Anti-STX5 / Syntaxin 5

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. STX5 antibody detects Syntaxin-5, a membrane-anchored SNARE protein essential for vesicle trafficking between the endoplasmic reticulum (ER) and Golgi apparatus. Syntaxin-5 mediates membrane fusion events within the early secretory pathway and ensures the proper transport of proteins and lipids through the Golgi complex. The STX5 antibody is widely used in studies of intracellular trafficking, Golgi organization, and protein secretion.Syntaxin-5 is encoded by the STX5 gene located on human chromosome 11q12.2. The protein exists as two isoforms generated by alternative translation initiation, a long (42 kilodalton) and short (35 kilodalton) form, both containing an N-terminal coiled-coil region and a C-terminal transmembrane domain. These isoforms localize to different Golgi subcompartments and coordinate SNARE complex formation with partners such as Bet1, Sec22b, and GosR2 to drive vesicle docking and fusion.The STX5 antibody detects a characteristic double band in western blot corresponding to both isoforms. Immunofluorescence typically shows strong perinuclear staining consistent with Golgi localization. Functionally, Syntaxin-5 plays a pivotal role in maintaining Golgi structure and retrograde transport from the Golgi to ER. Disruption of STX5 function leads to ER stress, defective glycosylation, and impaired secretion of transmembrane and secretory proteins.Syntaxin-5 also participates in autophagy and lipid metabolism by regulating membrane flow between organelles. Mutations in STX5 cause congenital disorders of glycosylation and multisystemic developmental delay. The protein further contributes to viral replication processes, as certain viruses exploit STX5-dependent pathways to reorganize host membranes. NSJ Bioreagents provides a validated STX5 antibody optimized for western blot, immunofluorescence, and immunohistochemistry, supporting research into vesicle trafficking, ER-Golgi transport, and cellular homeostasis.