Recombinant Human SNCaIP1 protein

SNCaIP1 (Alpha-synuclein-interacting protein 1), also known as Synphilin-1. is a cytoplasmic protein primarily recognized for its interaction with α-synuclein, a key player in Parkinson’s disease (PD) pathogenesis. Discovered in the late 1990s, SNCaIP1 forms cytoplasmic inclusions with α-synuclein, contributing to Lewy body formation—a hallmark of PD and related synucleinopathies. Structurally, it contains multiple domains, including an N-terminal region involved in protein-protein interactions and a C-terminal ubiquitin-like domain, suggesting roles in ubiquitination pathways and proteasomal degradation.

Recombinant SNCaIP1 protein is engineered to study its biological functions and molecular interactions in vitro or in cellular models. Researchers often express it in bacterial or mammalian systems with tags (e.g., His, GST) for purification and detection. Its recombinant form enables exploration of mechanisms underlying PD, particularly how α-synuclein aggregates disrupt cellular homeostasis. Studies show SNCaIP1 modulates α-synuclein toxicity, autophagy, and apoptosis, linking it to neurodegeneration. Additionally, it interacts with Parkin, an E3 ubiquitin ligase associated with autosomal recessive PD, implicating SNCaIP1 in ubiquitin-proteasome system regulation.

Beyond PD, SNCaIP1 is implicated in cancer and metabolic disorders, though its roles remain less defined. Recombinant protein tools facilitate high-throughput screening for therapeutic compounds targeting α-synuclein aggregation or protein degradation pathways. Challenges include understanding context-dependent post-translational modifications (e.g., phosphorylation) and isoform-specific functions. Overall, SNCaIP1 recombinant protein serves as a critical reagent for unraveling molecular pathways in neurodegenerative diseases and developing targeted therapies.