For Research Use Only
SNAP-8 is supplied exclusively for in vitro laboratory and pre-clinical research. Not for human or veterinary use. No formulation, application, or usage guidance is provided. Purchase confirms the buyer is a qualified researcher.
SNAP-8 10mg — Acetyl Octapeptide-3 for Neuromuscular Junction and SNARE Complex Research
SNAP-8 10mg is a research-grade lyophilised preparation of SNAP-8 (Acetyl Octapeptide-3), a synthetic octapeptide analogue of the N-terminal sequence of SNAP-25 (synaptosomal-associated protein 25 kDa), a key component of the SNARE (soluble NSF attachment protein receptor) complex responsible for neurotransmitter exocytosis at the neuromuscular junction. The sequence of SNAP-8 is Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ (Acetyl-EEMQRRAD-NH₂), corresponding to residues 12–19 of the SNAP-25 protein. SNAP-8 was developed as an extended analogue of the tetrapeptide Acetyl Glutamyl Heptapeptide-3 (Argireline), incorporating four additional amino acids from the SNAP-25 sequence to potentially enhance binding affinity and competitive inhibition of SNARE complex formation. Each 10mg vial supplied by AbsoluteBioLab contains lyophilised SNAP-8 acetate salt, verified by RP-HPLC to a minimum purity of ≥99.0%, with molecular identity confirmed by ESI-MS.
The SNARE complex is the core molecular machinery responsible for calcium-triggered neurotransmitter exocytosis at synaptic terminals and neuromuscular junctions. The complex is formed by the assembly of three SNARE proteins: SNAP-25 (on the presynaptic membrane), syntaxin-1 (on the presynaptic membrane), and VAMP/synaptobrevin (on the synaptic vesicle). Upon calcium influx triggered by an action potential, the SNARE complex zippers together, bringing the vesicle membrane into close apposition with the presynaptic membrane and driving membrane fusion and neurotransmitter release. SNAP-8 is proposed to compete with endogenous SNAP-25 for incorporation into the SNARE complex, thereby modulating the efficiency of SNARE complex assembly and vesicle fusion. This mechanism makes SNAP-8 a research tool for investigating SNARE complex dynamics, neuromuscular junction physiology, and the molecular mechanisms of neurotransmitter exocytosis.
Compound Identity Matrix
| Attribute | Value | Specification |
|---|---|---|
| Common Name | SNAP-8; Acetyl Octapeptide-3 | Synthetic SNAP-25 N-terminal octapeptide analogue |
| Sequence | Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ | 8 amino acids; N-Ac; C-terminal amide; SNAP-25 residues 12–19 |
| CAS Number | 868844-74-0 | SNAP-8 (Acetyl Octapeptide-3) |
| Molecular Formula | C41H70N14O16S | Free base |
| Molecular Weight | 1,075.15 Da | Free base (monoisotopic) |
| Molecular Target | SNARE complex / SNAP-25 | Competitive inhibitor of SNARE complex assembly |
| Physical Form | White lyophilised powder | Acetate salt; hygroscopic |
| Quantity per Vial | 10 mg | Research-grade lyophilised preparation |
| Purity (RP-HPLC) | ≥99.0% | C18 column, UV 220 nm |
| Identity Confirmation | ESI-MS | ±0.1 Da of theoretical MW |
Analytical Specification & Release Testing
Every batch of SNAP-8 10mg supplied by AbsoluteBioLab is manufactured under GMP-aligned conditions and subjected to a comprehensive analytical release protocol. Purity is determined by RP-HPLC (C18 column, UV 220 nm) confirming ≥99.0% purity with a maximum single impurity of ≤0.5%. Molecular identity is confirmed by ESI-MS with the observed [M+nH]ⁿ⁺ ion series matched against the theoretical mass of SNAP-8 (MW 1,075.15 Da) to within ±0.1 Da. Endotoxin content is confirmed at <1.0 EU/mg by LAL kinetic turbidimetric assay. Residual moisture is confirmed at <5.0% w/w by Karl Fischer titration.
| Test Parameter | Method | Specification | Typical Result |
|---|---|---|---|
| Purity (RP-HPLC) | C18 column, UV 220 nm | ≥99.0% | ≥99.5% |
| Identity (ESI-MS) | Electrospray ionisation MS | ±0.1 Da of theoretical MW | Conforms |
| Endotoxin (LAL) | Kinetic turbidimetric LAL | <1.0 EU/mg | <0.5 EU/mg |
| Residual Moisture | Karl Fischer titration | <5.0% w/w | <3.0% w/w |
| Appearance | Visual inspection | White lyophilised powder | Conforms |
Mechanism of Action — SNARE Complex Competitive Inhibition
SNAP-8 is proposed to act as a competitive inhibitor of SNARE complex assembly by mimicking the N-terminal sequence of SNAP-25 (residues 12–19). The SNARE complex is assembled through the progressive, N-to-C terminal zippering of the coiled-coil domains of SNAP-25 (contributing two helices), syntaxin-1, and VAMP/synaptobrevin. The N-terminal region of SNAP-25 that SNAP-8 mimics is involved in the initial nucleation of SNARE complex assembly — the rate-limiting step in the zippering process. By competing with endogenous SNAP-25 for binding to syntaxin-1 and VAMP at this nucleation site, SNAP-8 is proposed to reduce the efficiency of SNARE complex assembly and thereby modulate the probability of calcium-triggered vesicle fusion.
