Parkinson's disease is a progressive movement disorder caused by the degeneration of dopaminergic neurons in the substantia nigra pars compacta and the accumulation of intracellular inclusions known as Lewy bodies. The principal structural component of these inclusions is alpha-Synuclein, a small presynaptic protein that regulates vesicle trafficking and neurotransmitter release. Under pathological conditions alpha-Synuclein misfolds and aggregates into oligomers and fibrils, and its deposition is closely associated with Phospho-alpha-Synuclein at serine 129, a modification that marks the bulk of aggregated protein and serves as a hallmark of disease. Several genes that cause familial Parkinsonism converge on shared pathways of protein quality control and mitochondrial maintenance. LRRK2, a large kinase whose activating mutations are the most common genetic cause of late-onset disease, influences vesicle trafficking, autophagy, and synaptic signaling. Parkin, an E3 ubiquitin ligase, cooperates with the mitochondrial stress response to tag damaged mitochondria for clearance through mitophagy, and its loss produces early-onset disease. VPS35, a core component of the retromer complex, governs endosomal sorting and receptor recycling, linking membrane trafficking defects to neurodegeneration. DJ-1/PARK7 acts as a redox-sensitive protein protecting neurons against oxidative stress, while UCH-L1 is an abundant neuronal deubiquitinating enzyme that regulates ubiquitin homeostasis and protein turnover. The vulnerability of the affected circuit is reflected in Tyrosine Hydroxylase, the rate-limiting enzyme of dopamine synthesis and the definitive marker of the dopaminergic neurons that are selectively lost. Together these targets capture the intertwined themes of aberrant protein aggregation, impaired degradation, mitochondrial dysfunction, and oxidative injury that define the disease. This pack brings together validated antibodies against alpha-Synuclein, Phospho-alpha-Synuclein, LRRK2, Parkin, VPS35, DJ-1/PARK7, UCH-L1, and Tyrosine Hydroxylase to support mechanistic study of Parkinson's disease.