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    Thermo Fisher heated electrospray ionization source h esi
    Characterisation of Lb pro ubiquitin cleavage. a , Representative raw spectrum of Lb pro -treated Lys48-linked diubiquitin (diUb) analysed by <t>electrospray</t> ionization MS. Two species arise due to internal cleavage of ubiquitin after Arg74. One scan is shown from analysis performed in triplicate. b , After 24 h of Lb pro treatment, diubiquitin was further supplemented with fresh Lb pro and incubated for an additional 24 h. There are no changes in ubiquitin band intensities, suggesting that Lb pro products are stable. Lys27 diubiquitin in this panel and in was generated chemically from synthetically produced ubiquitin and was refolded; this generates a variable fraction of substrate that cannot be hydrolysed by DUBs, leading to apparent lower activity due to incomplete hydrolysis. Diubiquitin cleavage assays were performed in duplicate. c , Model of ubiquitin cleavage by Lb pro . Ubiquitin (green) was modelled based on the crystal structure of Lb pro ). A close-up view shows the C-terminus of ubiquitin placed across the active site, enabling cleavage between Arg74 and Gly75. Fig. 1a
    Heated Electrospray Ionization Source H Esi, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 178 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 178 article reviews
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    heated electrospray ionization source h esi - by Bioz Stars, 2020-07
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    85
    Thermo Fisher heated esi ii source
    Characterisation of Lb pro ubiquitin cleavage. a , Representative raw spectrum of Lb pro -treated Lys48-linked diubiquitin (diUb) analysed by <t>electrospray</t> ionization MS. Two species arise due to internal cleavage of ubiquitin after Arg74. One scan is shown from analysis performed in triplicate. b , After 24 h of Lb pro treatment, diubiquitin was further supplemented with fresh Lb pro and incubated for an additional 24 h. There are no changes in ubiquitin band intensities, suggesting that Lb pro products are stable. Lys27 diubiquitin in this panel and in was generated chemically from synthetically produced ubiquitin and was refolded; this generates a variable fraction of substrate that cannot be hydrolysed by DUBs, leading to apparent lower activity due to incomplete hydrolysis. Diubiquitin cleavage assays were performed in duplicate. c , Model of ubiquitin cleavage by Lb pro . Ubiquitin (green) was modelled based on the crystal structure of Lb pro ). A close-up view shows the C-terminus of ubiquitin placed across the active site, enabling cleavage between Arg74 and Gly75. Fig. 1a
    Heated Esi Ii Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/heated esi ii source/product/Thermo Fisher
    Average 85 stars, based on 36 article reviews
    Price from $9.99 to $1999.99
    heated esi ii source - by Bioz Stars, 2020-07
    85/100 stars
      Buy from Supplier

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    Characterisation of Lb pro ubiquitin cleavage. a , Representative raw spectrum of Lb pro -treated Lys48-linked diubiquitin (diUb) analysed by electrospray ionization MS. Two species arise due to internal cleavage of ubiquitin after Arg74. One scan is shown from analysis performed in triplicate. b , After 24 h of Lb pro treatment, diubiquitin was further supplemented with fresh Lb pro and incubated for an additional 24 h. There are no changes in ubiquitin band intensities, suggesting that Lb pro products are stable. Lys27 diubiquitin in this panel and in was generated chemically from synthetically produced ubiquitin and was refolded; this generates a variable fraction of substrate that cannot be hydrolysed by DUBs, leading to apparent lower activity due to incomplete hydrolysis. Diubiquitin cleavage assays were performed in duplicate. c , Model of ubiquitin cleavage by Lb pro . Ubiquitin (green) was modelled based on the crystal structure of Lb pro ). A close-up view shows the C-terminus of ubiquitin placed across the active site, enabling cleavage between Arg74 and Gly75. Fig. 1a

    Journal: Nature

    Article Title: Insights into ubiquitin chain architecture using Ub-clipping

    doi: 10.1038/s41586-019-1482-y

    Figure Lengend Snippet: Characterisation of Lb pro ubiquitin cleavage. a , Representative raw spectrum of Lb pro -treated Lys48-linked diubiquitin (diUb) analysed by electrospray ionization MS. Two species arise due to internal cleavage of ubiquitin after Arg74. One scan is shown from analysis performed in triplicate. b , After 24 h of Lb pro treatment, diubiquitin was further supplemented with fresh Lb pro and incubated for an additional 24 h. There are no changes in ubiquitin band intensities, suggesting that Lb pro products are stable. Lys27 diubiquitin in this panel and in was generated chemically from synthetically produced ubiquitin and was refolded; this generates a variable fraction of substrate that cannot be hydrolysed by DUBs, leading to apparent lower activity due to incomplete hydrolysis. Diubiquitin cleavage assays were performed in duplicate. c , Model of ubiquitin cleavage by Lb pro . Ubiquitin (green) was modelled based on the crystal structure of Lb pro ). A close-up view shows the C-terminus of ubiquitin placed across the active site, enabling cleavage between Arg74 and Gly75. Fig. 1a

    Article Snippet: Samples were ionized using a Heated Electrospray Ionization source (HESI-II, Thermo Fisher Scientific) at a flow rate of 5 μL/min.

    Techniques: Mass Spectrometry, Incubation, Generated, Produced, Activity Assay