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SCIEX x500b
X500b, supplied by SCIEX, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/x500b/product/SCIEX
Average 95 stars, based on 1 article reviews
Price from $9.99 to $1999.99
x500b - by Bioz Stars, 2022-07
95/100 stars

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    SCIEX x500b mass spectrometer
    Two development samples from different steps in the production of recombinant human GM-CSF were analyzed as intact proteins by RP-LC coupled to UV (upper picture) and ESI–MS. The MS data from the main UV peak were deconvoluted to obtain the most abundant proteoforms (lower picture). The intact proteins elute at 28 min. A A methionylated sample, before addition of proteases cleaving excessive N-terminal methionine, contained two species: the methionylated GM-CSF and the same species with an additional <t>mass</t> of 70 Da. B A sample which had been through all processing steps contained mainly the native protein (with an N-terminal alanine residue) but also lower amounts of the native protein + 70 Da and the methionylated protein + 70 Da. The location of the modification cannot be determined using intact mass analysis
    X500b Mass Spectrometer, supplied by SCIEX, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/x500b mass spectrometer/product/SCIEX
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    x500b mass spectrometer - by Bioz Stars, 2022-07
    86/100 stars
      Buy from Supplier

    x500b  (SCIEX)
    95
    SCIEX x500b
    Two development samples from different steps in the production of recombinant human GM-CSF were analyzed as intact proteins by RP-LC coupled to UV (upper picture) and ESI–MS. The MS data from the main UV peak were deconvoluted to obtain the most abundant proteoforms (lower picture). The intact proteins elute at 28 min. A A methionylated sample, before addition of proteases cleaving excessive N-terminal methionine, contained two species: the methionylated GM-CSF and the same species with an additional <t>mass</t> of 70 Da. B A sample which had been through all processing steps contained mainly the native protein (with an N-terminal alanine residue) but also lower amounts of the native protein + 70 Da and the methionylated protein + 70 Da. The location of the modification cannot be determined using intact mass analysis
    X500b, supplied by SCIEX, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/x500b/product/SCIEX
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    x500b - by Bioz Stars, 2022-07
    95/100 stars
      Buy from Supplier

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    Two development samples from different steps in the production of recombinant human GM-CSF were analyzed as intact proteins by RP-LC coupled to UV (upper picture) and ESI–MS. The MS data from the main UV peak were deconvoluted to obtain the most abundant proteoforms (lower picture). The intact proteins elute at 28 min. A A methionylated sample, before addition of proteases cleaving excessive N-terminal methionine, contained two species: the methionylated GM-CSF and the same species with an additional mass of 70 Da. B A sample which had been through all processing steps contained mainly the native protein (with an N-terminal alanine residue) but also lower amounts of the native protein + 70 Da and the methionylated protein + 70 Da. The location of the modification cannot be determined using intact mass analysis

    Journal: Amino Acids

    Article Title: Characterization of a novel + 70 Da modification in rhGM-CSF expressed in E. coli using chemical assays in combination with mass spectrometry

    doi: 10.1007/s00726-021-03004-9

    Figure Lengend Snippet: Two development samples from different steps in the production of recombinant human GM-CSF were analyzed as intact proteins by RP-LC coupled to UV (upper picture) and ESI–MS. The MS data from the main UV peak were deconvoluted to obtain the most abundant proteoforms (lower picture). The intact proteins elute at 28 min. A A methionylated sample, before addition of proteases cleaving excessive N-terminal methionine, contained two species: the methionylated GM-CSF and the same species with an additional mass of 70 Da. B A sample which had been through all processing steps contained mainly the native protein (with an N-terminal alanine residue) but also lower amounts of the native protein + 70 Da and the methionylated protein + 70 Da. The location of the modification cannot be determined using intact mass analysis

    Article Snippet: Peptide mapping of the methionylated GM-CSF development sample was performed using an Exion system coupled to an SCIEX x500b mass spectrometer.

    Techniques: Recombinant, Modification

    MS/MS spectra from low m/z ions after fragmentation of the N-terminal peptide MAPARSPSPSTQPWEHVNAIQE in the methionylated development sample of GM-CSF. The spectra from the 3 + charged precursor ion of A the non-modified peptide and B the + 70 Da modified peptide are shown. The modification mass was calculated by taking the m/z difference between the daughter ions from the two peptides for ions a 1 , a 2 , and b 2

    Journal: Amino Acids

    Article Title: Characterization of a novel + 70 Da modification in rhGM-CSF expressed in E. coli using chemical assays in combination with mass spectrometry

    doi: 10.1007/s00726-021-03004-9

    Figure Lengend Snippet: MS/MS spectra from low m/z ions after fragmentation of the N-terminal peptide MAPARSPSPSTQPWEHVNAIQE in the methionylated development sample of GM-CSF. The spectra from the 3 + charged precursor ion of A the non-modified peptide and B the + 70 Da modified peptide are shown. The modification mass was calculated by taking the m/z difference between the daughter ions from the two peptides for ions a 1 , a 2 , and b 2

    Article Snippet: Peptide mapping of the methionylated GM-CSF development sample was performed using an Exion system coupled to an SCIEX x500b mass spectrometer.

    Techniques: Tandem Mass Spectroscopy, Modification