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Synaptobrevin 2 - 104 403

Major vesicle protein involved in fusion
Polyclonal rabbit purified antibody
Cat. No.: 104 403
Amount: 50 µg
Price: 450.00 €
Cat. No. 104 403 50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin and azide were added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C until use.
Applications WB: 1 : 1000 up to 1 : 10000 gallery  
IP: not tested yet
ICC: 1 : 1000 up to 1 : 2000 gallery  
IHC: 1 : 1000 gallery  
IHC-P/FFPE: 1 : 2000 up to 1 : 5000 gallery  
Immunogen Synthetic peptide corresponding to AA 2 to 17 from rat Synaptobrevin2 (UniProt Id: P63045)
Reactivity Reacts with: mouse (P63044), rat (P63045).
Other species not tested yet.
Specificity Specific for VAMP 2. No cross-reactivity to VAMP 1 and VAMP 3.
Data sheet 104_403.pdf
Cat. No.: 104 403
Quantity: 50 µg
Price: 450.00 €
Background

Synaptobrevins/VAMPs represents a family of integral membrane proteins of 11-13 kDa with the N-terminal region exposed to the cytoplasm and a C-terminal transmembrane domain. Two isoforms were identified in the mammalian CNS, synaptobrevin 1 (VAMP 1 or p18-1) and synaptobrevin 2 (VAMP 2 or p18-2) that differ in their distribution within different brain regions.
Synaptobrevin 1 is highly conserved between vertebrates and invertebrates. It is a major constituent of synaptic vesicles and peptidergic secretory granules in all neurons examined so far. In addition, it is present on secretory granules of neuroendocrine cells. Low levels of synaptobrevin 2 are present in many other tissues where the protein resides on specialized microvesicles.
In non-neuronal cells the third isoform, cellubrevin (VAMP 3), is present where it is localized to an endosomal membrane pool.
Synaptobrevin/VAMP is an essential component of the exocytotic fusion machine, related to a larger protein family referred to as v-SNAREs. It is the sole target for tetanus and several of the botulinal neurotoxins which cleave the protein at single sites in the C-terminal portion of the molecule.