Semax
Semax is a synthetic heptapeptide consisting of the ACTH(4-7) fragment Met-Glu-His-Phe extended by the tripeptide Pro-Gly-Pro. Developed in Russia, it is studied in neurotrophic-signalling and cognitive model systems and is registered as a medicine in Russia but in no Western jurisdiction. VaultLabs supplies Semax as a lyophilised reference material for in vitro laboratory research only.
Research use only. For in vitro research use only. Not for human or animal consumption. Not for human consumption, medical use, or personal application.
Reviewed by VaultLabs Research Editorial Desk · Last updated 2026-08-03
Key facts
- Sequence is Met-Glu-His-Phe-Pro-Gly-Pro — an ACTH(4-7) fragment with a C-terminal Pro-Gly-Pro extension that slows enzymatic degradation.
- CAS registry number 80714-61-0; molecular formula C37H51N9O10; molecular weight 813.87 g/mol.
- Unlike the ACTH fragment it derives from, Semax is described in the literature as lacking corticotropic activity.
- Research themes are neurotrophic factor expression, particularly BDNF, and cognitive and neuroprotective model systems.
- Registered as a medicine in Russia; not approved by the UAE Ministry of Health and Prevention, the FDA or the EMA.
- Chemical name
- Semax (ACTH 4-10 analogue heptapeptide)
- Common synonyms
- MEHFPGP, ACTH(4-7)-PGP
- Sequence
- Met-Glu-His-Phe-Pro-Gly-Pro
- CAS number
- 80714-61-0
- Molecular formula
- C37H51N9O10
- Molecular weight
- 813.87 g/mol
- Appearance
- White lyophilised powder
- Catalog strength
- 10 mg vial
What Semax is
Semax is a seven-residue synthetic peptide built from two parts. The first four residues, Met-Glu-His-Phe, correspond to a fragment of adrenocorticotropic hormone. The final three, Pro-Gly-Pro, are a synthetic addition whose stated purpose in the design literature is to slow enzymatic breakdown of the peptide.
That design choice is the interesting part chemically. Proline-rich termini resist common exopeptidases, so appending Pro-Gly-Pro extends the useful lifetime of an otherwise very short peptide. The approach recurs across the Russian peptide-design programme that produced Semax and its relatives.
Despite deriving from an ACTH fragment, Semax is described in the literature as lacking the corticotropic activity of the parent hormone — the retained fragment is outside the region responsible for that effect. This is a point worth stating precisely, because the ACTH association is often misread.
Where the research literature sits
Semax has a substantial Russian-language literature and a smaller indexed English-language one. The dominant research themes are expression of neurotrophic factors, particularly brain-derived neurotrophic factor, and neuroprotection in ischaemia and stress model systems, generally in rodents or cell culture.
A practical caveat for anyone reviewing this evidence: much of the foundational work predates current reporting standards and is not indexed in the databases most researchers search first. Claims about Semax that circulate online frequently trace back to sources that are difficult to retrieve and evaluate. Treat the accessible preclinical record as the evidence base and read the rest with care.
Semax is registered as a medicine in Russia. It is not approved in the UAE, the United States or the European Union, and VaultLabs supplies it strictly as a research material irrespective of its regulatory status elsewhere.
Analytical characterisation and handling
Release is by reversed-phase HPLC against a stated purity specification, with the certificate tied to the vial lot number. The methionine residue at position one is the notable analytical feature: methionine is readily oxidised, and the oxidised form is a common related substance to look for in the chromatogram.
That same sensitivity drives the handling advice. Store sealed lyophilised vials at 2–8 °C protected from light, minimise open-vial time, and avoid conditions that promote oxidation once the material is in solution. Equilibrate vials to room temperature before opening to prevent condensation onto the cake.
After reconstitution, prepare close to the point of use, log the diluent and reconstitution date, and keep freeze-thaw cycles to a minimum. The certified purity applies to the released lyophilised material, not to a solution held over time.
Regulatory position and supply
Semax supplied by VaultLabs is a research reference material and is not supplied for human or veterinary use. Its registration as a medicine in another jurisdiction does not change that, and it confers no permission to use VaultLabs material in a person.
The catalog presentation is a 10 mg lyophilised vial held under controlled cold storage before dispatch, with lot-linked certificate retrieval through the batch verification tool.
Research interest areas
Neuronal culture viability assays
BDNF expression panels
Ischemia-reperfusion models (preclinical)
Cognitive behavior models (rodent literature)
Storage information
2–8 °C (lyophilized, sealed)
2–8 °C for sealed lyophilized vials. Avoid freeze-thaw on prepared solutions unless validated in your workflow.
Stability notes
Lyophilized Semax is stable when sealed and cold-stored. Reconstituted solutions degrade faster — use documented short-term storage windows.
Selected literature
Named papers behind the statements on this page. Each entry resolves on PubMed and through its DOI, so you can read the source rather than take our summary of it. Inclusion describes the research record and is not a claim about this material’s suitability for any use.
Semax, an analog of ACTH(4-10) with cognitive effects, regulates BDNF and trkB expression in the rat hippocampus
Dolotov OV, et al. · Brain Research · 2006
Primary rodent study underlying the neurotrophic-signalling claims commonly made about this sequence.
Semax, an ACTH(4-10) analogue with nootropic properties, activates dopaminergic and serotoninergic brain systems in rodents
Eremin KO, et al. · Neurochemical Research · 2005
Preclinical neurochemistry in rodents; characterises the monoamine endpoints reported for Semax.
Databases and verification
Registry and database entries for independent identity checks. These are standing searches rather than fixed records, so they stay current as new work is indexed.