Amino Science Labs sells research peptides exclusively to qualified researchers and laboratories for in vitro and laboratory use. Please confirm before continuing.
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Research Peptide
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Research
This listing supplies Semax as a pre-dissolved aqueous solution in a metered spray bottle, formatted for in-vitro and preclinical laboratory work rather than as a lyophilized powder. Semax is a synthetic heptapeptide with the sequence Met-Glu-His-Phe-Pro-Gly-Pro. Structurally it is related to the ACTH(4-10) fragment (Met-Glu-His-Phe-Arg-Trp-Gly) region, which was modified and shortened, with a C-terminal Pro-Gly-Pro tripeptide extension appended to the His-Phe-Pro core. That terminal Pro-Gly-Pro is the defining design feature: the proline residues were introduced specifically to slow enzymatic cleavage, giving the molecule notably greater resistance to peptidase degradation than the parent ACTH fragment. Because the peptide is derived from a corticotropin fragment but lacks the residues associated with the hormone's classic endocrine activity, laboratories treat it as a distinct short-chain research peptide rather than as an ACTH analog in the hormonal sense.
Supplying the material as a spray solution rather than a dry powder changes how it is characterized and handled on the bench. The peptide is already in solution at a defined nominal concentration, so the working parameters that matter are solution homogeneity, fill volume, delivered-volume reproducibility per actuation from the pump mechanism, and the stability of the dissolved peptide over the container's in-use life. Everything described below concerns the research substance and its solution format only: its documented study history, its analytical fingerprint, and standard laboratory handling of an aqueous peptide preparation. None of it describes, recommends, or implies any outcome, dosing, or administration in humans or animals.
Published investigation of Semax is predominantly rodent-model and in-vitro. A recurring theme in the literature is its use as a probe compound in central-nervous-system research: rodent studies and cell-culture work have examined its association with neurotrophic-factor expression, including brain-derived neurotrophic factor (BDNF) and its receptor TrkB, and transcriptional responses in cultured neuronal and glial systems. Other reported experimental lines include measurements of the peptide's rapid metabolism into shorter fragments (notably the Pro-Gly-Pro terminal fragment, itself studied as a distinct species) and characterization of its distribution in animal models following intranasal delivery in those experimental protocols. These are descriptions of what has been studied in controlled research settings, not statements of health effects.
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. Research on this peptide remains preliminary and ongoing, and nothing here is medical advice.
Each research lot is characterized before release so that the material on the Certificate of Analysis (COA) matches the sequence, mass, and stated concentration expected for the heptapeptide. Identity and purity are established on the peptide using orthogonal analytical methods, which separates purity (how much of the peptide content is the target sequence) from identity (confirmation that the target is the correct molecule) and from concentration (how much peptide is present per unit volume of solution).
The lot-specific COA is the definitive analytical record for the material received. Because purity, mass confirmation, and measured concentration can vary slightly between synthesis and formulation batches, researchers should reference the COA tied to the lot number in hand rather than generic specifications when documenting experimental inputs. Retaining the COA alongside experimental records supports reproducibility and traceability.
Because this material ships already in solution rather than as a freeze-dried solid, it does not require reconstitution, but a dissolved short peptide is generally less stable than its lyophilized counterpart. Standard laboratory practice is to keep the sealed container cold and protected from light and heat, to minimize headspace exposure and temperature cycling that can promote methionine oxidation, and to treat the in-use solution as having a limited, empirically confirmed working life. These are material-handling notes for laboratory use only and do not imply any human or animal use; refer to the storage table on this page for temperature and stability windows.
It is supplied as a pre-dissolved aqueous solution in a metered spray bottle at a defined nominal concentration, rather than as a lyophilized powder. For laboratory purposes this means no reconstitution step is needed, and the relevant working parameters are the stated concentration, fill volume, and the stability of the dissolved peptide over the container's in-use life. It is intended strictly for in-vitro and preclinical research handling by qualified researchers.
Semax is a synthetic heptapeptide, Met-Glu-His-Phe-Pro-Gly-Pro. It is based on a modified fragment of the ACTH(4-10) region with a C-terminal Pro-Gly-Pro tripeptide extension. That terminal Pro-Gly-Pro was added to slow enzymatic degradation, giving the molecule greater peptidase resistance than the parent ACTH fragment while lacking the residues tied to the hormone's classic endocrine activity.
Purity is measured on the peptide by reversed-phase HPLC and reported as a percentage of total peak area, while identity is confirmed by mass spectrometry (ESI-MS or MALDI-TOF) against the theoretical mass of the heptapeptide. Because the material is a solution, the COA also documents the nominal concentration, fill volume, and appearance. The lot-specific COA is the authoritative record for the exact material received.
The sequence begins with methionine, a residue that is prone to oxidation. Analytical characterization by RP-HPLC is designed to resolve the target peak from oxidized and truncated species, and handling practices that limit heat, light, and headspace exposure help preserve the reduced form. Reviewing the lot-matched chromatogram lets researchers confirm the material's oxidation state before use in an assay.
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.
Published work is predominantly in-vitro and rodent-model, spanning neurotrophic-factor expression such as BDNF and its TrkB receptor, transcriptional and immediate-early-gene responses in neuronal and glial cultures, and pharmacokinetic and metabolism studies tracking fragments such as the terminal Pro-Gly-Pro peptide. This research is preliminary and ongoing, describes laboratory systems only, and does not establish any human or animal outcome or benefit.
No. Despite the spray container format, this material is supplied strictly for in-vitro and laboratory research use by qualified researchers. It is not a drug, supplement, or food, is not intended for human or animal administration or any diagnostic or therapeutic purpose, and nothing on this page constitutes medical advice.
