Recombinant Human SYT11 protein

SYT11 (synaptotagmin-11) is a member of the synaptotagmin family, a group of membrane-trafficking proteins characterized by calcium-binding C2 domains. Unlike many synaptotagmins involved in neurotransmitter release, SYT11 lacks canonical calcium-binding motifs, suggesting distinct functional roles. It is widely expressed in neuronal and non-neuronal tissues, with emerging links to neurodegenerative diseases, particularly Parkinson’s disease (PD). Genetic studies have identified SYT11 as a risk locus for PD, and its dysregulation is associated with α-synuclein aggregation, a hallmark of PD pathology. SYT11 is also implicated in regulating vesicular transport, lysosomal function, and autophagy—processes critical for maintaining cellular homeostasis.

Recombinant SYT11 protein is engineered for in vitro studies to dissect its molecular mechanisms. Typically produced in bacterial or mammalian expression systems, the protein is purified using affinity tags (e.g., His-tag) and validated via Western blot or mass spectrometry. Researchers utilize recombinant SYT11 to investigate its interactions with binding partners, such as SNARE proteins or lipid membranes, and to explore its role in membrane dynamics. Additionally, it serves as an antigen for antibody development in diagnostic research. Structural studies using recombinant SYT11 aim to resolve its domain architecture, particularly the atypical C2 domains, to understand how it modulates membrane fusion or cargo sorting without calcium signaling. Its involvement in disease pathways has spurred interest in targeting SYT11 for therapeutic exploration, including small-molecule screens or gene therapy approaches. Despite progress, many aspects of SYT11 biology, including its precise physiological functions and pathological contributions, remain under investigation, highlighting the importance of recombinant tools in advancing this field.