SNAP-25 (187-203), a peptide corresponding to residues 187–203 of SNAP-25, is a substrate for botulinum neurotoxin (BoNT)/A and can be used as a substrate for quantifying the activity of BoNT/C1(1-430) .
CAT No: R1682
SNAP-25 187-203 is a synthetic peptide corresponding to amino acid residues 187 through 203 of the synaptosomal-associated protein 25 (SNAP-25), a crucial component of the SNARE complex involved in synaptic vesicle fusion and neurotransmitter release. As a C-terminal fragment of SNAP-25, this peptide serves as a valuable molecular tool for dissecting the protein-protein interactions and regulatory mechanisms that underlie synaptic transmission. Its defined sequence and structural features make it relevant for a wide range of neurobiological and biochemical investigations, particularly in studies focused on exocytosis, neuronal signaling, and the modulation of SNARE-mediated membrane fusion events.
Protein-protein interaction studies: The 187-203 region of SNAP-25 encompasses key residues involved in the assembly and stabilization of the SNARE complex. Researchers employ this peptide to probe the direct binding interfaces between SNAP-25 and its partners, such as syntaxin-1 and synaptobrevin/VAMP2. By acting as a competitive inhibitor or a structural mimic, the peptide enables detailed mapping of interaction domains, facilitating the elucidation of molecular determinants critical for vesicle docking and fusion. This approach is instrumental in advancing the understanding of synaptic machinery at a molecular level.
Mechanistic analysis of exocytosis: SNAP-25 187-203 is widely used in in vitro reconstitution assays and cell-free systems to investigate the mechanistic basis of regulated exocytosis. The peptide can modulate or disrupt SNARE complex formation, thereby allowing researchers to assess the functional consequences of C-terminal truncations or modifications on vesicle fusion efficiency. Such studies provide insight into the stepwise assembly of SNARE complexes and the specific contributions of SNAP-25 domains to membrane fusion events, offering a controlled platform for dissecting the temporal and spatial regulation of exocytosis.
Antibody validation and epitope mapping: The defined sequence of this peptide makes it an ideal standard for validating the specificity and affinity of antibodies raised against the C-terminal region of SNAP-25. By serving as an immunogen or as a competitive antigen in immunoassays, the peptide allows for precise epitope mapping and the assessment of antibody cross-reactivity. This application is essential for the development and characterization of high-quality research antibodies used in Western blotting, immunoprecipitation, and immunocytochemistry targeting SNAP-25.
Phosphorylation and post-translational modification research: The C-terminal domain of SNAP-25 contains residues that are subject to regulatory phosphorylation and other post-translational modifications, which can modulate synaptic plasticity and neurotransmitter release. The 187-203 peptide provides a defined substrate for in vitro kinase assays, mass spectrometry, and other analytical techniques aimed at characterizing modification patterns and their functional consequences. Utilizing this peptide enables researchers to systematically investigate the regulatory pathways influencing SNAP-25 activity and SNARE complex dynamics.
Neurotoxin substrate studies: The SNAP-25 C-terminus is a known target for several neurotoxins, including botulinum neurotoxins, which cleave specific peptide bonds and disrupt synaptic transmission. The 187-203 peptide serves as an accessible substrate for enzymatic assays designed to study neurotoxin specificity, cleavage kinetics, and inhibitor screening. By providing a minimal yet functionally relevant sequence, the peptide supports the development of robust in vitro assays for characterizing neurotoxin activity and for identifying novel modulators of SNARE complex integrity.
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