|Cat. No. 104 211BT||50 µg purified IgG, lyophilized, biotin-labeled. 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.|
Immunoprecipitation (IP); Immunoisolation or pulldown of a target molecule using an antibody. For details and product specific hints, please refer to the ”Remarks” section.', $event)" style="cursor: help;">IP: yes (see remarks)
Immunocytochemistry (ICC) on 4% PFA fixed cells. Immunoreactivity is usually revealed by fluorescence. Some antibodies require special fixation methods. For details, please refer to the “Remarks” section.', $event)" style="cursor: help;">ICC: 1 : 500 up to 1 : 1000 gallery
Immunohistochemistry (IHC) on 4% PFA perfusion fixed tissue with 24h PFA post fixation. Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate. Some antibodies require special fixation methods or antigen retrieval steps. For details, please refer to the ”Remarks” section.', $event)" style="cursor: help;">IHC: 1 : 200 gallery
Immunohistochemistry (IHC-P) of formalin fixed, paraffin embedded (FFPE) tissue (some antibodies require special antigen retrieval steps, please refer to the ”Remarks” section). Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate.', $event)" style="cursor: help;">IHC-P: 1 : 500 gallery
|Subtype||IgG1 (κ light chain)|
|Immunogen||Synthetic peptide corresponding to residues near the amino terminus of rat Synaptobrevin2 (UniProt Id: P63045)|
Epitop: AA 2 to 17 from rat Synaptobrevin2 (UniProt Id: P63045)
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|
Although the epitope for this antibody is still present in the Botulinumtoxin B cleavage product (aa 1 - 76), it is not recognized for unknown reasons.
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.