What is Humanin 10MG

Humanin 10MG is a mitochondrial-derived peptide (MDP) studied in research for its profound cytoprotective, anti-apoptotic, and metabolic regulatory effects. It is intended exclusively for research use.

Regarding its chemical identity, Humanin has a molecular formula of C119H204N34O32S2 and a molecular weight of 2687.2 g/mol. Its reported canonical sequence is Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala. A confirmed CAS number is not available in open primary reference sources and is therefore omitted.

Its synonyms include Humanin.

Product for research use.

Mechanism of action of Humanin

Humanin acts by binding to specific cellular receptors (such as the CNTFR/WSX-1/gp130 complex) and interacting intracellularly with apoptosis-inducing proteins like Bax. By sequestering Bax, Humanin prevents mitochondrial dysfunction and halts programmed cell death under severe stress.

Pharmacokinetics and pharmacodynamics of Humanin

As an endogenous peptide, its circulating half-life is relatively short, but its intracellular effects on mitochondrial stability are long-lasting. Modified, highly stable analogues (like HNG) are often used in research to prolong its action.

Scientific evidence on Humanin

The available evidence on Humanin is preliminary and largely inconclusive, and should be interpreted with caution. The literature describes it as having been investigated for multiple indications in preclinical models.

Investigated extensively in models of Alzheimer’s disease, atherosclerosis, and myocardial infarction. Evidence shows it protects neurons from beta-amyloid toxicity and improves insulin sensitivity by acting directly on the hypothalamus and peripheral tissues.

Humanin applications in research

Ideal for (research context):
– In vitro and preclinical studies of its specific receptor pathways.
– Investigation of tissue repair, cell proliferation, and functional restoration in laboratory models.
– Comparative work with related peptides.

Not applicable for:
– clinical, diagnostic or therapeutic use.
– Any administration to humans or animals outside of an authorized research protocol.

Product for research use.

Humanin protocols in preclinical studies

The literature consulted does not include numerical doses from studies that can be cited for Humanin, so no trial schemes or quantities are specified.

The presentations of this product (10MG) refer only to the amount of lyophilized peptide per vial (or volume for liquids) and do not constitute a dosage recommendation. The design of any protocol, including concentrations and working volumes, is the responsibility of the researcher, based on their experimental objectives and the relevant primary literature.

Information provided exclusively for research purposes.

Reconstitution and manipulation of Humanin

As a general guideline for laboratory handling, lyophilized peptides such as Humanin are usually reconstituted with bacteriostatic water (sterile water with approximately 0.9% benzyl alcohol).

Add the solvent slowly down the side of the vial, letting it run over the lyophilized powder; avoid injecting the stream directly onto the powder.
Do not shake: gently rotate the vial until completely dissolved.
Adjust the solvent volume according to the desired working concentration, considering the 10MG contents of the vial.

These guidelines are for general technique and do not replace the internal procedures of each laboratory.

Humanin Stability and Storage

As a standard laboratory handling procedure for peptides:

Freeze-dried (unreconstituted): This is the most stable form. It is best preserved by freezing and protecting it from moisture and light for long-term storage.
Reconstituted: once in solution, the peptide is less stable and must be kept refrigerated, being used within a short period; for extended storage, freezing in aliquots is usually preferred.
Avoid repeated freeze-thaw cycles, as they can degrade the peptide.

Given that the molecule is characterized by rapid enzymatic degradation in biological media, careful cold chain management is especially relevant.

Documented Humanin security profile

The documented safety information in open sources for Humanin is limited and should be interpreted with caution, also considering that it is research material and not for clinical use.

Because it acts primarily as a cellular protector and metabolic normalizer, theoretical risks of toxicity are low. However, its anti-apoptotic nature theoretically necessitates caution regarding the survival of pre-malignant cells, though unverified in humans.

Formal contraindications and adverse event rates are not available in the consulted literature, so no figures are reported.

Humanin in a comparative context

Humanin belongs to the unique class of mitochondrial-derived peptides, distinguishing it from nuclear-encoded peptides. Unlike general antioxidants, Humanin acts specifically at the receptor and genetic level to preserve mitochondrial function under critical stress.

History and development of Humanin

Discovered in 2001 in the occipital lobe of patients with Alzheimer’s disease. It was identified as a survival factor transcribed from the 16S ribosomal RNA region of the mitochondrial genome, revolutionizing the understanding of mitochondrial signaling.