|Application ||WB, IF|
|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 human Synaptophysin was used as an immunogen.|
|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 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 is an integral membrane protein of small synaptic vesicles in brain and endocrine cells (1). Synaptophysin (syp I) is a synaptic vesicle membrane protein that constitutes approximately 7% of the total vesicle protein. Multiple lines of evidence implicate syp I in a number of nerve terminal functions (2). Synaptophysin is one of the most abundant membrane proteins of small synaptic vesicles. In mature nerve terminals it forms a complex with the vesicular membrane protein synaptobrevin, which appears to modulate synaptobrevin's interaction with the plasma membrane-associated proteins syntaxin and SNAP25 to form the SNARE complex as a prerequisite for membrane fusion. It has been shown that synaptobrevin is preferentially cleaved by tetanus toxin while bound to synaptophysin or when existing as a homodimer (3). data suggest that synaptophysin is released from the Golgi apparatus in a vesicular form, after glycosylation, and is then transported to nerve endings by a mechanism which requires integrity of microtubules (4).
1. Ozcelik T, et al. Am J Hum Genet 47(3):551-61, 1990.
2. McMahon HT, et al. Proc Natl Acad Sci 93(10):4760-4, 1996.
3. Reisinger C, et al. J. Neurochem 90(1):1-8, 2004.
4. Tixier-Vidal A, et al. Neuroscience 26(3):847-61, 1988.
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