AmericanPeptide
Catalog/Humanin

Humanin

Also known as HN · MT-RNR2 peptide

A 24-amino-acid mitochondrial-derived peptide with cytoprotective, anti-apoptotic activity — a companion to MOTS-c on the mitochondrial-signaling frontier.

Research refreshed

Overview

Humanin was the first mitochondrial-derived peptide discovered — a 24-amino-acid peptide encoded not in the nuclear genome but within the mitochondrial 16S ribosomal RNA gene. It is cytoprotective and anti-apoptotic: it was originally identified for protecting neurons against Alzheimer’s-related toxicity, and it has since been tied to metabolic regulation and longevity, with higher levels associated with healthy aging.

Background

Humanin rewrote a small piece of the rulebook when it was found in 2001: a bioactive peptide encoded inside the mitochondrial genome, in the 16S ribosomal RNA region, rather than by nuclear DNA. It was discovered in the search for factors that protect neurons in Alzheimer’s disease — hence the name — and it turned out to be a broadly cytoprotective, anti-apoptotic signal that helps cells survive stress.

It is now recognized as the founding member of the mitochondrial-derived peptides (MDPs), the same family as MOTS-c catalogued just above, and part of the larger idea that mitochondria actively signal to the rest of the body. Beyond neuroprotection, humanin has been linked to insulin sensitivity, cardiovascular protection, and longevity — circulating levels decline with age and tend to be higher in long-lived individuals. It is a research compound and is not FDA-approved.

Mechanism

Cytoprotective, anti-apoptotic signaling — binds and antagonizes the pro-apoptotic protein BAX and signals through a cell-surface receptor complex (CNTFR / WSX-1 / gp130); also interacts with IGFBP-3.

Key research findings

  • First mitochondrial-derived peptide — encoded within the mitochondrial 16S rRNA gene (MT-RNR2); discovered in 2001 in Alzheimer’s research.
  • Cytoprotective / anti-apoptotic — antagonizes the pro-apoptotic protein BAX and signals via a CNTFR / WSX-1 / gp130 receptor complex.
  • Longevity association — circulating levels decline with age and are higher in some long-lived individuals; studied in aging biology.
  • Metabolic effects — linked to improved insulin sensitivity and cardiovascular protection in preclinical work.
  • Companion to MOTS-c — both are mitochondrial-derived signaling peptides; not FDA-approved.

How Humanin is made

Behind every vial of Humanin is the same exacting pipeline every research peptide runs — but the chemistry plays out differently for this molecule. Here is how Humanin, specifically, is brought into being.

  1. On paper first

    On paper, Humanin is C119H204N34O32S2 — about 2,687.2 daltons of precisely arranged atoms. Before a single bond is made, the target sequence, salt form, and purity threshold are written down as the contract the finished material must meet.

  2. Built residue by residue

    Assembling Humanin means roughly 24 coupling cycles on the synthesizer — one protected residue added at a time, which is also 24 chances for an incomplete coupling to seed a deletion impurity.

  3. Purity is won here

    The crude mixture — Humanin plus its deletions and side products — is then separated on preparative HPLC, and where the cut is taken decides the difference between a genuinely pure peptide and a barely-passable one. Humanin carries 1 cysteine, whose thiol is oxidation-sensitive and can form disulfide links — reactive chemistry that purification has to control rather than ignore. It also contains oxidation-prone methionine or tryptophan residues, another family of impurities the chromatography has to resolve away.

  4. Proven, then protected

    A real batch of Humanin proves itself: identity confirmed by mass spectrometry against its ~2,687.2 Da, purity read directly off an analytical HPLC trace, water and counterion content measured. That batch-specific certificate of analysis is the only honest way to know what is actually in a vial of Humanin — and a short, cold, accountable chain of custody is how that purity survives the trip to your bench.

Walk the full synthesis pipeline

Handling, storage & why purity is hard

Humanin is a 24-residue mitochondrial-derived peptide with a hydrophobic, aggregation-prone core and both a methionine and a cysteine that are oxidation-sensitive. It is made by solid-phase synthesis, where the length, the difficult hydrophobic stretch, and protecting Met / Cys from oxidation make clean assembly and purification the demanding part.

Demanding synthesis

Don't judge a vial by its cake. A fluffy, good-looking lyophilized powder reflects bulking agents and freeze-drying parameters — not purity. Insist on a batch-specific certificate of analysis.

How peptides are made — the full pipeline

Research areas

  • Aging biology
  • Neuroprotection
  • Metabolic regulation
  • Cytoprotection

Research-area guides

Latest research

Recent clinical trials and publications mentioning Humanin, pulled automatically from ClinicalTrials.gov and PubMed and refreshed daily. Listings are unfiltered search results, not curated endorsements.

Frequently asked questions

What is Humanin?+

Humanin is a 24-amino-acid mitochondrial-derived peptide with cytoprotective, anti-apoptotic activity, first discovered for protecting neurons in Alzheimer’s research.

What does "mitochondrial-derived" mean?+

Unlike most peptides, humanin is encoded within the mitochondrial genome (the 16S rRNA region), not by nuclear DNA — it was the first such peptide identified.

How does it relate to MOTS-c?+

Both are mitochondrial-derived peptides (MDPs). Humanin is the cytoprotective, anti-apoptotic member; MOTS-c is studied more for metabolism and AMPK activation.

Is Humanin approved?+

No — it is a research compound, not FDA-approved. This page is a research and educational reference.

Related peptides

Peptide Agent

Ask the Agent about Humanin

Dosing protocols, mechanism, comparisons, and the latest trials — citation-backed answers grounded in PubMed, PubChem, and ClinicalTrials.gov.