_Bovine (DsbC-His6x tag); (K3 ) IGF1_Goose; (K4 ) IGF1_Frog; ( J1 ) IGF2_Human; ( J2 ) IGF2_Bovine; ( J3 ) IGF2_Nile tilapia (D) TGFβ-1 cloned in pMCSG53-His6x-DsbC and expressed in SHuffle T7 express cells. Targets shown are TGFβ1_human ( T1 ); TGFβ−1_bovine ( T2 ); TGFβ−1_chicken ( T3 ); TGFβ−1_little egret ( T4 ). UC =uncut before TEV digest; C =48h post-TEV digest; TEV protease runs at 25 kDa (marked with ^). After the TEV digest and a second Ni-NTA affinity chromatography step, the concentrated, purified FGF-2/FGF-1 runs at 15 kDa on an SDS-PAGE (marked with ) shown in (A) . PDGF-BB runs at 15 kDa corresponding to the monomer (marked with ⊇) shown in (B) . DsbC fusion IGF-1/IGF-2 runs at 35 kDa (marked with *). IGF1-SUMO runs at 20 kDa (marked with **), as seen in (C) . DsbC-TGFβ-1 runs at 40 kDa (marked with # ).

    Article Snippet: For protein expression, BL21 (DE3) Gold, Shuffle T7 express (NEB), Origami B (DE3), Rosetta Gami B (DE3) (EMD-Millipore) competent cells were used.

    Techniques: Recombinant, Clone Assay, Plasmid Preparation, Affinity Chromatography, Purification, SDS Page