SOLVED: Student performed a Bradford assay and determined the concentration of the protein extract was 1.0 mg/mL. The SDS-PAGE protocol first asks you to mix 25 microliters of your 1.0 mg/mL extract with 75 microliters of buffer. What volume of this protein buffer mixture will you add to your SDS-PAGE gel so that you end up with 5 micrograms of protein on your gel? Show calculations. Pretty sure it is a two-step calculation.

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Purification and Visualization of Lipopolysaccharide from Gram-negative Bacteria by Hot Aqueous-phenol Extraction

SOLVED: Investigators decide to analyze the purity of a preparation of antibody molecules using SDS polyacrylamide-gel electrophoresis (SDS-PAGE). In Lane 1 of the gel, they load a sample of the antibody. In Lane 2, they load an antibody sample that has been treated with a reducing agent called mercaptoethanol, which breaks disulfide linkages. Following electrophoresis, they see distinct bands representing polypeptides with molecular weights of 50 kD and 25 kD in Lane 2, and only one band weighi

How to separate proteins using an Invitrogen precast SDS-PAGE gel

A protein has an apparent mass of 800 kD by gel filtration chromatography, but SDS-PAGE shows a single band at a position corresponding to 200 kD . In an ultracentrifuge, will the protein exhibit a sedimentation coefficient corresponding to 200 kD or 800 kD ? | Numerade