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This study focuses on the purification process of Gap1 protein across two distinct batches, utilizing phosphatase treatment to enhance the yield and purity of the protein. Detailed methodologies for each batch, along with comparative analysis, are documented. The results highlight the effectiveness of phosphatase treatment in optimizing the purification process, allowing for improved characterization of Gap1 activity in various biochemical assays. This work aims to provide a framework for effective protein purification techniques in research laboratories.
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