|Application ||IHC, WB|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||33845 Da|
|Other Names||Synaptophysin, Major synaptic vesicle protein p38, SYP|
|Target/Specificity||A synthetic peptide corresponding to residues in C-terminus (cytoplasmic domain) of human Synaptophysin was used as immunogen. Predicted to cross-react with bovine, based on sequence homology.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Synaptophysin Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane. Involved in the regulation of short-term and long-term synaptic plasticity (By similarity).|
|Cellular Location||Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. Cell junction, synapse, synaptosome|
|Tissue Location||Characteristic of a type of small (30-80 nm) neurosecretory vesicles, including presynaptic vesicles, but also vesicles of various neuroendocrine cells of both neuronal and epithelial phenotype|
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Provided below are standard protocols that you may find useful for product applications.
Synaptophysin (SypI), also referred as p38 (1), constitutes approximately 7% of the total vesicle protein and is selectively associated with small synaptic vesicles (SSVs). Syp I contains four transmembrane regions and can be phosphorylated on its cytoplasmic C-terminus by both serine/threonine and tyrosine kinases (2). In addition to syp I, synaptic vesicles contain a highly homologous membrane protein named synaptoporin or synaptophysin II (Syp II) (3). While Syp I is ubiquitously expressed and present in virtually all synapses whereas Syp II is expressed at high levels only in selected neurons (4).
1. Navone F, Jahn R, Di Gioia G, Stukenbrok H, Greengard P, De Camilli P. J Cell Biol. 1986 Dec;103(6 Pt 1):2511-27
2. Linstedt, A. D., Vetter, M. L., Bishop, J. M. & Kelly, R. B. (1992) J. Cell Biol. 117, 1077-1084.
3. Knaus, P., Marqueze-Pouey, B., Scherer, H. & Betz, H. (1990) Neuron 5, 453-462.
4. Marqueze-Pouey, B., Wisden, W., Malosio, M. L. & Betz, H.(1991) J. Neurosci. 11, 3388-3397.
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