Description_x000D_ General description_x000D_ Vesicle-associated membrane protein 8 (VAMP-8/endobrevin) is located at 2p11.2 on the human chromosome._x000D_ Immunogen_x000D_ Synthetic peptide corresponding to amino acids 1-16 located at the N-terminal of human VAMP8, conjugated to KLH. This sequence is highly conserved (~75%) in mouse and rat VAMP8._x000D_ Application_x000D_ Anti-VAMP-8 (N-terminal) antibody has been used in immunoblotting, western blotting._x000D_ Physical form_x000D_ Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ Vesicle-associated membrane protein 8 (VAMP-8/endobrevin) is as an endosomal v-SNARE (vesicles or granules-soluble NSF attachment protein receptors) involved in fusion between early and late endosomes. It can interact with syntaxin-7, syntaxin-8, and Vti1b (Vesicle transport through interaction with t-SNAREs homolog 1B) to form an endosomal fusion complex. VAMP8 interacts with syntaxin-2 and is involved in the terminal step of cytokinesis in mammalian cells. VAMP8 is the major vesicular v-SNARE of zymogen granules from pancreatic acinar cells and has been shown to be a general vesicular SNARE for regulated exocytosis of the exocrine system. For platelet release reaction VAMP8 is the primary v-SNARE.