Syntaxin-4 (E6W7B) Rabbit mAb #67657

Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in intracellular vesicle trafficking and exocytosis, and are essential for processes that require rapid, targeted, and regulated membrane fusion such as cell growth, hormone secretion, and neurotransmission (reviewed in 1,2). Functioning as a target or t-SNARE protein, Syntaxin-4 is characterized by a long cytoplasmic N-terminal region encompassing two coiled-coil domains, a single transmembrane domain, and a very short extracellular C-terminus (3). Syntaxin-4 is known to regulate glucose uptake in skeletal muscle and adipose tissue by facilitating the translocation of the glucose transporter GLUT4 from an intracellular compartment to the plasma membrane (4,5). Moreover, human islet β-cells overexpressing Stx4 exhibited enhanced insulin secretory capability, resilience against proinflammatory cytokine-induced apoptosis, and reduced chemokine expression (6). Additionally, research studies have indicated that Syntaxin-4 plays a role in the exocytosis of AMPA receptors in hippocampal neurons (7), lytic granule exocytosis in cytotoxic T-lymphocytes (8), and hepatitis C viral particle release (9).