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Snap-8
Price range: $32.00 through $281.00
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VERIFICATION
How to read this report
Snap-8, in structural terms.
- Sequence
- Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ One-letter representation: Ac-EEMQRRAD-NH₂ The sequence corresponds to residues 12–19 of human SNAP-25 (UniProt P60880). SNAP-8 extends the shorter hexapeptide acetyl hexapeptide-8 by two residues at the C-terminus.
- Molecular formula
- C₄₁H₇₀N₁₆O₁₆SPubChem CID 76283482.
- Molecular weight
- 1075.2 g/molNet peptide content is reported on a per-vial basis on the certificate of analysis published on this page.
- CAS number
- 868844-74-0 — Acetyl octapeptide-3 (SNAP-8)
- Peptide length
- 8 amino acids
- Structure type
- Linear peptide
- Primary molecular target
- SNAP-25 within the SNARE complex (syntaxin-1A, VAMP-2, SNAP-25)The proposed mechanism is competitive interference with SNAP-25 incorporation into the ternary SNARE complex, reducing the efficiency of vesicle docking and fusion. This model derives from in vitro complex assembly work rather than from receptor binding studies.
- Physical form
- Lyophilized powder
- PubChem CID
- 76283482
SNAP-8 is an eight-residue peptide that reproduces a segment of the N-terminal region of SNAP-25, a core component of the SNARE complex that mediates vesicle fusion at the presynaptic membrane. The peptide is N-terminally acetylated and C-terminally amidated. It is studied as a competitive mimic that can occupy a SNAP-25 binding position within the assembling complex.
Where Snap-8 appears in the literature.
- Published experimental use of SNARE-derived peptides includes:
- In vitro SNARE complex assembly and disassembly assays
- Liposome fusion assays reconstituted with purified SNARE proteins
- Catecholamine release assays in chromaffin cell preparations
- Peptide penetration and delivery studies in reconstructed skin models
- Stability and formulation studies for topical carrier systems
- These areas describe experimental research contexts and do not establish therapeutic efficacy or safety in humans.
- Experimental systems reported in this literature include:
- Purified recombinant SNARE protein preparations
- Reconstituted proteoliposome fusion systems
- Bovine chromaffin cell cultures
- Reconstructed human epidermis models
- Franz diffusion cell systems for permeation study
- Assay formats reported in this literature include:
- SDS-resistant SNARE complex formation assayed by gel electrophoresis
- FRET-based liposome fusion assays
- Amperometric detection of catecholamine release
- HPLC quantification in permeation studies
- Circular dichroism for peptide secondary structure
- Reversed-phase HPLC and mass spectrometry for identity and purity
- Endpoints reported in published research on SNARE-derived peptides include:
- SNARE complex formation efficiency relative to control
- Lipid mixing rate in reconstituted fusion assays
- Catecholamine release amplitude and frequency
- Cumulative permeation and flux in skin models
- Chromatographic purity and mass accuracy
- Research use only. Not for human or animal consumption.
What has been studied, and in what systems.
Research on SNAP-8 sits at the intersection of two literatures: the well-established structural and functional biology of the SNARE complex, and a smaller applied literature concerning peptide delivery in topical formulation. Compound-specific primary research on the octapeptide itself is limited; most mechanistic understanding is inferred from the broader SNARE literature and from work on the related hexapeptide.
These are published research systems. They do not describe approved clinical applications, and they do not establish efficacy or safety in humans.
Palfreyman MT et al., 2023. SNARE Proteins in Synaptic Vesicle Fusion. Adv Neurobiol. PMID 37615864. https://pubmed.ncbi.nlm.nih.gov/37615864/
Rizo J et al., 2024. Molecular mechanism underlying SNARE-mediated membrane fusion enlightened by all-atom molecular dynamics simulations. Proc Natl Acad Sci U S A. PMID 38593076. https://pubmed.ncbi.nlm.nih.gov/38593076/
Yang J et al., 2022. A dynamic template complex mediates Munc18-chaperoned SNARE assembly. Proc Natl Acad Sci U S A. PMID 36454760. https://pubmed.ncbi.nlm.nih.gov/36454760/
About this compound and its batch data.
What purity did this Snap-8 batch achieve?
Lot NP810 was analysed by Freedom Diagnostics and returned chromatographic purity of 99.18% by HPLC with UV detection coupled to mass spectrometry. Identity was confirmed by mass spectral match. The full certificate is published on this page, and every figure shown here is taken from it.
How much Snap-8 is in the vial?
The laboratory measured 11.54 mg, which is 115.4% of the label claim. Net content is reported on a per-vial basis. Astramide publishes the measured figure rather than the label claim, whether it falls above or below.
Was this Snap-8 batch tested for endotoxins?
Yes. Endotoxin testing was performed using the Limulus Amebocyte Lysate assay in accordance with USP <85>, and this batch returned Pass, 2 of 2 at ≤0.05 EU/mL. The result appears on the certificate published on this page.
How should Snap-8 be stored for research use?
As supplied, the lyophilized powder should be held at -20°C and protected from light and moisture. Once reconstituted, store at 2-8°C and use within 14 to 30 days. Avoid repeated freeze-thaw cycles and follow the handling procedures appropriate to your laboratory.
What is the difference between research-grade and pharmaceutical-grade Snap-8?
These are separate classifications. Research-grade material is supplied for laboratory research use only and is not intended for human or animal consumption. Pharmaceutical-grade is an FDA classification that applies to drugs manufactured for human use. Astramide supplies research-grade material only.
How can I verify this Snap-8 certificate independently?
The certificate was issued by Freedom Diagnostics under lot NP810, laboratory reference 2606080460. Quote that reference to the laboratory directly. The same document is published here in full, and is not summarised or reformatted by Astramide.
This product is intended strictly for in-vitro laboratory research conducted by qualified professionals. It is not intended for human or animal consumption, clinical use, or therapeutic application. The statements on this page have not been reviewed by the FDA. These research peptides are not intended to diagnose, treat, cure, or prevent any disease. Research Use Only.








