STXBP6 Human

STXBP6 is a single-pass type IV membrane protein that belongs to the syntaxin family . It is primarily localized in the plasma membrane and contains a t-SNARE coiled-coil homology domain . This domain is essential for its role in intracellular vesicle trafficking, particularly in the docking and fusion of synaptic vesicles .

STXBP6 interacts with various syntaxins, including syntaxins 1, 2, and 3, but not syntaxin 4 . It is involved in the regulation of synaptic vesicle docking and fusion through its interaction with GTP-binding proteins . This interaction is crucial for neurotransmission, as it ensures the proper release of neurotransmitters at synaptic junctions .

Recent studies have highlighted the role of STXBP6 in prion diseases. For instance, it has been shown to delay prion protein fibril formation and prolong the presence of toxic aggregation intermediates . This finding suggests that STXBP6 could be a potential therapeutic target for prion diseases, as it can alter the initial phase of prion protein self-assembly and act as an "anti-chaperone" .

Additionally, genetic variants that increase the expression of STXBP6 in the brain have been identified as risk factors for sporadic Creutzfeldt–Jakob disease . This discovery underscores the importance of STXBP6 in neurodegenerative diseases and opens new avenues for research into its potential therapeutic applications.

The recombinant form of human Syntaxin Binding Protein 6 is typically produced in E. coli expression systems . The protein is purified to a high degree, with a purity of 95% as determined by reducing SDS-PAGE . It is usually provided as a lyophilized powder, which can be reconstituted for use in various research applications .

Lyophilized STXBP6 is stable for up to 12 months when stored at -20°C to -80°C . Once reconstituted, the protein solution can be stored at 4-8°C for 2-7 days or at -20°C for up to 3 months . Proper storage and handling are essential to maintain the protein’s stability and functionality.