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reactions cell free transcription translation systems  (New England Biolabs)


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    New England Biolabs reactions cell free transcription translation systems
    Reactions Cell Free Transcription Translation Systems, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 98/100, based on 677 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cell+free+transcription+translation+reactions/PURExpress/us12601018-220-1-5
    Average 98 stars, based on 677 article reviews
    reactions cell free transcription translation systems - by Bioz Stars, 2026-10
    98/100 stars

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    In Vitro:

    Article Title: Programmable RNA-guided DNA endonucleases are widespread in eukaryotes and their viruses.
    Article Snippet: .. Cell-free transcription/translation reactions were carried out using the PURExpress In Vitro Protein Synthesis Kit (NEB) as per the manufacturer’s protocol with half-volume reactions, using 75 ng of template for the protein of interest, 125 ng of template for the corresponding fRNA or ωRNAwith a guide targeting the TAM library, and 30 ng of TAM library plasmid. ..

    Article Title: Biosensors for polyketide extender units and uses thereof
    Article Snippet: .. A premixed solution for cell-free transcription-translation reactions was purchased from New England Biolabs (PURExpress In Vitro Protein Synthesis Kit). ..

    Article Title: Programmable RNA-guided DNA endonucleases are widespread in eukaryotes and their viruses
    Article Snippet: Fanzor protein sequences were E. coli codon–optimized using the Integrated DNA Technologies (IDT) codon optimization tool, and fRNA scaffolds were synthesized by IDT eBlock gene fragments. .. Cell-free transcription/translation reactions were carried out using the PURExpress In Vitro Protein Synthesis Kit (NEB) as per the manufacturer’s protocol with half-volume reactions, using 75 ng of template for the protein of interest, 125 ng of template for the corresponding fRNA or ωRNA with a guide targeting the TAM library, and 30 ng of TAM library plasmid. ..

    Article Title: Programmable RNA-guided DNA endonucleases are widespread in eukaryotes and their viruses
    Article Snippet: .. Cell-free transcription/translation reactions were carried out using the PURExpress In Vitro Protein Synthesis Kit (NEB) as per the manufacturer’s protocol with half-volume reactions using 75 ng of template for the protein of interest and a 100 ng of fRNA or ωRNA. ..

    Article Title: Supplementary Information Development of a genetically-encoded biosensor for detection of polyketide synthase extender units in Escherichia coli
    Article Snippet: .. LCMS m/z 220.0 ([M+H]+).2 Dose-response analysis of the cell-free TX-TL FapR assay A premixed solution for cell-free transcription-translation reactions was purchased from New England Biolabs (PURExpress In Vitro Protein Synthesis Kit). ..

    Plasmid Preparation:

    Article Title: Programmable RNA-guided DNA endonucleases are widespread in eukaryotes and their viruses.
    Article Snippet: .. Cell-free transcription/translation reactions were carried out using the PURExpress In Vitro Protein Synthesis Kit (NEB) as per the manufacturer’s protocol with half-volume reactions, using 75 ng of template for the protein of interest, 125 ng of template for the corresponding fRNA or ωRNAwith a guide targeting the TAM library, and 30 ng of TAM library plasmid. ..

    Article Title: Programmable RNA-guided DNA endonucleases are widespread in eukaryotes and their viruses
    Article Snippet: Fanzor protein sequences were E. coli codon–optimized using the Integrated DNA Technologies (IDT) codon optimization tool, and fRNA scaffolds were synthesized by IDT eBlock gene fragments. .. Cell-free transcription/translation reactions were carried out using the PURExpress In Vitro Protein Synthesis Kit (NEB) as per the manufacturer’s protocol with half-volume reactions, using 75 ng of template for the protein of interest, 125 ng of template for the corresponding fRNA or ωRNA with a guide targeting the TAM library, and 30 ng of TAM library plasmid. ..

    Liquid Chromatography with Mass Spectroscopy:

    Article Title: Supplementary Information Development of a genetically-encoded biosensor for detection of polyketide synthase extender units in Escherichia coli
    Article Snippet: .. LCMS m/z 220.0 ([M+H]+).2 Dose-response analysis of the cell-free TX-TL FapR assay A premixed solution for cell-free transcription-translation reactions was purchased from New England Biolabs (PURExpress In Vitro Protein Synthesis Kit). ..



