Product Description
Acetyl Hexapeptide-8 (AH-8) is a synthetic hexapeptide with the amino acid sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-NH₂. This sequence corresponds to the N-terminal fragment of the synaptosomal-associated protein of 25 kDa (SNAP-25), a key component of the neuronal SNARE complex. The peptide is acetylated at the N-terminus and amidated at the C-terminus, modifications that enhance resistance to exopeptidases and improve stability in biological media. In the research supply chain, it is often catalogued under the cosmetic ingredient name Argireline; however, as a raw material for investigative laboratories, it is correctly identified by its International Nomenclature Cosmetic Ingredient (INCI) designation—Acetyl Hexapeptide-8—or its CAS number 616204-22-9.
For laboratories searching for a high‑purity Acetyl Hexapeptide-8 raw material for sale, our product is supplied as a sterile, lyophilized white powder that is freely soluble in water, phosphate‑buffered saline, and other aqueous buffers commonly used in cell biology. The molecular weight of the acetate salt is approximately 889.0 Da. Every lot is validated by reversed‑phase high‑performance liquid chromatography (RP‑HPLC) to guarantee a purity of ≥98%, and identity is confirmed by mass spectrometry—measures that ensure the material is suited for rigorous mechanistic studies. The absence of undefined excipients makes this peptide an ideal tool for neuronal function research, where even minor contaminants could confound interpretation of synaptic transmission data.
Anwendungen in der Forschung
Mechanism of Action Studies
The principal research application of Acetyl Hexapeptide-8 lies in its ability to inhibit the formation of the ternary SNARE complex. As originally described by Blanes‑Mira et al. (2002, International Journal of Cosmetic Science), the peptide mimics the N‑terminal α‑helical domain of SNAP‑25 and competes with the native protein for binding to syntaxin and VAMP/synaptobrevin. By disrupting the coiled‑coil bundle that drives synaptic vesicle docking and fusion, AH‑8 serves as a reversible, dose‑dependent blocker of regulated exocytosis. This mechanism has been exploited in a variety of cellular models, including primary neuronal cultures and neuroendocrine cell lines, to examine the role of SNARE proteins in neurotransmission.
In bovine adrenal chromaffin cells, for instance, the addition of AH‑8 has been demonstrated to attenuate Ca²⁺‑evoked catecholamine secretion in a concentration‑dependent manner, providing researchers with a pharmacological tool to dissect the kinetics of readily releasable and reserve vesicle pools. Electrophysiological recordings of miniature end‑plate potentials in neuromuscular junction preparations have further confirmed that the peptide’s action is specific to SNARE‑mediated fusion, not to voltage‑gated ion channels or second messenger cascades. These findings underpin the peptide’s utility in exploring synaptic plasticity, the presynaptic basis of neuromodulation, and the design of peptide‑based SNARE disruptors.
In Vitro Assays
Beyond whole‑cell electrophysiology, Acetyl Hexapeptide-8 is widely employed in biochemical and cell‑based in vitro assays. In peptide‑uptake studies, researchers label the molecule with fluorophores such as fluorescein isothiocyanate (FITC) or tetramethylrhodamine (TAMRA) to track its internalization by endocytosis and monitor intracellular trafficking via confocal microscopy. These experiments help elucidate the routes that synthetic peptides use to enter neurons and other secretory cells, as well as their subsequent localization to sub‑cellular compartments.
Stability assays using liquid chromatography‑tandem mass spectrometry (LC‑MS/MS) are performed to determine the peptide’s half‑life in cell‑culture media or cytoplasmic extracts, quantifying degradation by aminopeptidases and endopeptidases. The inhibitory activity of AH‑8 is also validated in reconstituted proteoliposome systems, where the peptide blocks lipid mixing between vesicles bearing purified SNARE proteins—an assay that specifically measures the membrane fusion step. Surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) have further quantified the binding affinity (KD in the low micromolar range) of AH‑8 for recombinant syntaxin‑1A, helping to map the critical contact residues necessary for SNARE interference. Such a comprehensive in vitro toolbox makes Acetyl Hexapeptide-8 a reference standard in membrane traffic research and early‑stage neurobiology drug discovery programs.
