Alzheimer’s disease tauopathy is characterized by the aggregation of tau protein, which can form intracellular fibrillar structures that accumulate within neurons and contribute to cognitive decline. Low-density lipoprotein receptor-related protein 1 (LRP1) is a major receptor that mediates tau internalization. The mLRP4 construct, which contains binding domain 4 (BD4) of LRP1, represents the minimal domain necessary for tau endocytosis. Altered glycosylation patterns are observed in AD, including hyperglycosylation of LRP1. To model this phenomenon, Enhanced Aromatic Sequon (EAS) mutations are made to promote glycan addition to asparagine residues and increase glycosylation site occupancy. Despite evidence that glycosylation regulates receptor maturation and function, the site-specific effects of N-linked glycosylation on LRP1-mediated tau uptake remain unclear. To address this, point mutation constructs were also designed to enable comparison of individual glycosylation sites and their contributions to tau internalization. This study investigated how mutations in N-linked glycosylation sites of mLRP4 influence tau uptake mechanisms. Mutant constructs were generated using point mutations and EAS motifs, with vectors synthesized commercially and assembled into an optimized mLRP4 plasmid using Gibson Assembly following restriction digestion with SmaI, BlpI, PshAI, and AfeI. Lentivirus was produced in HEK293T cells and used to transduce mammalian H4i cells, followed by secondary transduction with an LRP1i3 sgRNA construct. Preliminary results demonstrate successful lentiviral production, transduction into H4i cells, and validation of cloning workflows with high-yield plasmid preparations. This work lays the foundation for future tau-uptake quantification studies and provides insight into how glycosylation regulates LRP1 function. Ultimately, this research may help define molecular mechanisms underlying AD progression and identify glycosylation-dependent therapeutic targets.