Research Compound Reference
Semax Research Peptide
Semax is a synthetic heptapeptide, Met-Glu-His-Phe-Pro-Gly-Pro, derived from the ACTH(4-7) fragment with a C-terminal Pro-Gly-Pro extension. This reference covers its chemical identity, documented research history and analytical characterisation.
For research use only. Not for human consumption.
Chemical identity reference
- Compound name
- Semax
- Common synonyms
- ACTH(4-7)-Pro-Gly-Pro
- Peptide sequence
- MEHFPGPMet-Glu-His-Phe-Pro-Gly-Pro
- Residue count
- 7 amino acids
- Molecular formula
- C37H51N9O10S
- Average molecular weight
- ≈ 813.9 g/mol
- CAS number
- 80714-61-0
- UNII
- I5FAL2585H
- Structural origin
- Analogue of the ACTH(4-7) fragment with the natural 8–10 residues replaced by Pro-Gly-Pro
- Research classification
- Synthetic regulatory peptide (ACTH fragment analogue)
- Vial Drop research format
- Supplied as the Semax 10 mg component of the Semax / Selank 10 mg / 10 mg research blend
Chemical identity
Semax is a seven-residue synthetic peptide with the sequence MEHFPGP. The first four residues correspond to positions 4 through 7 of adrenocorticotropic hormone; the terminal Pro-Gly-Pro is a synthetic addition that replaces the natural continuation of the hormone sequence.
That C-terminal tripeptide is the design feature of the molecule. Pro-Gly-Pro is widely reported to increase resistance to aminopeptidase and carboxypeptidase activity relative to the unmodified fragment, and the substitution removes the corticotropic character of the parent hormone. Semax is consequently a distinct chemical entity from ACTH and carries its own CAS registry number, 80714-61-0.
The sequence contains methionine, which is oxidation-sensitive, and histidine, which affects ionisation behaviour — both relevant to how the material is stored and how it is measured.
Documented research history
Semax was developed in the 1980s at the Institute of Molecular Genetics of the Russian Academy of Sciences, within a research programme on neurotropic fragments of ACTH led by I. P. Ashmarin and colleagues. Published work since then has examined its structure–activity relationships, its stability profile, and its effects in animal models of neurological injury.
Mechanistic studies published in the peer-reviewed literature include work reporting increased brain-derived neurotrophic factor levels in the rat basal forebrain following intranasal administration, and physicochemical characterisation of the peptide's copper(II) binding behaviour.
An honest reading of this literature has to note its structure. The great majority of clinical and mechanistic work on Semax originates from Russian institutions, is frequently published in Russian-language journals, and is often authored by groups connected to the original development programme. Independent replication outside Russia is limited, and reported clinical studies are generally small. This is a limitation of the evidence base, and nothing on this page should be read as a statement about human use.
Analytical methodology
A heptapeptide of approximately 814 g/mol is well within the routine working range of reversed-phase HPLC. On current Vial Drop Labs reports, the chromatographic run reports the area-percent share of the principal component and its content against label claim, and identity is reported as conforming by retention-time and UV/DAD comparison against a reference standard.
No analytical report has been published for a standalone Semax material at this time. The published Vial Drop Labs report covering Semax is the one issued for the Semax / Selank 10mg / 10mg blend, and it applies to that formulation and tested sample only.
Methionine oxidation is the specific degradation route worth watching for this sequence — it produces a mass shift of +16 and a resolvable additional peak. This is one reason storage conditions and analytical documentation are discussed together.
Reading the analytical documentation
A Certificate of Analysis links a submitted sample to the analytical work performed on it. Current Vial Drop Labs reports are produced by validated HPLC-DAD methodology and answer two separate questions — what the material is, and how much of it is present.
- Identity — on current Vial Drop Labs reports, identity is reported as conforming on the basis of retention time and UV/DAD spectral comparison against a reference standard. Current reports do not include mass-spectrometry results.
- Purity — HPLC separates the dissolved sample across a column; the target peak's share of total integrated peak area is reported as an area-percent purity figure.
- Content — peptide and compound reports separately state the content per vial in mg against the stated label claim. Chromatographic purity and content per vial are two different measurements and should not be read as one.
- Sample scope — the report identifiers and test date describe the randomized sample the laboratory received and the batch it was drawn from as supplied to the laboratory. Recording the certificate ID alongside your own experimental records keeps the analytical record resolvable.
- Scope — a report describes only the specific sample submitted. Unless a report expressly states otherwise, it does not assess sterility, endotoxin, microbial content, heavy metals or residual solvents, and it is not a safety or fitness-for-use determination.
How Vial Drop publishes analytical documentation
Vial Drop Labs publishes independent analytical reports for tested research materials, with available reports accessible through the Research Documentation portal against the research material and the sample identified on each report. Each analytical report applies only to the sample submitted for analysis and should not be interpreted as testing of every vial or production unit.
Not every report is publicly listed. Where no report has been published for a material, the portal shows none rather than substituting another material's, strength's or batch's results. Documentation is never averaged, combined, or extrapolated between lots.
Current reports are issued by an independent third-party analytical laboratory using validated HPLC-DAD methodology. They report chromatographic purity as area %, content per vial against label claim, and identity as conforming by retention-time and UV/DAD comparison against a reference standard. Current reports do not include mass-spectrometry results.
Vial Drop Labs makes no representation that material is pharmaceutical grade, clinical grade, sterile, safe, or approved by any regulatory authority. Published documentation states exactly what was tested, by which method, and on which date — nothing further should be inferred from it.
Laboratory storage and handling
Material is supplied lyophilised in a sealed glass vial. General laboratory practice for lyophilised peptides applies: store sealed at -20 °C for long-term storage, protect from light, and minimise exposure to atmospheric moisture.
Allow a cold sealed vial to equilibrate to ambient temperature before opening so that atmospheric moisture does not condense onto the dry cake. Lyophilised peptide material is hygroscopic, and repeated warm/cold cycling of an opened vial is the most common cause of avoidable degradation in a laboratory setting.
Handle as an uncharacterised laboratory chemical using standard laboratory protective equipment and institutional handling procedures.
Research use only
This material is supplied strictly as a laboratory research chemical. It is not a drug, supplement, cosmetic, food or medical device, and it is not manufactured, labelled or sold for human or animal use of any kind.
Vial Drop Labs does not provide, and cannot provide, dosing, administration, preparation-for-use, therapeutic or clinical guidance. Published information is limited to chemical identity, laboratory handling and analytical documentation.
Research catalog access
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