trxr1 variants Search Results


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    Thermo Fisher human trxr1
    <t>TrxR1</t> produced using UAG for Sec in absence of both RF1 and a SECIS element resulted in a mixture of Sec-containing enzyme, UAG-truncated variant, and additional forms presumed to be Sec-to-Gln or Sec-to-Lys substituted variants. Shown is an electrospray mass spectrometry analysis of rat TrxR1 produced using the pABC2-rTR UAG plasmid in C321.ΔA host cells. The three major species of enzyme detected corresponded in size to a native Sec-containing variant ( green arrow ), UAG-truncated enzyme ( red arrow ), and a variant likely corresponding to Sec-to-Gln- or Sec-to-Lys-substituted forms ( blue arrow ). See text for further discussion.
    Human Trxr1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human trxr1/product/Thermo Fisher
    Average 92 stars, based on 24 article reviews
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    human trxr1 - by Bioz Stars, 2020-08
    92/100 stars
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    TrxR1 produced using UAG for Sec in absence of both RF1 and a SECIS element resulted in a mixture of Sec-containing enzyme, UAG-truncated variant, and additional forms presumed to be Sec-to-Gln or Sec-to-Lys substituted variants. Shown is an electrospray mass spectrometry analysis of rat TrxR1 produced using the pABC2-rTR UAG plasmid in C321.ΔA host cells. The three major species of enzyme detected corresponded in size to a native Sec-containing variant ( green arrow ), UAG-truncated enzyme ( red arrow ), and a variant likely corresponding to Sec-to-Gln- or Sec-to-Lys-substituted forms ( blue arrow ). See text for further discussion.

    Journal: The Journal of Biological Chemistry

    Article Title: Selenocysteine Insertion at a Predefined UAG Codon in a Release Factor 1 (RF1)-depleted Escherichia coli Host Strain Bypasses Species Barriers in Recombinant Selenoprotein Translation *

    doi: 10.1074/jbc.M117.776310

    Figure Lengend Snippet: TrxR1 produced using UAG for Sec in absence of both RF1 and a SECIS element resulted in a mixture of Sec-containing enzyme, UAG-truncated variant, and additional forms presumed to be Sec-to-Gln or Sec-to-Lys substituted variants. Shown is an electrospray mass spectrometry analysis of rat TrxR1 produced using the pABC2-rTR UAG plasmid in C321.ΔA host cells. The three major species of enzyme detected corresponded in size to a native Sec-containing variant ( green arrow ), UAG-truncated enzyme ( red arrow ), and a variant likely corresponding to Sec-to-Gln- or Sec-to-Lys-substituted forms ( blue arrow ). See text for further discussion.

    Article Snippet: The gene for human TrxR1 was synthesized by a commercial service (GeneArt, ) with codons optimized for expression in E. coli and cloned into the pABC2 vector between XbaI and EagI, which resulted in plasmid pABC2-hTRSUAG .

    Techniques: Produced, Size-exclusion Chromatography, Variant Assay, Mass Spectrometry, Plasmid Preparation

    Production of Sec-containing TrxR1 using UAG for Sec validated with mass spectrometry. Utilizing expression with UAG targeting in C321.ΔA host cells, the purified enzymes were analyzed with electrospray mass spectrometry. These analyses revealed that rat TrxR1 ( top ) as well as human TrxR1 ( bottom ) were purified as dominant forms of intact Sec-containing enzymes ( green arrows ) and with very little UAG-truncated protein detected ( red arrows ). The x axes indicate the mass range analyzed.

    Journal: The Journal of Biological Chemistry

    Article Title: Selenocysteine Insertion at a Predefined UAG Codon in a Release Factor 1 (RF1)-depleted Escherichia coli Host Strain Bypasses Species Barriers in Recombinant Selenoprotein Translation *

    doi: 10.1074/jbc.M117.776310

    Figure Lengend Snippet: Production of Sec-containing TrxR1 using UAG for Sec validated with mass spectrometry. Utilizing expression with UAG targeting in C321.ΔA host cells, the purified enzymes were analyzed with electrospray mass spectrometry. These analyses revealed that rat TrxR1 ( top ) as well as human TrxR1 ( bottom ) were purified as dominant forms of intact Sec-containing enzymes ( green arrows ) and with very little UAG-truncated protein detected ( red arrows ). The x axes indicate the mass range analyzed.

    Article Snippet: The gene for human TrxR1 was synthesized by a commercial service (GeneArt, ) with codons optimized for expression in E. coli and cloned into the pABC2 vector between XbaI and EagI, which resulted in plasmid pABC2-hTRSUAG .

    Techniques: Size-exclusion Chromatography, Mass Spectrometry, Expressing, Purification