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    T65 is important, but not essential, for NTase and phosphorylation activity. ( A ) In <t>vitro</t> <t>transcription/translation</t> reactions assessing levels of DHFR control protein produced in the presence of either 5 µM AbiEii WT or AbiEii-p. ( B ) In vitro transcription/translation reactions assessing levels of DHFR control protein produced in the absence and presence of 5 µM AbiEii T65A, AbiEii D192A, or AbiEii-p. Reactions were loaded onto 4-20% gradient gels ran at 180 V for 1 h. ( C ) Densitometric analysis of SDS-PAGE bands from ( B ) corresponding to DHFR. ( D ) Dose-response curves of increasing concentrations of either AbiEii WT or AbiEii T65A plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4A and B . ( E ) Logarithmic dose-response curves of either 5 µM AbiEii WT or AbiEii T65A incubated with increasing concentrations of AbiEi plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4C and D . Logarithmic curves were generated using non-linear regression in Prism (GraphPad). ( F ) Endpoint viable count antitoxicity assays of E. coli DH5α transformed with either pBAD30 empty vector, pTRB482 (AbiEii WT), or pTRB736 (AbiEii T65A), and either pTA100 empty vector or pTRB481 (AbiEi). Overnight cultures were re-seeded into fresh LB supplemented with Ap, Sp and D-glu and grown to mid-log phase. Samples were serially diluted 10 −2 -10 −9 and spotted onto M9A plates containing Ap and Sp, with or without D-glu, L-ara, and IPTG for repression of toxin expression, induction of toxin expression, and induction of antitoxin expression, respectively. Plates were incubated at 37 °C for 48 h, after which they were imaged and colonies counted to determine CFU/ml (one-way ANOVA, P < 0.05). “T” = toxin induced, “TA” = antitoxin + toxin induced. Assays shown are representative of three independent biological replicates and plotted data represent the mean ± SEM.
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    T65 is important, but not essential, for NTase and phosphorylation activity. ( A ) In <t>vitro</t> <t>transcription/translation</t> reactions assessing levels of DHFR control protein produced in the presence of either 5 µM AbiEii WT or AbiEii-p. ( B ) In vitro transcription/translation reactions assessing levels of DHFR control protein produced in the absence and presence of 5 µM AbiEii T65A, AbiEii D192A, or AbiEii-p. Reactions were loaded onto 4-20% gradient gels ran at 180 V for 1 h. ( C ) Densitometric analysis of SDS-PAGE bands from ( B ) corresponding to DHFR. ( D ) Dose-response curves of increasing concentrations of either AbiEii WT or AbiEii T65A plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4A and B . ( E ) Logarithmic dose-response curves of either 5 µM AbiEii WT or AbiEii T65A incubated with increasing concentrations of AbiEi plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4C and D . Logarithmic curves were generated using non-linear regression in Prism (GraphPad). ( F ) Endpoint viable count antitoxicity assays of E. coli DH5α transformed with either pBAD30 empty vector, pTRB482 (AbiEii WT), or pTRB736 (AbiEii T65A), and either pTA100 empty vector or pTRB481 (AbiEi). Overnight cultures were re-seeded into fresh LB supplemented with Ap, Sp and D-glu and grown to mid-log phase. Samples were serially diluted 10 −2 -10 −9 and spotted onto M9A plates containing Ap and Sp, with or without D-glu, L-ara, and IPTG for repression of toxin expression, induction of toxin expression, and induction of antitoxin expression, respectively. Plates were incubated at 37 °C for 48 h, after which they were imaged and colonies counted to determine CFU/ml (one-way ANOVA, P < 0.05). “T” = toxin induced, “TA” = antitoxin + toxin induced. Assays shown are representative of three independent biological replicates and plotted data represent the mean ± SEM.
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    T65 is important, but not essential, for NTase and phosphorylation activity. ( A ) In vitro transcription/translation reactions assessing levels of DHFR control protein produced in the presence of either 5 µM AbiEii WT or AbiEii-p. ( B ) In vitro transcription/translation reactions assessing levels of DHFR control protein produced in the absence and presence of 5 µM AbiEii T65A, AbiEii D192A, or AbiEii-p. Reactions were loaded onto 4-20% gradient gels ran at 180 V for 1 h. ( C ) Densitometric analysis of SDS-PAGE bands from ( B ) corresponding to DHFR. ( D ) Dose-response curves of increasing concentrations of either AbiEii WT or AbiEii T65A plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4A and B . ( E ) Logarithmic dose-response curves of either 5 µM AbiEii WT or AbiEii T65A incubated with increasing concentrations of AbiEi plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4C and D . Logarithmic curves were generated using non-linear regression in Prism (GraphPad). ( F ) Endpoint viable count antitoxicity assays of E. coli DH5α transformed with either pBAD30 empty vector, pTRB482 (AbiEii WT), or pTRB736 (AbiEii T65A), and either pTA100 empty vector or pTRB481 (AbiEi). Overnight cultures were re-seeded into fresh LB supplemented with Ap, Sp and D-glu and grown to mid-log phase. Samples were serially diluted 10 −2 -10 −9 and spotted onto M9A plates containing Ap and Sp, with or without D-glu, L-ara, and IPTG for repression of toxin expression, induction of toxin expression, and induction of antitoxin expression, respectively. Plates were incubated at 37 °C for 48 h, after which they were imaged and colonies counted to determine CFU/ml (one-way ANOVA, P < 0.05). “T” = toxin induced, “TA” = antitoxin + toxin induced. Assays shown are representative of three independent biological replicates and plotted data represent the mean ± SEM.

