Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- For fluorochrome spectra and suitable instrument settings, please refer to our Multicolor Flow Cytometry web page at www.bdbiosciences.com/colors.
Signal transmission between neurons is regulated by the release of neurotransmitters at the synapse. This process is controlled by a complex pathway of membrane trafficking in the presynaptic nerve terminal, which leads to membrane fusion and subsequent neurotransmitter secretion. Syntaxin is involved in three important protein complexes that modulate this process: syntaxin and n-sec1, syntaxin, VAMP and SNAP-25, and syntaxin, VAMP, SNAP-25, αSNAP, and NSF (20S complex). A model has been proposed to explain docking, activation, and fusion of synaptic vesicles with donor membranes. This model suggests that VAMP/synaptobrevin and synaptotagmin (vSNARE) on the synaptic vesicle, and SNAP-25 and syntaxin (tSNAREs) on the plasma membrane, interact to form a 7S complex. It appears that syntaxin associates with -sec1 prior to and/or during the formation of the 7S complex. Two additional soluble proteins, αSNAP and NSF, associate with this complex as synaptotagmin releases from the complex. The resulting 20S complex contains syntaxin, SNAP-25, VAMP, αSNAP, and NSF. A large region including the N-terminus is involved in binding n-sec1 while both VAMP and SNAP-25 bind within residues 199-288 of syntaxin.
Development References (5)
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Bennett MK, Calakos N, Scheller RH. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science. 1992; 257(5067):255-259. (Biology). View Reference
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Faigle W, Colucci-Guyon E, Louvard D, Amigorena S, Galli T. Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery. Mol Biol Cell. 2000; 11(10):3485-3494. (Clone-specific: Immunofluorescence). View Reference
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Kee Y, Lin RC, Hsu SC, Scheller RH. Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation. Neuron. 1995; 14(5):991-998. (Biology). View Reference
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Polgár J, Chung SH, Reed GL. Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion. Dev Biol. 2002; 100(3):1081-1083. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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Ramalho-Santos J, Moreno RD. SNAREs in mammalian sperm: possible implications for fertilization. Dev Biol. 2000; 223(1):54-69. (Clone-specific: Electron microscopy, Immunofluorescence, Western blot). View Reference
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