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biotinylated molecular mass markers  (Bio-Rad)


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    Bio-Rad biotinylated molecular mass markers
    Biotinylated Molecular Mass Markers, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated molecular mass markers/product/Bio-Rad
    Average 90 stars, based on 1 article reviews
    biotinylated molecular mass markers - by Bioz Stars, 2026-05
    90/100 stars

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    Biotinylated plasminogen ligand blot with whole-cell lysates of strain PG50. Whole-cell lysates were fractionated by SDS-12% PAGE (approximately 30 μg/lane), and the proteins were transferred to PVDF and subjected to ligand blotting with 5 nM biotinylated human glu-plasminogen (lanes 2) in the presence (A) or absence (B) of 100 mM ɛ-amino caproic acid. Lanes 1, biotinylated low-molecular-mass markers (Bio-Rad). After ligand analysis, the blots were washed and briefly stained with amido black to show the amount of protein transferred (lanes 3). All blots shown were derived from gels run, transferred, and probed in parallel and were exposed onto the same piece of autoradiograph film so that a direct comparison could be made between them. Note the absence of lysine-dependent plasminogen binding proteins in panel A (lane 2). Molecular masses of prestained molecular mass markers are as indicated.

    Journal:

    Article Title: Cell Surface Antigens of Mycoplasma Species Bovine Group 7 Bind to and Activate Plasminogen.

    doi: 10.1128/IAI.71.8.4823-4827.2003

    Figure Lengend Snippet: Biotinylated plasminogen ligand blot with whole-cell lysates of strain PG50. Whole-cell lysates were fractionated by SDS-12% PAGE (approximately 30 μg/lane), and the proteins were transferred to PVDF and subjected to ligand blotting with 5 nM biotinylated human glu-plasminogen (lanes 2) in the presence (A) or absence (B) of 100 mM ɛ-amino caproic acid. Lanes 1, biotinylated low-molecular-mass markers (Bio-Rad). After ligand analysis, the blots were washed and briefly stained with amido black to show the amount of protein transferred (lanes 3). All blots shown were derived from gels run, transferred, and probed in parallel and were exposed onto the same piece of autoradiograph film so that a direct comparison could be made between them. Note the absence of lysine-dependent plasminogen binding proteins in panel A (lane 2). Molecular masses of prestained molecular mass markers are as indicated.

    Article Snippet: Lanes 1, biotinylated low-molecular-mass markers (Bio-Rad).

    Techniques: Staining, Derivative Assay, Autoradiography, Binding Assay