    Journal: bioRxiv

    Article Title: Antitoxin-induced auto-phosphorylation neutralizes the nucleotidyltransferase toxin AbiEii from Streptococcus agalactiae to safeguard global translation

    doi: 10.64898/2026.01.19.700257

    Figure Lengend Snippet: T65 is important, but not essential, for NTase and phosphorylation activity. ( A ) In vitro transcription/translation reactions assessing levels of DHFR control protein produced in the presence of either 5 µM AbiEii WT or AbiEii-p. ( B ) In vitro transcription/translation reactions assessing levels of DHFR control protein produced in the absence and presence of 5 µM AbiEii T65A, AbiEii D192A, or AbiEii-p. Reactions were loaded onto 4-20% gradient gels ran at 180 V for 1 h. ( C ) Densitometric analysis of SDS-PAGE bands from ( B ) corresponding to DHFR. ( D ) Dose-response curves of increasing concentrations of either AbiEii WT or AbiEii T65A plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4A and B . ( E ) Logarithmic dose-response curves of either 5 µM AbiEii WT or AbiEii T65A incubated with increasing concentrations of AbiEi plotted against DHFR expression, normalized against DHFR expressed in the absence of toxin (100% expression). Data points were generated following densitometric analysis of bands corresponding to DHFR from Supplementary Figs. S4C and D . Logarithmic curves were generated using non-linear regression in Prism (GraphPad). ( F ) Endpoint viable count antitoxicity assays of E. coli DH5α transformed with either pBAD30 empty vector, pTRB482 (AbiEii WT), or pTRB736 (AbiEii T65A), and either pTA100 empty vector or pTRB481 (AbiEi). Overnight cultures were re-seeded into fresh LB supplemented with Ap, Sp and D-glu and grown to mid-log phase. Samples were serially diluted 10 −2 -10 −9 and spotted onto M9A plates containing Ap and Sp, with or without D-glu, L-ara, and IPTG for repression of toxin expression, induction of toxin expression, and induction of antitoxin expression, respectively. Plates were incubated at 37 °C for 48 h, after which they were imaged and colonies counted to determine CFU/ml (one-way ANOVA, P < 0.05). “T” = toxin induced, “TA” = antitoxin + toxin induced. Assays shown are representative of three independent biological replicates and plotted data represent the mean ± SEM.

    Article Snippet: Five μM of purified AbiEii WT or AbiEii-p were added to cell-free transcription/translation protein synthesis reactions (PURExpress ® ; NEB) to quantify changes in DHFR control protein expression.

    Techniques: Phospho-proteomics, Activity Assay, In Vitro, Control, Produced, SDS Page, Expressing, Generated, Incubation, Transformation Assay, Plasmid Preparation