Application Methods: Immunohistochemistry (Paraffin), Western Blotting
Background: Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion by pairing of vesicular SNAREs (v-SNAREs) with cognate target SNAREs (t-SNAREs) (reviewed in 1,2). Vesicle associated membrane protein 3 (VAMP3), also known as cellubrevin, has a broad tissue distribution and localizes to endosomal compartments (3). VAMP3 interacts with the t-SNAREs syntaxin1, syntaxin4, SNAP23, and SNAP25 (4,5). Research studies indicate that VAMP3 is involved in transferrin receptor recycling to the plasma membrane (6) and in T-cell receptor recycling to immunological synapses (7). Inhibition of VAMP3 with tetanus toxin impairs membrane trafficking during cell migration (8).
|Human, Mouse, Rat|
Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting
Background: Vesicle-associated membrane protein 2 (VAMP2, also called synaptobrevin) is part of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex (1). The SNARE complex is involved in vesicular transport and membrane fusion, a process regulated by calcium (2). In neurons, VAMP2 is predominantly inserted in presynaptic vesicle membranes. Assembly of VAMP2 with the plasma membrane SNAREs syntaxin 1 and SNAP25 is a key event necessary for membrane fusion and neurotransmitter release (2). In addition to this important function, VAMP2 is also involved in granule exocytosis in neutrophils (3) and release of bioactive peptides from cardiac myocytes (4) and juxtaglomerular cells (5).