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    New England Biolabs t7 shuffle
    Experiments to compare the yield of <t>T7</t> <t>SHuffle</t> ® , 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
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    t7 shuffle - by Bioz Stars, 2022-08
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    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: T7 SHuffle® The supplement recipe used for the designed experiments and initial tests is a modified version of the PANOx-SP system that is improved to form disulfide bonds ( ).

    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: T7 SHuffle® The supplement recipe used for the designed experiments and initial tests is a modified version of the PANOx-SP system that is improved to form disulfide bonds ( ).

    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: T7 SHuffle® The supplement recipe used for the designed experiments and initial tests is a modified version of the PANOx-SP system that is improved to form disulfide bonds ( ).

    Techniques: Modification