MGSSHHHHHH SSGLVPRGSH MDNSGKEAEA MALLAEAERK VKNSQSFFSG LFGGSSKIEE ACEIYARAAN MFKMAKNWSA AGNAFCQAAQ LHLQLQSKHD AATCFVDAGN AFKKADPQEA INCLMRAIEI YTDMGRFTIA AKHHISIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAG YAALLEQYQK AIDIYEQVGT NAMDSPLLKY SAKDYFFKAA LCHFCIDMLN AKLAVQKYEE LFPAFSDSRE CKLMKKLLEA
HEEQNVDSYT ESVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR.
N-Ethylmaleimide-Sensitive Factor Attachment Protein, Alpha (α-SNAP) is a crucial component of the cellular machinery involved in membrane fusion. This protein is encoded by the NAPA gene and is ubiquitously expressed in eukaryotic cells . The recombinant form of this protein is often used in research to study its function and interactions.
α-SNAP is a soluble protein that plays a pivotal role in the SNARE (Soluble NSF Attachment Protein Receptor) complex . The SNARE complex is essential for the fusion of vesicles with target membranes, a process critical for intracellular trafficking and neurotransmitter release . α-SNAP binds to the SNARE complex and recruits the N-ethylmaleimide-sensitive factor (NSF), an ATPase that disassembles the SNARE complex after membrane fusion .
The primary function of α-SNAP is to mediate the disassembly of the SNARE complex. This process is ATP-dependent and involves the hydrolysis of ATP by NSF . The binding of α-SNAP to the SNARE complex is a prerequisite for NSF attachment and subsequent ATP hydrolysis . This disassembly is crucial for the recycling of SNARE proteins and the maintenance of vesicular trafficking .
Recombinant α-SNAP is widely used in biochemical and structural studies to understand its role in membrane fusion and SNARE complex dynamics . It is also employed in the development of therapeutic strategies targeting SNARE-mediated processes in diseases such as epilepsy and neurodegenerative disorders .