Qualitätssicherung
Every batch of our Acetyl Hexapeptide-8 raw material for sale undergoes rigorous analytical testing before shipment. Chromatographic purity is determined by RP‑HPLC using a C18 column and a linear gradient of acetonitrile in water containing 0.1% trifluoroacetic acid, with detection at 220 nm. The area‑percent purity must exceed 98%; any peak attributable to by‑products or deletion sequences is reported. Mass identity is confirmed by electrospray ionization mass spectrometry (ESI‑MS) on a triple‑quadrupole instrument, yielding the expected [M+H]⁺ ion. For additional confidence, selected lots are analyzed by matrix‑assisted laser desorption/ionization time‑of‑flight (MALDI‑TOF) mass spectrometry.
A Analysezertifikat (CoA) is supplied with every order and includes the following information:
- Chromatogram and purity data from RP‑HPLC
- ESI‑MS spectrum confirming molecular mass
- Peptide content determined by quantitative amino acid analysis or UV absorbance
- Residual trifluoroacetic acid (if the peptide is supplied as a TFA salt; typical value <0.1%)
- Water content (Karl Fischer titration, typically <5%)
- Residual organic solvents (gas chromatography, compliant with ICH Q3C guidelines)
- Appearance and solubility observations
Manufacturing takes place in temperature‑ and humidity‑controlled cleanrooms under a quality management system that emphasizes process validation, in‑line monitoring, and full traceability of raw materials. Accelerated and real‑time stability studies support the assigned shelf life and storage recommendations. By adhering to these stringent practices, we ensure that researchers receive a consistently reliable reagent, enabling reproducible experimental outcomes and eliminating the need for in‑house re‑characterization before use.
Packaging and Storage
Acetyl Hexapeptide-8 raw material is available in standard research quantities of 1 g, 5 g, and 10 g. The lyophilized powder is filled into amber borosilicate glass vials under a dry argon atmosphere, sealed with PTFE‑lined silicone septa, and labeled with lot number, net weight, and expiration date. Custom packaging, such as aliquots of 100 mg or bulk containers of 50 g, can be arranged to suit the demands of long‑term projects or high‑throughput screening facilities, thereby minimizing freeze‑thaw cycling and reducing handling losses.
To maintain peptide integrity, vials should be stored at −20 °C in a desiccated, light‑protected environment immediately upon receipt. The hygroscopic nature of the powder necessitates avoidance of repeated exposure to ambient moisture; storage in a sealed container with a desiccant is strongly recommended. Under these conditions, the shelf life is 24 months from the date of manufacture, as indicated on the CoA. Once reconstituted in sterile, degassed buffer, stock solutions should be aliquoted into single‑use volumes and stored at −20 °C or −80 °C. While solutions kept at 4 °C may be usable for up to one week, researchers should verify peptide stability under their own assay conditions, as degradation can be accelerated by specific buffer compositions or light exposure.
Bestellinformationen
If you are sourcing Acetyl Hexapeptide-8 raw material for sale, please find our standard terms below. The minimum order quantity is 1 g. For standard orders up to 10 g, the lead time is 2–3 business days after confirmation of payment. Larger quantities and customized packaging requests may require additional processing time; a specific delivery schedule will be provided during quotation. We ship to research institutions, pharmaceutical companies, and authorized distributors worldwide, with all necessary documentation for international customs clearance.
Each shipment includes a commercial invoice, the batch‑specific Certificate of Analysis, and a Material Safety Data Sheet (MSDS) outlining safe handling, personal protective equipment recommendations, and first‑aid measures. As this product is intended strictly for laboratory research, it is not registered with the U.S. Food and Drug Administration, the European Medicines Agency, or any other regulatory body for diagnostic, therapeutic, or cosmetic use. Shipments comply with the import regulations of the destination country, and appropriate harmonized system codes for research‑only peptides are used to expedite processing. Cold‑chain logistics (dry ice) can be arranged at the client’s request to maintain low temperatures during transit, particularly for temperature‑sensitive destinations. For pricing, bulk discounts, batch reservations, or technical inquiries, please contact our sales team through the B2B portal or by email; all communications are treated confidentially.
Research use only statement: This product is intended solely for laboratory research purposes. It is not for human or veterinary use. The information provided here is not intended to diagnose, treat, cure, or prevent any disease, and has not been evaluated by any regulatory agency. Purchasers are responsible for ensuring compliance with all applicable laws and regulations governing the use of research compounds in their jurisdiction.
Nur für Forschungszwecke. Nicht zur Anwendung am Menschen oder bei Tieren bestimmt.
