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Research Peptide
Semax for research.
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Third-party tested
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99%+ purity
HPLC verified
7AA
HEPTAPEPTIDE
ACTH(4-7)-Pro-Gly-Pro analogue
BDNF
UPREGULATION
Brain-derived neurotrophic factor
100+
PUBLICATIONS
In neuroprotection research
2011
APPROVED IN RUSSIA
For cognitive enhancement
813Da
MOL. WEIGHT
Modified ACTH fragment
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on orders over $150
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Research
This listing supplies Semax as a 10 mg lyophilized (freeze-dried) research peptide intended strictly for in-vitro and preclinical laboratory work. Semax is a synthetic heptapeptide with the sequence Met-Glu-His-Phe-Pro-Gly-Pro, corresponding to the molecular formula C37H51N9O10S and CAS 80714-61-0. Structurally it is built on the ACTH(4-7) fragment (Met-Glu-His-Phe) extended at the C-terminus with a Pro-Gly-Pro tripeptide. That terminal Pro-Gly-Pro motif is the defining engineering feature in the research literature: the proline residues flanking the core sequence markedly increase the peptide's resistance to aminopeptidase and carboxypeptidase cleavage relative to the parent ACTH fragment, which is why Semax is frequently described as a stabilized, non-hormonal analog rather than a corticotropin mimic.
Because the sequence omits the residues responsible for the adrenocorticotropic activity of full-length ACTH, Semax is studied in laboratory settings as a peptide tool compound rather than as a hormone. The material offered here is a characterized reference peptide for controlled benchtop investigation, and all descriptions below concern the research substance itself — its documented study history, its analytical fingerprint, and standard handling of freeze-dried peptide reference material. Nothing here describes an outcome in humans or animals, and none of the information provided is medical advice.
The published literature on Semax is predominantly rodent-model and in-vitro in nature, and much of it originates from neuropeptide and melanocortin-system research groups. The summaries below describe observations in laboratory systems only; they are hypothesis-generating, remain preliminary and ongoing, and do not establish any effect in people. Reported experimental lines of inquiry include:
Research Context
These references describe experimental laboratory work only. They are not medical claims, are not evidence of safety or efficacy in humans or animals, and should not be interpreted as guidance for any use outside a controlled research environment. Observations in isolated cells or rodent models do not necessarily translate to other biological systems.
For a short peptide of this kind, identity and purity verification is central to reproducible results because truncated sequences and residual synthesis byproducts can co-occur with the target. Research-grade Semax is typically assessed by reversed-phase high-performance liquid chromatography (RP-HPLC) to quantify chromatographic purity, reported as the percentage of total peak area; the chromatogram resolves the main heptapeptide peak from process-related impurities and deletion sequences. This product is characterized at a purity of ≥98%.
Identity is confirmed by mass spectrometry (commonly ESI-MS or MALDI-TOF), where the observed molecular mass is matched against the theoretical value calculated for the C37H51N9O10S composition, verifying that the material is the intended Met-Glu-His-Phe-Pro-Gly-Pro sequence rather than a truncated or modified analog. A lot-specific Certificate of Analysis (COA) documents these analyses, along with appearance and net peptide content. Because a lyophilized peptide vial also contains counter-ion (frequently acetate) and residual water, the net peptide mass can differ from the gross fill weight; reviewing the lot-matched COA before use lets researchers calculate accurate stock concentrations and supports traceability.
The following describes conventional handling of lyophilized research peptides and is not instruction for human or animal use. As a freeze-dried powder, Semax is hygroscopic; sealed vials are typically allowed to equilibrate to room temperature before opening to minimize condensation, then reconstituted with an appropriate research-grade solvent using standard sterile laboratory technique. Aliquoting reconstituted stock into single-use portions limits the freeze-thaw cycles that can degrade peptide integrity. Detailed temperature and stability windows for lyophilized, reconstituted, and working solutions appear in the storage table elsewhere on this page, and handling should follow standard institutional chemical-safety practice.
Semax is a synthetic heptapeptide (Met-Glu-His-Phe-Pro-Gly-Pro; C37H51N9O10S; CAS 80714-61-0) based on the ACTH(4-7) fragment extended with a C-terminal Pro-Gly-Pro sequence. It ships as a 10 mg lyophilized (freeze-dried) powder in a sealed vial for the researcher to reconstitute using standard sterile laboratory technique. It is a research chemical for in-vitro and preclinical laboratory use only, not a drug or supplement, and not for human or animal consumption.
Semax corresponds to the ACTH(4-7) fragment (Met-Glu-His-Phe) with an added Pro-Gly-Pro tripeptide at the C-terminus. Because it lacks the residues responsible for full-length ACTH's adrenocorticotropic activity, it is characterized in the literature as a non-corticotropic analog. The flanking proline residues also make it markedly more resistant to peptidase cleavage than the unmodified fragment in vitro, which is why it is described as a stabilized peptide.
Published in-vitro and rodent-model work has examined Semax as a tool compound in neuropeptide and melanocortin-system research, including concentration-dependent changes in neurotrophic-factor gene and protein expression such as BDNF and NGF, and enzymatic-stability comparisons against the parent ACTH fragment. These are mechanistic, model-based observations that are preliminary and ongoing, and they do not establish any outcome in humans or animals.
Purity is measured by reversed-phase HPLC and reported as a percentage of total peak area, with this product characterized at ≥98%; the chromatogram separates the main peak from deletion sequences and process impurities. Identity is confirmed by mass spectrometry (ESI-MS or MALDI-TOF) against the theoretical mass of the C37H51N9O10S sequence. The lot-specific Certificate of Analysis records both values plus appearance and net peptide content.
This product is sold strictly for in-vitro research and laboratory use only. It is not intended for human or animal consumption, diagnostic purposes, or therapeutic application.
By purchasing this product, you confirm that you are a qualified researcher operating within an appropriate laboratory environment and will use this compound in accordance with all applicable local, state, and federal regulations.
Amino Science Labs assumes no liability for misuse of this product outside of its intended research application.
A lyophilized peptide vial contains counter-ion (often acetate) and residual water in addition to the peptide, so the net peptide mass can be lower than the gross fill weight. Reviewing the lot-matched COA for reported net peptide content and HPLC purity lets researchers prepare accurate stock concentrations, which is essential for reproducible in-vitro experiments and for documenting experimental inputs against the exact material received.
Allow the sealed vial to reach room temperature before opening to limit condensation on the hygroscopic powder, then reconstitute with a research-grade solvent using standard sterile technique and aliquot the stock to avoid repeated freeze-thaw cycles. Follow the specific temperature and time windows in the storage table on this page for lyophilized, reconstituted, and working solutions, and observe standard institutional laboratory safety practice. This material is for in-vitro research only.
