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biotinylated molecular mass markers  (Millipore)


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    Millipore biotinylated molecular mass markers
    Biotinylated Molecular Mass Markers, supplied by Millipore, 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/product/biotinylated+molecular+mass+marker/biotinylated+molecular+weight+markers/pmc05418773-85-1-0
    Average 90 stars, based on 1 article reviews
    biotinylated molecular mass markers - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Marker:

    Article Title: Biochemical typing of pathological prion protein in aging cattle with BSE
    Article Snippet: .. A biotinylated molecular mass marker (2 lanes, Sigma) and a C-type brainstem control sample from an average aged (5 years) C-type BSE affected cattle were included on each gel. .. After electrophoresis for 90 min at 150 V and transfer of the proteins to PVDF membranes (Millipore), the membranes were blocked with Prionics blocking buffer or 5% (w/v) non-fat dried milk in TBST.

    Control:

    Article Title: Biochemical typing of pathological prion protein in aging cattle with BSE
    Article Snippet: .. A biotinylated molecular mass marker (2 lanes, Sigma) and a C-type brainstem control sample from an average aged (5 years) C-type BSE affected cattle were included on each gel. .. After electrophoresis for 90 min at 150 V and transfer of the proteins to PVDF membranes (Millipore), the membranes were blocked with Prionics blocking buffer or 5% (w/v) non-fat dried milk in TBST.



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    <t>Biotinylated</t> 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.
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    <t>Biotinylated</t> 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.
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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