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Synaptobrevin 2 antibody - 104 211C3

Synaptobrevin2 also known as Vamp2 is a major vesicle protein involved in fusion
Mouse monoclonal purified IgG
Cat. No.: 104 211C3
Amount: 50 µg
Price: $465.00
Cat. No. 104 211C3 50 µg purified IgG, lyophilized, fluorescence-labeled with Sulfo-Cyanine 3. Albumin was added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Either add 1:1 (v/v) glycerol, then aliquot and store at -20°C until use, or store aliquots at -80°C without additives.
Reconstitute immediately upon receipt! Avoid bright light when working with the antibody to minimize photo bleeching of the fluorescent dye.
Applications
 
WB: N/A
IP: N/A
ICC: 1 : 1000 gallery  
IHC: 1 : 200
IHC-P: not tested yet
Label Sulfo-Cyanine 3
Clone 69.1
Subtype IgG1 (κ light chain)
Immunogen Synthetic peptide corresponding to residues near the amino terminus of rat Synaptobrevin2 (UniProt Id: P63045)
Epitop Epitop: AA 2 to 17 from rat Synaptobrevin2 (UniProt Id: P63045)
Reactivity Reacts with: human (P63027), rat (P63045), mouse (P63044), hamster.
No signal: chicken, zebrafish.
Other species not tested yet.
Specificity Specific for VAMP 2. No cross-reactivity to VAMP 1 and VAMP 3. K.O.
Matching control protein/peptide 104-2P
Data sheet 104_211c3.pdf

References for Synaptobrevin 2 - 104 211C3

Nanoscale 3D EM reconstructions reveal intrinsic mechanisms of structural diversity of chemical synapses.
Zhu Y, Uytiepo M, Bushong E, Haberl M, Beutter E, Scheiwe F, Zhang W, Chang L, Luu D, Chui B, Ellisman M, et al.
Cell reports (2021) 351: 108953. 104 211C3 IHC; tested species: mouse
Assembly of Excitatory Synapses in the Absence of Glutamatergic Neurotransmission.
Sando R, Bushong E, Zhu Y, Huang M, Considine C, Phan S, Ju S, Uytiepo M, Ellisman M, Maximov A
Neuron (2017) 942: 312-321.e3. 104 211C3 IHC; tested species: mouse
Breakdown of axonal synaptic vesicle precursor transport by microglial nitric oxide.
Stagi M, Dittrich PS, Frank N, Iliev AI, Schwille P, Neumann H
The Journal of neuroscience : the official journal of the Society for Neuroscience (2005) 252: 352-62. 104 211C3 IHC
Cat. No.: 104 211C3
Amount: 50 µg
Price: $465.00
Nanoscale 3D EM reconstructions reveal intrinsic mechanisms of structural diversity of chemical synapses.
Zhu Y, Uytiepo M, Bushong E, Haberl M, Beutter E, Scheiwe F, Zhang W, Chang L, Luu D, Chui B, Ellisman M, et al.
Cell reports (2021) 351: 108953. 104 211C3 IHC; tested species: mouse
Assembly of Excitatory Synapses in the Absence of Glutamatergic Neurotransmission.
Sando R, Bushong E, Zhu Y, Huang M, Considine C, Phan S, Ju S, Uytiepo M, Ellisman M, Maximov A
Neuron (2017) 942: 312-321.e3. 104 211C3 IHC; tested species: mouse
Breakdown of axonal synaptic vesicle precursor transport by microglial nitric oxide.
Stagi M, Dittrich PS, Frank N, Iliev AI, Schwille P, Neumann H
The Journal of neuroscience : the official journal of the Society for Neuroscience (2005) 252: 352-62. 104 211C3 IHC
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.