SNAP-8

Scientific identity: Snap-8 is an N-terminally acetylated octapeptide with the sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂, corresponding to residues 12–19 of the SNAP-25 protein N-terminal domain. SNAP-25 (synaptosomal-associated protein of 25 kDa) is one of three core SNARE proteins — alongside syntaxin-1 and VAMP/synaptobrevin — that form the ternary SNARE complex driving synaptic vesicle fusion and neurotransmitter exocytosis at the presynaptic membrane. Research has proposed that Snap-8 competes with native SNAP-25 for incorporation into the SNARE complex in experimental systems, potentially modulating SNARE-mediated vesicle fusion as a research mechanism.

Primary research target: SNARE complex assembly — specifically the N-terminal domain of SNAP-25, one of three core SNARE proteins mediating synaptic vesicle fusion at the presynaptic membrane of the neuromuscular junction and central synapses.

Research areas: SNARE complex biology, synaptic vesicle fusion research, neuromuscular junction signaling, SNAP-25 protein interaction research, neurotransmitter exocytosis models, comparative SNARE peptide research.

Available quantities: 10mg and 20mg per vial.

Purity: Greater than 99%, confirmed by HPLC and LC-MS analysis at the batch level.

Analytical documentation: A batch-specific Certificate of Analysis is available on the Longevia Research website, covering compound identity, purity, and lot traceability.

Research-use classification: For laboratory research use only. Not for human or veterinary use, clinical diagnostics, or any in-vivo application in humans.

SNARE Complex Biology

The SNARE complex is the core molecular machinery driving synaptic vesicle fusion and neurotransmitter exocytosis at chemical synapses and the neuromuscular junction. The ternary SNARE complex is formed by the coiled-coil assembly of three proteins: syntaxin-1 (target membrane), VAMP/synaptobrevin (vesicle membrane), and SNAP-25 (target membrane, contributing two helical domains). SNAP-25 contributes both its N-terminal and C-terminal SNARE domains to the four-helix bundle that drives membrane fusion. The N-terminal SNARE domain of SNAP-25 — the region from which Snap-8 is derived — is a key structural element of this assembly.

Proposed Research Mechanism

Research has investigated Snap-8 as a competitive peptide analogue of the SNAP-25 N-terminal SNARE domain. The proposed mechanism under study is that Snap-8, by mimicking this domain, may compete with native SNAP-25 for incorporation into the assembling SNARE complex in experimental systems, potentially attenuating SNARE complex formation and downstream vesicle fusion events. These are experimental mechanistic proposals characterised in defined cell-based and biochemical systems. They represent research hypotheses about SNARE complex competitive inhibition rather than established physiological mechanisms confirmed across all biological contexts.

Relationship to Argireline

Argireline (Acetyl Hexapeptide-3, Ac-Glu-Glu-Met-Gln-Arg-Arg-NH₂) covers the first six residues of the same SNAP-25 N-terminal sequence that Snap-8 extends to eight residues (Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂). Both peptides have been investigated in SNARE complex research contexts. Snap-8 has been proposed to offer improved SNARE domain coverage relative to Argireline by extending the sequence into the Ala-Asp region, though direct comparative findings in the primary literature are limited. The two are structurally related but distinct compounds with different molecular identifiers and should not be treated as equivalent in research documentation.

Research Status

Snap-8 has a more limited primary research literature than longer-established SNARE research tools. Published findings are primarily from biochemical binding studies and cell-based systems examining SNARE complex assembly. No human clinical trial data is available for Snap-8 as a standalone research compound, and it holds no regulatory approval for any therapeutic indication. It is supplied for Research Use Only.

Reliable research begins with accurately characterised material. For an acetylated octapeptide such as Snap-8, that means confirming sequence integrity, N-terminal acetylation, and purity at the batch level — because sequence errors, missing acetylation, or truncated forms produce structurally distinct peptides with different SNARE domain binding profiles that can confound complex assembly assays and cell-based signaling experiments.

Purity assessment. Each production lot is characterised to greater than 99% purity by high-performance liquid chromatography (HPLC). Chromatographic purity data is reported on the batch Certificate of Analysis.

Identity confirmation. Peptide identity and N-terminal acetylation are confirmed by mass spectrometry (LC-MS), providing molecular-weight verification consistent with the acetylated octapeptide form. HPLC and LC-MS data together confirm that the material supplied corresponds to the labelled compound at the labelled purity.

Batch traceability and Certificate of Analysis. Every vial of Snap-8 10mg and 20mg is traceable to a specific production lot. A batch-specific Certificate of Analysis is accessible directly on the Longevia Research website, covering purity, identity, and lot information. Researchers evaluating this material for assay work are encouraged to review the current batch documentation before use, since analytical specifications are applied at the lot level.

Handling. This material should be handled by qualified personnel using appropriate laboratory technique and personal protective equipment, consistent with institutional protocols for research-grade synthetic peptides.

Longevia Research supplies Snap-8 10mg and 20mg for laboratory and in-vitro research use only. The product is intended for use by qualified researchers and trained laboratory personnel in appropriate controlled research environments.

Snap-8 is a synthetic research peptide supplied strictly as a research tool. It is not a drug, not a dietary supplement, not a food or food ingredient, and not a cosmetic. No regulatory authority has approved Snap-8 for any human or veterinary therapeutic use, and Longevia does not supply it for administration to humans or animals, for clinical diagnostics, or for any therapeutic purpose.

Longevia provides no dosing instructions, administration guidance, treatment protocols, or reconstitution recommendations for this compound. The scientific literature summarised on this product page describes experimental observations in defined biochemical and cell-based systems. Those findings are not medical claims and should not be interpreted as evidence of human efficacy, human safety, or fitness for any clinical application.

The purchaser assumes full responsibility for lawful acquisition, handling, storage, use, and disposal of this material, and for compliance with all applicable local, state, federal, and institutional regulations. By purchasing this product, the buyer confirms that it will be used solely for legitimate laboratory research purposes by qualified personnel, and that its acquisition and intended use comply with applicable laws in the buyer's jurisdiction.