Cat. No. 104 318 |
50 µg purified recombinant IgG, lyophilized. 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 to -80°C until use. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
Applications | |
Clone | Gp69.1 |
Subtype | IgG2 (κ light chain) |
Immunogen | Synthetic peptide corresponding to residues near the amino terminus of rat Synaptobrevin2 (UniProt Id: P63045) |
Reactivity |
Reacts with: mouse (P63044), rat (P63045), human (P63027), hamster. No signal: chicken, zebrafish. Other species not tested yet. |
Specificity | K.O. validated |
Matching control protein/peptide | 104-2P |
Remarks |
This antibody is a chimeric antibody based on the well known monoclonal mouse antibody 69.1. The constant regions of the heavy and light chains have been replaced with Guinea pig specific sequences. The antibody can therefore be used with standard anti-Guinea pig secondary reagents. |
Data sheet | 104_318.pdf |
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, synaptobrevin1 (VAMP1 or p18-1) and synaptobrevin2 (VAMP2 or p18-2) that differ in their distribution within different brain regions.
Synaptobrevin1 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 synaptobrevin2 are present in many other tissues where the protein resides on specialized microvesicles.
In non-neuronal cells the third isoform, cellubrevin (VAMP3), 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.