Abstract
Analysis of proteins by immunoblotting in general refers to detection under denatured condition. Immunoblotting GAPDH under denatured or SDS-PAGE condition enables the recognition and identification of any quantitative and qualitative changes in GAPDH related to the biological or health/disease condition of the cells. However, considering the occurrence of multiple isoforms and also the cross-reactivity of antibodies with similar proteins it is imperative to verify the GAPDH using more than one antibody that recognizes different domains of GAPDH and preferably from different suppliers as well. Especially with the emergence of two-dimensional (2D) electrophoresis detailed biochemical characterization of molecular changes in GAPDH subunits is feasible and may provide insights into their biological function.
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Ganapathy-Kanniappan, S. (2017). Analysis of GAPDH under Denaturing Conditions. In: Advances in GAPDH Protein Analysis: A Functional and Biochemical Approach. Springer, Singapore. https://doi.org/10.1007/978-981-10-7342-7_4
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DOI: https://doi.org/10.1007/978-981-10-7342-7_4
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