Technical Data
Synaptophysin is an ~38kD integral membrane protein involved in neurotransmitter exocytosis present on synaptic vesicles. This protein consists of four transmembrane domains, with its amino- and carboxyl-terminus facing the cytoplasm. Due to its transmembrane domain structure, synaptophysin has been postulated to be a gap junction-like protein because voltage-dependent channel activity is seen when synaptophysin hexamers are reconstituted into lipid membranes. Recent studies have shown synaptophysin to be a major cholesterol-binding protein in brain synaptic vesicles and it has been proposed that this cholesterol-binding ability may be of key importance in the generation of synaptic vesicles at plasma membranes. A regional reduction of synaptophysin was found in patients with Alzheimers disease and schizophrenia.

Suitable for use in Western Blot and Immunohistochemistry. Other applications have not been tested.

Recommended Dilutions:
Western Blot (Colorimetric): 1:2000
Immunohistochemistry: 1:50 using human neuroblastoma tissue
Optimal dilutions to be determined by researcher.

Positive Controls:
Mouse and rat brain tissue extract

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20CBlue IceHumanMouse
Synaptic vesicle-containing fractions immunoprecipitated from human brain homogenates.
Purified by ammonium sulfate precipitation
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide, 50% glycerol.
Recognizes human synaptophysin at ~38kD. Species Crossreactivity: mouse, rat and bovine. No reactivity was detected in mouse liver extracts.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Honer, W.G., Hu, L. and Davies, P., Brain Research 609: 9-20 (1993). 2. Rehm, H., Wiedenmann, B. and Betz, H., EMBO J. 5: 535-541 (1986). 3. Thomas, L., et al., Science 242: 1050-1053 (1988). 4. Thiele, C., et al., Nat. Cell Biol. 2: 42-49 (2000). 5. Martin, T.F., Nat. Cell Biol. 2: E9-E11 (2000). 6. Landen, M., et al., Biol. Psychiatry 46: 1698-1702 (1999). 7. Honer, W., et al., Neurobiol. Aging 13: 373-382 (1992).