Anti-SNAP25 Antibody Picoband® Fluoro488 Conjugated

Synaptosome-associated protein of 25,000 daltons, also known as SNAP-25, is a protein which in humans encodes a 25-kD protein of 206 amino acids. It was first investigated as a neuron-specific gene preferentially expressed in mouse hippocampus. The tSNARE (the target-membrane soluble NSF-attachment protein receptor, where NSF is N-ethylmaleimide-sensitive fusion protein) synaptosomal-associated protein of 25 kDa (SNAP-25) is expressed in pancreatic B-cells and its cleavage by botulinum neurotoxin E (BoNT/E) abolishes stimulated secretion of insulin. In the nervous system, two SNAP-25 isoforms (a and b) have been described, which are produced by alternative splicing. It is identified mammalian Snap25a and Snap25b as targets of protein kinase A, a key regulator of neurosecretion that primes slowly releasable pools and readily releasable pools of secretory vesicles. SNAP-25 inhibits P/Q- and L-type voltage-gated calcium channels located presynaptically and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion. In glutamatergic synapses SNAP-25 decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses.

Cancer, Cancer Metabolism, Cell Type Marker, Energy Transfer Pathways, Integration Of Energy, Integration Of Energy Metabolism, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Neuron Marker, Neuroscience, Neurotransmission, Pathways and Processes, Protein Trafficking, Secretory Vesicles, Signal Transduction, Synapse Marker, Vesicle Transport

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. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells.

1. Gonelle-Gispert, C.; Halban, P. A.; Niemann, H.; Palmer, M.; Catsicas, S.; Sadoul, K. : SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion. Biochem. J. 339: 159-165, 1999. 2. Nagy, G.; Reim, K.; Matti, U.; Brose, N.; Binz, T.; Rettig, J.; Neher, E.; Sorensen, J. B. : Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25. Neuron 41: 417-429, 2004. 3. Hodel A (1998) . SNAP-25. The International Journal of Biochemistry & Cell Biology 30 (10) : 1069–1073. 4. Chapman ER (2002) . Synaptotagmin: A Ca2+ sensor that triggers exocytosis?. Nature Reviews Molecular Cell Biology 3: 498–508. 5. Pozzi D, Verderio C, Patti L, Grumelli C, Inverardi F, Frassoni C, Bonanno G, Matteoli M (2004) . SNAP-25 modulation of calcium dynamics underlies differences in GABAergic and glutamatergic responsiveness to depolarization. Neuron 41 (4) : 599–610.