SNAP-8 1g Raw Powder

SNAP‑8 (acetyl octapeptide‑3; Ac‑Glu‑Glu‑Met‑Gln‑Arg‑Arg‑Ala‑Asp‑NH₂) is a research-grade synthetic octapeptide that functions as a competitive inhibitor of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex formation at the neuromuscular junction. By mimicking the N-terminal region of SNAP‑25 — a core component of the SNAP‑23/SNAP‑25 SNARE complex responsible for docking and fusing synaptic vesicles with the presynaptic membrane — SNAP‑8 interferes with acetylcholine vesicle release, providing a non-paralytic, reversible model for studying neurotransmitter exocytosis inhibition. Available in 1g raw powder format for research applications requiring larger quantities or custom formulation.

SNARE Complex Inhibition and Neurotransmitter Exocytosis Research

• Competes with endogenous SNAP‑25 for incorporation into the ternary SNARE complex (syntaxin-1/SNAP‑25/synaptobrevin), reducing the efficiency of calcium-triggered synaptic vesicle fusion and acetylcholine release in neuromuscular junction models — enabling controlled, graded inhibition studies without the irreversible mechanism of botulinum neurotoxin.
• Used in in vitro neuromuscular junction assays to characterize the contribution of SNAP‑25 N-terminal domain integrity to SNARE assembly kinetics and exocytosis efficiency, supporting structure-function studies of the SNARE machinery.
• Provides a useful pharmacological tool for dissecting the relative contributions of SNAP‑23 versus SNAP‑25 isoforms in non-neuronal secretory pathways, where SNAP‑23 is the predominant isoform.

Facial Muscle Contraction and Mechanobiology Models

• Applied in ex vivo and cell-based models to investigate muscle contraction signaling under repetitive mechanical stress; its mechanism of reducing acetylcholine-mediated neuromuscular signaling makes it useful for studying cytoskeletal adaptation, collagen fiber remodeling, and mechanotransduction responses in myofibroblast and facial muscle research.
• Comparative studies alongside botulinum toxin fragments in organotypic skin and muscle models assess reversibility, depth of neuromuscular inhibition, and downstream effects on fibroblast extracellular matrix production under reduced mechanical loading.

Cosmetic Dermatology Research Applications

• Investigated as a topical research tool in ex vivo skin models for evaluating the relationship between neuromuscular activity reduction and dermal collagen architecture, providing mechanistic data relevant to expression line formation research and the role of chronic muscle contraction in dermal matrix degradation.
• Formulation studies in peptide delivery research use SNAP‑8 as a model compound for assessing transdermal peptide penetration enhancement strategies, given its defined sequence, moderate molecular weight (~1.075 kDa), and well-characterized bioactivity endpoint.

Purity and Presentation

• Supplied as a 1g raw lyophilized powder for bulk research formulation. Verified ≥99% purity by HPLC. Third-party tested for identity and sterility.

For research purposes only. Not intended for human consumption, disease prevention, diagnosis, or any therapeutic use. This product is intended solely for in vitro and laboratory research.

Research Guide

For a detailed scientific overview of this compound, read our research guide.