Cat. No.: 104 211C5
Amount: 50 µg
Price:
$470.00
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| Cat. No. 104 211C5 |
50 µg purified IgG, lyophilized, fluorescence-labeled with Cyanine 5.
Fluorescence labeled antibodies conjugated to Cyanine dyes are well suited for standard epi-fluorescence setups and confocal microscopy.
Cyanine 5 dyes are well suited for STORM high resolution microscopy. Reconstitute immediately upon receipt! Avoid bright light when working with the antibody to minimize photo bleeching of the fluorescent dye. |
| Applications | |
| Label | Sulfo-Cyanine 5 |
| Clone | 69.1 |
| Subtype | IgG1 (κ light chain) |
| Immunogen | Synthetic peptide corresponding to residues near the amino terminus of 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 | K.O. validated |
| Matching control protein/peptide | 104-2P |
| Data sheet | 104_211c5.pdf |
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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.