Cloning and the protein isolation of APP gene exone 16 and 17 region

Amyloid Beta Precursor Protein (APP) is a type I transmembrane glycoprotein that plays a central role in the molecular pathogenesis of Alzheimer's disease. Encoded by the APP gene located on the long arm of human chromosome 21 (21q21.3), this protein is involved in key neuronal processes such as synaptic plasticity, cellular adhesion, and neuroprotective signaling pathways. Proteolytic cleavage of APP leads to the formation of Aβ peptides, whose accumulation in the brain contributes to the formation of amyloid plaques—one of the hallmark pathological features of Alzheimer's disease. In this thesis study, the recombinant production of APP protein was aimed. For this purpose, a synthetic vector containing the APP gene fragment was designed and cloned into a suitable expression plasmid using molecular cloning techniques. The recombinant plasmid was then introduced into a prokaryotic host system to achieve target protein expression. Following protein expression, affinity chromatography was employed to purify the protein, and the obtained product was evaluated via SDS-PAGE analysis. As a result, a protocol enabling high-purity production of recombinant APP protein was successfully established. This system is considered to have strong potential as a foundational platform for future studies focusing on peptide-based therapeutics or biomarker development related to APP. Key Words: APP, Alzheimer, Biotechnology, E. coli, Recombinant Protein,