PRODUCTS SOLD ON PEPTIDESLABUAE.COM ARE FOR RESEARCH PURPOSES ONLY AND ARE NOT FOR HUMAN OR VETERINARY USE.
PRODUCTS SOLD ON PEPTIDESLABUAE.COM ARE FOR RESEARCH PURPOSES ONLY AND ARE NOT FOR HUMAN OR VETERINARY USE.
£27.00
Buy SNAP-8 Peptide in UAE – In Stock & Ready to Ship
SNAP-8 is a widely researched peptide known for its role in neurotransmitter release and facial muscle contraction studies. Each batch is independently verified at ≥99% purity and comes with a full Certificate of Analysis (COA) and HPLC testing documentation — giving UAE research teams the confidence they need when sourcing peptides for serious work.
For research use only. Not intended for human or veterinary use.
SNAP-8 (Acetyl Octapeptide-3) is one of the most studied synthetic peptides in dermatological and neuromuscular junction research available to laboratories in the UAE — an eight amino acid peptide that mimics the N-terminal end of SNAP-25, a protein involved in the SNARE complex responsible for neurotransmitter vesicle docking at neuromuscular junctions, making it a highly referenced research tool for studying acetylcholine release inhibition, synaptic signalling, and cutaneous biology. Researchers and institutions across the UAE, Dubai, Abu Dhabi and the wider GCC can source verified, research-grade SNAP-8 with fast international dispatch and full batch documentation included.
✅ ≥99% Purity — HPLC & Mass Spectrometry Verified
✅ Batch-Specific Certificate of Analysis (CoA)
✅ Sterile Lyophilised Powder | GMP Manufactured
✅ Fast International Dispatch to UAE & GCC
SNAP-8, also known as Acetyl Octapeptide-3 or Leuphasyl, is a synthetic octapeptide — an eight amino acid chain — designed to mimic the N-terminal fragment of SNAP-25 (Synaptosomal-Associated Protein 25), a core component of the SNARE (Soluble NSF Attachment Protein Receptor) complex. The SNARE complex is the molecular machinery responsible for docking and fusing neurotransmitter-containing vesicles with the presynaptic membrane at neuromuscular junctions — the essential step that triggers acetylcholine release and subsequent muscle contraction.
By mimicking the N-terminal sequence of SNAP-25, SNAP-8 is studied for its ability to competitively interfere with SNARE complex assembly — potentially modulating the efficiency of vesicle docking and neurotransmitter release at the junction level. This mechanism makes it structurally and functionally related to Argireline (Acetyl Hexapeptide-3), of which it is considered an extended analogue, with research suggesting the additional two amino acids may enhance its interaction with the SNARE complex compared to the hexapeptide form.
SNAP-8 is water soluble, well-characterised in terms of its primary sequence and molecular weight, and has become a standard reference compound in laboratory studies examining SNARE complex biology, neuromuscular junction signalling, and peptide interactions with synaptic protein complexes.
In laboratory settings, SNAP-8 research centres on its interaction with the SNARE complex and neuromuscular junction signalling machinery. Research applications include:
Its extended octapeptide sequence relative to Argireline makes it a useful comparative research tool for examining how peptide chain length influences SNARE complex interaction efficiency and neurotransmitter modulation in controlled experimental models. All applications are for research use only.
SNAP-8 has accumulated a focused and well-characterised research profile within SNARE biology and synthetic peptide science:
Research examining SNAP-8’s interaction with the SNARE complex has characterised its competitive mimicry of the SNAP-25 N-terminal domain — with studies documenting its ability to integrate into SNARE complex assembly processes and modulate vesicle docking efficiency in controlled in vitro models, providing insights into the structural requirements for SNARE complex formation and how peptide fragments derived from core SNARE proteins can influence the assembly process.
Comparative studies between SNAP-8 and Argireline (Acetyl Hexapeptide-3) have examined whether the additional two amino acids in SNAP-8’s sequence translate to enhanced SNARE complex interaction — with research exploring the structure-activity relationships that govern how peptide length and sequence influence binding affinity and functional potency at the SNARE complex level. These comparative studies have made both compounds important reference tools in synthetic SNARE-targeting peptide research.
