SNAP-8 10 mg

SNAP-8 (Acetyl Glutamyl Octapeptide-3) is a synthetic, acetylated octapeptide whose sequence is derived from the N-terminal region of the SNAP-25 protein, a core component of the SNARE complex. It belongs to the family of acetylated peptides that are investigated as model compounds in peptide and cosmetic chemistry. Within scientific research, SNAP-8 is studied in relation to vesicular signaling and the stability of short synthetic peptides. Intended exclusively for laboratory and research purposes.

What is SNAP-8?

SNAP-8 is an octapeptide with the amino acid sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ (Ac-EEMQRRAD-NH₂ for short). The compound is an extended analog of Argirelin (Acetyl Hexapeptide-8, also called Acetyl Hexapeptide-3): whereas that molecule has six amino acids, SNAP-8 adds two extra residues (alanine and aspartic acid) to the C-terminal end. The N-terminus carries an acetyl group and the C-terminus an amide group. Both modifications increase resistance to degradation by amino- and carboxypeptidases, making SNAP-8 a structurally stable model for research on short peptides.

The research importance of SNAP-8 stems from that derived sequence. Because the fragment mimics the N-terminal motif of SNAP-25, it is used in a laboratory context as a model compound to study the assembly of the SNARE complex—the protein complex that drives vesicle fusion—and the associated release of signaling molecules. In this sense, SNAP-8 functions as a defined, reproducible tool for mechanistic research, not as a compound with an application outside the laboratory.

Áreas de investigación

In a laboratory context, SNAP-8 is used in the following research areas, among others:

• SNARE complex and SNAP-25 research — model link for the assembly of the SNARE fusion complex in in vitro vesicle fusion models.
• Vesicular signaling — models regarding the release of catecholamines and acetylcholine at the neuromuscular junction in controlled systems.
• Dermatological peptide models — research into mimic muscle cell signaling and extracellular matrix-related components in cell culture.
• Peptide formulation and stability — study of solubility and proteolytic stability of acetylated and amidated octapeptides.
• Structure-Activity Study (SAR) — comparison with shorter argireline-like analogues to model the effect of sequence length.
• Analytical reference — use as an HPLC reference standard in the characterization of synthetic peptides.

SNAP-8 compared with related compounds

Within the range of investigational peptides with a dermatological research background, SNAP-8 stands alongside several related molecules that each model a different mechanism. GHK-Cu is a copper tripeptide that is classically studied in models involving the extracellular matrix and collagen expression, while Matrixyl as a palmitoyl pentapeptide features in collagen and skin research models. Whereas those two focus on matrix and synthesis pathways, SNAP-8 falls within the SNARE and signaling molecule domain, making the molecules complementary in comparative research.

SNAP-8 also appears as a component in a topical research formulation: the GHK-Cu and SNAP-8 Serum 30ml combines both peptides for research into concurrent matrix and signaling molecule models. The separate SNAP-8 vial offered here is intended for researchers who wish to reconstitute and characterize the compound separately.

Presupuesto

Forma, manipulación y almacenamiento

SNAP-8 is supplied as a freeze-dried powder (lyophilisate) of 10 mg per vial. In a research context, the lyophilisate is reconstituted with a suitable solvent such as bacteriostatic or sterile water before use; the octapeptide is highly water-soluble. Handle the powder in a cool place and protected from light and moisture, and avoid repeated freeze-thaw cycles to maintain structural integrity.

The dry lyophilisate is most stable when stored in a cool, dark place. After reconstitution, the solution is usually stored refrigerated (2–8 °C) and used within a limited period. Work with clean, calibrated materials and record the concentration and date of reconstitution so that measurements remain reproducible. In research, dosages are expressed in mg of active substance per experiment.

Pureza y resultados de laboratorio

SNAP-8 is offered with a controlled purity of ≥ 99%, determined via HPLC. This degree of purity makes the compound suitable as a defined model compound and reference standard in analytical and preclinical research. Certificates of analysis and lab results of our research compounds can be found bundled on the página de resultados de laboratorio.

Preguntas frecuentes

What exactly is SNAP-8?
SNAP-8 is a synthetic, acetylated octapeptide (Acetyl Glutamyl Octapeptide-3) with a sequence derived from the SNAP-25 protein. It is used in scientific research as a model compound regarding vesicular signaling and peptide stability.

How does SNAP-8 differ from Argireline?
SNAP-8 is an extended analog of Argireline (Acetyl Hexapeptide-8). Whereas Argireline has six amino acids, SNAP-8 carries two extra residues (Ala-Asp) at the C-terminal end, making it a longer model variant for comparative research.

In what form is SNAP-8 delivered?
As a freeze-dried powder (lyophilisate) of 10 mg per vial, with a purity of ≥ 99% (HPLC). In research, it is reconstituted with bacteriostatic or sterile water.

How do I store SNAP-8?
Store the dry lyophilisate in a cool, dark place, protected from light and moisture. After reconstitution, the solution is stored refrigerated (2–8 °C).

Is SNAP-8 suitable for human or cosmetic use?
No. SNAP-8 is offered exclusively for laboratory and research purposes and is not intended for human or animal consumption or for cosmetic use.

¿Quieres saber más? Lea nuestra guía: Agua bacteriostática: ¿para qué se utiliza y cómo se prepara correctamente?

Destinado exclusivamente a fines de laboratorio e investigación. No apto para consumo humano ni animal, ni para uso médico, diagnóstico, terapéutico o cosmético. El comprador debe ser mayor de 18 años y confirmar el contexto de la investigación. No es un medicamento.