Review



q10 anion exchange proteinchip array surfaces  (Bio-Rad)


Bioz Verified Symbol Bio-Rad is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 93
      Buy from Supplier

    Structured Review

    Bio-Rad q10 anion exchange proteinchip array surfaces
    Identification and validation of peak 3790 as prothymosin- α . Mass spectrum of proteins from fraction Q3 that bound to <t>Q10</t> <t>ProteinChip</t> array and was analyzed on QSTAR XL instrument (mass range from 1000 to 4000 m/z).
    Q10 Anion Exchange Proteinchip Array Surfaces, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/q10 anion exchange proteinchip array surfaces/product/Bio-Rad
    Average 93 stars, based on 36 article reviews
    q10 anion exchange proteinchip array surfaces - by Bioz Stars, 2026-06
    93/100 stars

    Images

    1) Product Images from "Proteomic Analysis of Pichindé virus Infection Identifies Differential Expression of Prothymosin- α"

    Article Title: Proteomic Analysis of Pichindé virus Infection Identifies Differential Expression of Prothymosin- α

    Journal: Journal of Biomedicine and Biotechnology

    doi: 10.1155/2010/956823

    Identification and validation of peak 3790 as prothymosin- α . Mass spectrum of proteins from fraction Q3 that bound to Q10 ProteinChip array and was analyzed on QSTAR XL instrument (mass range from 1000 to 4000 m/z).
    Figure Legend Snippet: Identification and validation of peak 3790 as prothymosin- α . Mass spectrum of proteins from fraction Q3 that bound to Q10 ProteinChip array and was analyzed on QSTAR XL instrument (mass range from 1000 to 4000 m/z).

    Techniques Used: Biomarker Discovery

    (a) The peptide with m/z approximately 3790 was identified as the fragment of prothymosin alpha by the following MS/MS microsequencing. (b) Mass spectrum of proteins pulled out from cytoplasmic fraction of murine macrophage samples by antiprothymosin alpha which was coupled to protein G agarose beads (mass range from 1000 to 20,000 m/z). Antiprothymosin alpha-coupled protein G agarose beads were incubated with cytoplasmic fraction and eluted proteins were analyzed on NP 20 ProteinChip array.
    Figure Legend Snippet: (a) The peptide with m/z approximately 3790 was identified as the fragment of prothymosin alpha by the following MS/MS microsequencing. (b) Mass spectrum of proteins pulled out from cytoplasmic fraction of murine macrophage samples by antiprothymosin alpha which was coupled to protein G agarose beads (mass range from 1000 to 20,000 m/z). Antiprothymosin alpha-coupled protein G agarose beads were incubated with cytoplasmic fraction and eluted proteins were analyzed on NP 20 ProteinChip array.

    Techniques Used: Tandem Mass Spectroscopy, Incubation



    Similar Products

    q10 anion exchange proteinchip array surfaces  (Bio-Rad)
    93
    Bio-Rad q10 anion exchange proteinchip array surfaces
    Identification and validation of peak 3790 as prothymosin- α . Mass spectrum of proteins from fraction Q3 that bound to <t>Q10</t> <t>ProteinChip</t> array and was analyzed on QSTAR XL instrument (mass range from 1000 to 4000 m/z).
    Q10 Anion Exchange Proteinchip Array Surfaces, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/q10 anion exchange proteinchip array surfaces/product/Bio-Rad
    Average 93 stars, based on 1 article reviews
    q10 anion exchange proteinchip array surfaces - by Bioz Stars, 2026-06
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Identification and validation of peak 3790 as prothymosin- α . Mass spectrum of proteins from fraction Q3 that bound to Q10 ProteinChip array and was analyzed on QSTAR XL instrument (mass range from 1000 to 4000 m/z).

    Journal: Journal of Biomedicine and Biotechnology

    Article Title: Proteomic Analysis of Pichindé virus Infection Identifies Differential Expression of Prothymosin- α

    doi: 10.1155/2010/956823

    Figure Lengend Snippet: Identification and validation of peak 3790 as prothymosin- α . Mass spectrum of proteins from fraction Q3 that bound to Q10 ProteinChip array and was analyzed on QSTAR XL instrument (mass range from 1000 to 4000 m/z).

    Article Snippet: 10 μ L of each fraction was added to 90 μ L 50 mM Tris (pH 8) buffer and was captured on Q10 anion exchange ProteinChip array surfaces (Bio-Rad Laboratories, Hercules, CA) with a bioprocessor Biomek 3000 (Beckman Coulter, Fullerton, CA).

    Techniques: Biomarker Discovery

    (a) The peptide with m/z approximately 3790 was identified as the fragment of prothymosin alpha by the following MS/MS microsequencing. (b) Mass spectrum of proteins pulled out from cytoplasmic fraction of murine macrophage samples by antiprothymosin alpha which was coupled to protein G agarose beads (mass range from 1000 to 20,000 m/z). Antiprothymosin alpha-coupled protein G agarose beads were incubated with cytoplasmic fraction and eluted proteins were analyzed on NP 20 ProteinChip array.

    Journal: Journal of Biomedicine and Biotechnology

    Article Title: Proteomic Analysis of Pichindé virus Infection Identifies Differential Expression of Prothymosin- α

    doi: 10.1155/2010/956823

    Figure Lengend Snippet: (a) The peptide with m/z approximately 3790 was identified as the fragment of prothymosin alpha by the following MS/MS microsequencing. (b) Mass spectrum of proteins pulled out from cytoplasmic fraction of murine macrophage samples by antiprothymosin alpha which was coupled to protein G agarose beads (mass range from 1000 to 20,000 m/z). Antiprothymosin alpha-coupled protein G agarose beads were incubated with cytoplasmic fraction and eluted proteins were analyzed on NP 20 ProteinChip array.

    Article Snippet: 10 μ L of each fraction was added to 90 μ L 50 mM Tris (pH 8) buffer and was captured on Q10 anion exchange ProteinChip array surfaces (Bio-Rad Laboratories, Hercules, CA) with a bioprocessor Biomek 3000 (Beckman Coulter, Fullerton, CA).

    Techniques: Tandem Mass Spectroscopy, Incubation