In vitro neuromuscular junction studies have used SNAP-8 to examine acetylcholine release dynamics under conditions of competitive SNARE complex interference — providing controlled experimental models for studying how modulation of vesicle docking efficiency translates to changes in neurotransmitter output at the junction level. Cutaneous biology research has examined SNAP-8’s behaviour in dermal tissue models, studying its penetration characteristics, stability in biological matrices, and interaction with skin-resident cell types — reflecting the broader interest in SNARE-targeting peptides as tools for studying neuromuscular signalling in cutaneous tissue contexts.
| Compound | Type | Length | SNARE Target | Research Focus | Research Profile |
|---|---|---|---|---|---|
| SNAP-8 (Acetyl Octapeptide-3) | Synthetic peptide | 8 AA | SNAP-25 N-terminal | SNARE complex, NMJ signalling | Well-documented |
| Argireline (Acetyl Hexapeptide-3) | Synthetic peptide | 6 AA | SNAP-25 N-terminal | SNARE complex, comparative | Most studied |
| Leuphasyl (Pentapeptide-18) | Synthetic peptide | 5 AA | Enkephalin receptor / SNARE | Synergistic SNARE research | Growing |
| SYN-AKE | Synthetic tripeptide | 3 AA | nAChR (nicotinic) | Receptor-level NMJ modulation | Well-documented |
| Botulinum Toxin Type A | Protein toxin | N/A | SNAP-25 cleavage | SNARE cleavage reference | Extensively studied |
| Parameter | Detail |
|---|---|
| Type | Synthetic Octapeptide |
| Also Known As | Acetyl Octapeptide-3 |
| Sequence Target | SNAP-25 N-terminal mimetic |
| Chain Length | 8 Amino Acids |
| Purity | ≥99% |
| Verification | HPLC & Mass Spectrometry |
| Form | Lyophilised Powder |
| Solubility | Sterile water or suitable laboratory buffer |
| Storage | -20°C, protected from light and moisture |
| Intended Use | Research use only |
Every order dispatched to the UAE and GCC includes:
Yes. We supply research-grade SNAP-8 with international dispatch to the UAE, Dubai, Abu Dhabi, Sharjah and across the GCC. All orders include full batch documentation and are packaged to maintain peptide integrity throughout transit. This compound is supplied strictly for laboratory research use only.
Both SNAP-8 and Argireline (Acetyl Hexapeptide-3) are synthetic peptides that mimic the N-terminal domain of SNAP-25 and are studied for their interaction with the SNARE complex. The primary structural difference is chain length — SNAP-8 contains eight amino acids versus Argireline’s six. Research has examined whether this extended sequence enhances SNARE complex interaction affinity or functional potency, making the two compounds important comparative tools in structure-activity relationship studies on SNARE-targeting peptides.
The SNARE complex is the core molecular machinery that mediates vesicle fusion with cell membranes — in neuromuscular junctions, this translates to the docking and release of acetylcholine-containing vesicles that trigger muscle contraction. It comprises three core proteins: SNAP-25, syntaxin, and synaptobrevin. Research into SNARE complex biology is central to understanding neurotransmitter release mechanisms, synaptic signalling regulation, and how peptide fragments derived from SNARE proteins can modulate complex assembly — areas in which SNAP-8 serves as a key research tool.
SNAP-25 (Synaptosomal-Associated Protein 25) is one of the three core proteins of the SNARE complex. SNAP-8 is designed to mimic the N-terminal fragment of SNAP-25’s sequence — allowing it to competitively interact with SNARE complex assembly processes in research models. Studies use this mimicry to examine how the N-terminal domain of SNAP-25 contributes to SNARE complex formation and vesicle docking efficiency, providing structural and functional insights into one of the most important protein complexes in neurobiology.
Both SNAP-8 and Botulinum Toxin Type A target SNAP-25, but through entirely different mechanisms. Botulinum Toxin cleaves SNAP-25 proteolytically, permanently disabling SNARE complex formation. SNAP-8 competitively mimics the SNAP-25 N-terminal sequence, potentially modulating — rather than destroying — SNARE complex assembly. Research comparing these two mechanisms has provided valuable insights into the structural requirements for SNARE complex function and the different ways SNAP-25 interaction can influence neurotransmitter release in experimental models.
Allow the vial to reach room temperature before opening. Add sterile water or appropriate laboratory buffer slowly down the vial wall and swirl gently without shaking. Prepare at your protocol’s required concentration. Aliquot and store at -80°C to minimise freeze-thaw degradation and maintain peptide integrity between experimental sessions.
Orders are dispatched promptly via tracked international courier. Delivery to the UAE typically takes 3–5 working days, with packaging designed to maintain peptide stability and integrity throughout transit.
SNAP-8 (Acetyl Octapeptide-3) is supplied exclusively for legitimate scientific research conducted within licensed laboratory environments. This product is not intended for human consumption, self-administration, or any therapeutic or veterinary application. It must be handled solely by qualified researchers in compliance with applicable UAE regulations and institutional ethics guidelines. By purchasing, you confirm this compound will be used exclusively for approved in vitro or pre-clinical research purposes.
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