SNAP-8 is structurally related to Argireline (Acetyl Hexapeptide-3, Ac-EEMQRR-NH₂), which corresponds to residues 12–17 of SNAP-25. SNAP-8 extends the Argireline sequence by two additional amino acids (Ala-Asp, residues 18–19), potentially providing enhanced binding affinity for the SNARE complex nucleation site. Both compounds are used as research tools for investigating the molecular mechanisms of SNARE-mediated vesicle fusion and the consequences of partial SNARE complex inhibition on neurotransmitter release kinetics and neuromuscular junction function.
SNARE Complex Research Targets
| Target / Component | Role in SNARE Complex | SNAP-8 Interaction |
|---|---|---|
| SNAP-25 | Presynaptic membrane t-SNARE; contributes two SNARE motifs | SNAP-8 mimics SNAP-25 N-terminal sequence (residues 12–19) |
| Syntaxin-1 | Presynaptic membrane t-SNARE; anchors SNARE complex | Competitive inhibition of SNAP-25/syntaxin-1 interaction |
| VAMP/Synaptobrevin | Vesicle v-SNARE; drives membrane fusion upon zippering | Indirect effect via reduced SNARE complex nucleation |
| Neuromuscular junction | Site of acetylcholine exocytosis; SNARE-dependent | Pre-clinical model for studying SNARE inhibition effects |
Research Applications
SNAP-8 is used in neuroscience and cell biology research focused on SNARE complex dynamics and neurotransmitter exocytosis. In SNARE complex biochemistry, SNAP-8 is used in cell-free reconstitution assays to investigate the kinetics of SNARE complex assembly and the effects of competitive inhibition on zippering efficiency. Standard assays include fluorescence resonance energy transfer (FRET)-based SNARE assembly assays, surface plasmon resonance (SPR) binding studies, and co-immunoprecipitation experiments to characterise SNAP-8 binding to SNARE complex components.
In neuromuscular junction research, SNAP-8 is employed in electrophysiological studies of neuromuscular transmission, including miniature endplate potential (mEPP) frequency analysis and evoked endplate potential (EPP) amplitude measurements in nerve-muscle preparations. These assays allow researchers to quantify the effects of SNARE complex inhibition on the probability and kinetics of acetylcholine release at the neuromuscular junction.
SNAP-8 is also used in comparative pharmacology studies alongside Argireline (Acetyl Hexapeptide-3) to investigate the structure-activity relationships of SNAP-25-derived peptides as SNARE complex inhibitors. The two-amino-acid extension in SNAP-8 relative to Argireline provides a useful tool for probing the contribution of residues 18–19 of SNAP-25 to SNARE complex nucleation and inhibitor binding affinity.
Storage, Stability & Handling
| Condition | Specification | Notes |
|---|---|---|
| Long-term storage (lyophilised) | −20°C | Stable for ≥24 months from manufacture date |
| Short-term storage (lyophilised) | 2–8°C | Acceptable for up to 4 weeks; desiccated |
| Reconstituted solution | 2–8°C, use within 14 days | Aliquot and freeze at −80°C for extended storage |
| Freeze-thaw cycles | Minimise; ≤3 cycles recommended | Aliquot prior to freezing |
| Humidity | Low humidity environment | Hygroscopic peptide; desiccant recommended |
Frequently Asked Questions
What is the molecular weight of SNAP-8?
The molecular weight of SNAP-8 (Acetyl Octapeptide-3) is 1,075.15 Da (free base). The molecular formula is C41H70N14O16S and the CAS number is 868844-74-0. The sequence is Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂.
How does SNAP-8 differ from Argireline (Acetyl Hexapeptide-3)?
Argireline (Acetyl Hexapeptide-3, Ac-EEMQRR-NH₂) corresponds to residues 12–17 of SNAP-25. SNAP-8 (Acetyl Octapeptide-3, Ac-EEMQRRAD-NH₂) extends the Argireline sequence by two additional amino acids (Ala-Asp, residues 18–19). Both compounds are proposed to act as competitive inhibitors of SNARE complex assembly by mimicking the N-terminal sequence of SNAP-25. The additional residues in SNAP-8 may provide enhanced binding affinity for the SNARE complex nucleation site, making it a useful comparator compound in structure-activity relationship studies.
Is a Certificate of Analysis available?
Yes. Batch-specific CoA documents — including annotated HPLC chromatograms and MS data — are available through the AbsoluteBioLab CoA Portal and are included with each order.
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