| Pack Size | Single Vial, 10-Pack |
|---|
SNAP-8 (Acetyl Octapeptide-3) is a synthetic eight-residue peptide designed to mimic the N-terminal segment of SNAP-25, a component of the SNARE complex that mediates neurotransmitter release. It is an elongated analogue of the hexapeptide Argireline and is studied primarily in topical cosmetic-science research on expression lines. Every batch is independently third-party tested by HPLC for purity and mass spectrometry for identity, to a minimum of 99 percent purity. Supplied as a lyophilized powder for laboratory research use only.
Description
SNAP-8, known by the INCI name Acetyl Octapeptide-3, is a synthetic octapeptide developed as an extension of Acetyl Hexapeptide-8 (Argireline). Where Argireline reproduces six residues of the SNAP-25 N-terminus, SNAP-8 extends the mimetic sequence to eight residues, a modification intended to strengthen its interaction with the SNARE assembly. It is N-terminally acetylated and C-terminally amidated.
In the research-supply context, SNAP-8 is a standard tool in topical cosmetic-peptide research, where it is studied for its proposed competitive effect on SNARE-complex formation. It is provided strictly as a research-grade reagent for laboratory benchwork and is not a cosmetic or therapeutic product.
Mechanism in research literature
The SNARE complex — assembled from SNAP-25, syntaxin, and VAMP/synaptobrevin — drives the fusion of neurotransmitter vesicles with the presynaptic membrane, releasing acetylcholine at the neuromuscular junction. SNAP-8 is based on a fragment of SNAP-25 and is studied for its ability to compete with the native protein for incorporation into the complex. By occupying that position, the peptide is proposed to reduce the efficiency of vesicle fusion and, in turn, acetylcholine-driven muscle contraction.
In cosmetic-science research this competitive-inhibition mechanism is the basis for studying SNAP-8 on contraction-driven expression lines. It is a topical research model; the mechanism is the object of study rather than an established outcome.
Studied properties
Documented areas of SNAP-8 research include: SNARE-complex modulation; competitive inhibition of SNAP-25 incorporation; reduction of neurotransmitter (acetylcholine) exocytosis in model systems; and topical cosmetic-science investigation of contraction-driven expression lines as an elongated analogue of Argireline. These describe the published research landscape and are provided for scientific context only. They are not claims of efficacy. Ronin Peptides supplies SNAP-8 exclusively as a research-grade reagent and provides no dosing protocols or therapeutic recommendations.
Compound specifications
| Compound | SNAP-8 (Acetyl Octapeptide-3) |
|---|---|
| CAS number | 868844-74-0 |
| Molecular weight | approximately 951.1 g/mol |
| Sequence | Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2 |
| Length | 8 amino acids (N-acetylated, C-terminal amide) |
| Class | SNARE-mimetic cosmetic research peptide |
| Parent analogue | Acetyl Hexapeptide-8 (Argireline) |
| Form | Lyophilized white-to-off-white powder |
| Solubility | Bacteriostatic water; sterile water for injection |
| Vial contents | 10 mg peptide, sealed amber-glass vial under inert gas |
| Purity | ≥99% by HPLC (verified per batch by a third-party analytical lab) |
Storage and handling
Store unopened lyophilized vials dry and cold; long-term storage should be at or below −20 °C, protected from light and moisture. Once reconstituted, keep refrigerated at 2–8 °C and use within a few weeks; avoid repeated freeze–thaw cycles. Note that the methionine residue is sensitive to oxidation. Bring vials to room temperature before opening.
Compare with similar compounds
SNAP-8 is most directly compared with Argireline (Acetyl Hexapeptide-8), from which it is elongated by two residues; the extension is intended to improve SNARE-complex interaction. Both are SNAP-25-mimetic cosmetic-research peptides that act through competitive inhibition of the SNARE assembly, distinguishing them mechanistically from signal-peptide or growth-factor cosmetic compounds such as GHK-Cu, which acts through copper-peptide signalling rather than neurotransmitter modulation.
Reconstitution and laboratory handling
A 10 mg vial of SNAP-8 reconstituted with 2 mL of bacteriostatic water yields a final concentration of 5 mg/mL, or 5,000 mcg/mL. Other diluent volumes scale linearly: 1 mL gives 10 mg/mL, 5 mL gives 2 mg/mL.
- Bring both vials to room temperature before opening.
- Sanitise both rubber stoppers with an alcohol swab.
- Pull the chosen diluent volume into a sterile transfer syringe.
- Direct the water against the inner wall of the peptide vial as it is injected — never onto the lyophilized cake.
- Invert slowly or swirl gently until dissolved. Do not vortex or shake.
- Refrigerate at 2–8 °C.
Frequently asked questions
What is SNAP-8?
SNAP-8 (Acetyl Octapeptide-3) is a synthetic octapeptide that mimics a fragment of SNAP-25, a SNARE-complex protein. It is an elongated analogue of Argireline studied in topical cosmetic-science research.
How does SNAP-8 differ from Argireline?
SNAP-8 extends the SNAP-25 mimetic sequence from six residues (Argireline) to eight, a modification designed to enhance SNARE-complex binding.
What is the regulatory status?
Supplied as a research-grade reagent for laboratory use only, not for human, cosmetic, or veterinary use.
How is SNAP-8 verified?
Each batch passes through an independent third-party analytical lab for HPLC purity and mass-spectrometry identity confirmation, to a minimum of 99 percent purity.
How do I receive the COA for my batch?
A certificate of analysis is available for your specific batch on request, tied to your lot.
References
- Blanes-Mira C et al. A synthetic hexapeptide (Argireline) with antiwrinkle activity. International journal of cosmetic science. 2002. PMID 18498523.
- Wang Y et al. The anti-wrinkle efficacy of argireline, a synthetic hexapeptide, in Chinese subjects: a randomized, placebo-controlled study. American journal of clinical dermatology. 2013. PMID 23417317.
- Südhof TC, Rothman JE. Membrane fusion: grappling with SNARE and SM proteins. Science (New York, N.Y.). 2009. PMID 19164740.
