|Application ||DB, E|
|Other Accession||P60881, P60879, P60878, Q17QQ3, Q6PC54, NP_003072.2|
|Predicted||Zebrafish, Bovine, Chicken, Mouse, Rat|
|Calculated MW||23315 Da|
|Other Names||Synaptosomal-associated protein 25, SNAP-25, Super protein, SUP, Synaptosomal-associated 25 kDa protein, SNAP25, SNAP|
|Target/Specificity||This SNAP25 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding T138 of human SNAP25.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-SNAP25(T138) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF.|
|Cellular Location||Cytoplasm, perinuclear region. Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region (By similarity).|
|Tissue Location||Neurons of the neocortex, hippocampus, piriform cortex, anterior thalamic nuclei, pontine nuclei, and granule cells of the cerebellum|
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Provided below are standard protocols that you may find useful for product applications.
t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF.
Mohrmann, R., et al. Science 330(6003):502-505(2010)
Tsai, Y.C., et al. Proc. Natl. Acad. Sci. U.S.A. 107(38):16554-16559(2010)
Condliffe, S.B., et al. J. Biol. Chem. 285(32):24968-24976(2010)
Weber, J.P., et al. EMBO J. 29(15):2477-2490(2010)
Walter, A.M., et al. J. Cell Biol. 188(3):401-413(2010)
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