After collecting the lysates, BCA assay immediately comes next to determine the quantity of the lysates to be used for western blot. However, the scaffolds used are plant protein-based, which hypothetically contributes to the total protein concentration of the lysate considering the mechanical and chemical degradation during lysis procedure. Thus, even when loaded with equal protein concentrations per sample, after western blotting, the cultured meat samples show low expression levels. How can i establish a fair comparison of protein expression given the situation?
Do a control where you use an antibody against a protein from your scaffold?
Is there a marker protein you could blot for? You could then normalize the density of your signal of interest to that of the marker protein.
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