SNAP-25 (Phospho-Ser¹⁸⁷) Polyclonal Antibody

Synaptosomal-associated protein 25 (SNAP-25) is a member of the SNARE complex, which also includes syntaxin and VAMP, that is responsible for fusing synaptic vesicles with the presynaptic plasma membrane to facilitate neurotransmitter release.¹ Two SNAP-25 isoforms, SNAP-25a and SNAP-25b, are generated through alternative splicing, with SNAP-25b expressed only during the postnatal period and as the predominant isoform in the brain.² SNAP-25 contains two α helices, as well as one large and several smaller intrinsically disordered domains.¹ SNAP-25 is located primarily on the intracellular side of the presynaptic plasma membrane in neurons and interacts with a variety of proteins to orchestrate vesicle fusion in a calcium-triggered manner and to mediate spine development.¹ It is also found in the pancreas, enteroendocrine cells, and the chromaffin cells of the adrenal medulla where it is involved in hormone secretion.² SNAP-25 can be phosphorylated at serine 187 (Ser¹⁸⁷) in a neuronal activity-dependent manner by PKC, a modification that increases the rate of synaptic vesicle recruitment and is essential for SNAP-25b inhibition of voltage-gated calcium channels (VGCCs) and incorporation of NMDA receptors into the postsynaptic membrane.^3,4,5 Phosphorylation at Ser¹⁸⁷ also facilitates neurotransmitter release and inhibits presynaptic short-term plasticity via regulation of synaptic vesicle dynamics.⁶ A point mutation at Ser¹⁸⁷ (S187A) induces anxiety-like behavior in mice homozygous for the mutation and induces working memory deficits and an immature phenotype in hippocampal dental granule cells of adult mice heterozygous for the mutation.^7,8 Cayman’s SNAP-25 (Phospho-Ser¹⁸⁷) Polyclonal Antibody can be used for Western blot (WB) applications. The antibody recognizes SNAP-25 (phospho-Ser¹⁸⁷) at approximately 25 kDa from mouse and rat samples.

WARNING This product is not for human or veterinary use.

1. Karmakar, S., Sharma, L.G., Roy, A., et al. Neuronal SNARE complex: A protein folding system with intricate protein-protein interactions, and its common neuropathological hallmark, SNAP25. Neurochem. Int. 122, 196-207 (2019).

2. Kádková, A., Radecke, J., and Sørensen, J.B. The SNAP-25 protein family. Neuroscience 420, 50-71 (2019).

3. Nagy, G., Matti, U., Nehring, R.B., et al. Protein kinase C-dependent phosphorylation of synaprosome-associated protein of 25 kDa at Ser¹⁸⁷ potentiates vesicle recruitment. J. Neurosci. 22(21), 9278-9286 (2002).

4. Pozzi, D., Condliffe, S., Bozzi, Y., et al. Activity-dependent phosphorylation of Ser¹⁸⁷ is required for SNAP-25-negative modulation of neuronal voltage-gated calcium channels. PNAS 105(1), 323-328 (2008).

5. Lau, C.G., Takayasu, Y., Rodenas-Ruano, A., et al. SNAP-25 is a target of protein kinase C phosphorylation critical to NMDA receptor trafficking. J. Neurosci. 30(1), 242-254 (2010).

6. Katayama, N., Yamamori, S., Fukaya, M., et al. SNAP-25 phosphorylation at Ser¹⁸⁷ regulates synaptic facilitation and short-term plasticity in an age-dependent manner. Sci. Rep. 7, 7996 (2017).

7. Kataoka, M., Yamamori, S., Suzuki, E., et al. A single amino acid mutation in SNAP-25 induces anxiety-related behavior in mouse. PLoS One 6(9), e25158 (2011).

8. Ohira, K., Kobayashi, K., Toyama, K., et al. Synaptosomal-associated protein 25 mutation induces immaturity of the dentate granule cells of adult mice. Mol. Brain 6, 12 (2013).