Biotech Compounds
Humanin
Research Compound

Humanin

Humanin is a 24-amino acid mitochondrial-derived peptide (MDP) encoded within the mitochondrial 16S rRNA region. It is studied for its cytoprotective and anti-apoptotic signaling activity, particularly its interaction with pro-apoptotic Bcl-2 family proteins.

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10mg
SKU: HU10
Batch: 202607-01-HU
$129.99
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Est. Arrival: 09/16/2026
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For Research Use Only. This product is intended for laboratory and scientific research purposes only. It is not a drug or dietary supplement and is not for human or veterinary consumption. Not intended to diagnose, treat, cure, or prevent any disease.
99%+ Purity
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Categories:
HormonalInhibitoryTherapeutic
Tags:
cytoprotectionanti-apoptoticmitochondrial signalingmitochondrial-derived peptideneuroprotectionBax inhibitioncellular stress resistanceoxidative stress modulationmetabolic signalinginsulin sensitivitySTAT3 signalingcardioprotectionlongevityanti-inflammatorycell survival

Product Details

Humanin (HN) was the first identified member of the mitochondrial-derived peptide (MDP) family, a class of small bioactive peptides encoded within the mitochondrial genome. Comprising 24 amino acids, Humanin functions as a signaling peptide with characterized cytoprotective properties across multiple cell types.


Its principal described mechanism is anti-apoptotic: Humanin binds and antagonizes pro-apoptotic Bcl-2 family members including Bax, Bid, and BimEL, suppressing mitochondrial-mediated apoptosis. It additionally signals through cell-surface receptor complexes (including the formyl peptide receptor–like 1 and the gp130/CNTFR/WSX-1 trimeric receptor), activating downstream STAT3 and other pro-survival pathways. Humanin has been examined in the context of neuronal viability, metabolic and insulin-related signaling, oxidative-stress modulation, and cardiomyocyte protection, and is of interest in the broader study of mitochondrial signaling and cellular stress resistance.


Disclaimer: This product is intended for laboratory and in-vitro use only. It is not for human consumption, ingestion, or any form of in-vivo administration in humans or animals. Not a drug, food, or dietary supplement. Handling should be performed only by qualified personnel.

Frequently Asked Questions About Humanin

Answers summarize published research and are provided for laboratory research purposes only.

Humanin is a 24-amino acid mitochondrial-derived peptide, the first member of that family to be identified. It is encoded within the 16S rRNA region of the mitochondrial genome rather than in the nucleus. Research studies have examined Humanin as a cytoprotective signaling peptide in models of neuronal survival, oxidative stress, metabolic signaling, and cardiac cell protection. Biotech Compounds supplies Humanin as a lyophilized powder for laboratory research.
The principal mechanism described for Humanin is suppression of mitochondrial-mediated apoptosis. In vitro studies have shown that Humanin binds pro-apoptotic Bcl-2 family proteins including Bax, Bid, and BimEL and prevents them from triggering the mitochondrial death pathway. Researchers have also reported that Humanin signals through cell-surface receptors, including formyl peptide receptor-like 1 and a trimeric gp130, CNTFR, and WSX-1 complex, which activates STAT3 and other pro-survival pathways in cell culture.
Mitochondrial-derived peptides are small bioactive peptides encoded by short open reading frames inside mitochondrial DNA. Humanin was the first one discovered, and MOTS-c and the SHLP peptides were identified later. Research studies have shown that these peptides act as signaling molecules that travel from mitochondria to the rest of the cell and to other tissues. Humanin is studied as a model for how mitochondria communicate stress and survival signals.
The primary research area for Humanin is cytoprotection, especially neuronal viability. Humanin was originally identified in a screen for factors that protect neurons in cell culture. In research studies, Humanin has been reported to reduce neuronal cell death under oxidative and toxic challenge in vitro, and in animal models researchers have examined its activity in brain tissue exposed to stress. This neuroprotection literature remains the largest body of Humanin research.
Humanin has been examined in several secondary research areas. In animal models, researchers have reported that Humanin influences insulin sensitivity and glucose metabolism. Published research suggests that Humanin protects cardiomyocytes in models of ischemic injury and modulates markers of oxidative stress. Researchers have also studied circulating Humanin levels in relation to aging and longevity, and in vitro studies have examined its effect on inflammatory signaling in several cell types.
Humanin research is mostly preclinical. The mechanism of Humanin has been characterized in cell culture and in vitro binding studies, and its activity has been examined in rodent models of neuronal stress, cardiac injury, and metabolic function. Humanin remains an investigational research peptide with no completed clinical program. Much published work has used potent analogs of Humanin, so researchers should note which form a given study used when reading the literature.
Humanin and MOTS-c are both mitochondrial-derived peptides but they differ in origin, size, and focus. Humanin is 24 amino acids and is encoded in the 16S rRNA region, while MOTS-c is 16 amino acids and is encoded in the 12S rRNA region. Research studies have focused Humanin on anti-apoptotic and neuroprotective signaling, whereas researchers have examined MOTS-c mainly as a metabolic regulator acting through AMPK in muscle and fat models.
Humanin and SS-31 both appear in mitochondrial research but work differently. Humanin is a naturally encoded 24-amino acid peptide that research studies have shown blocks pro-apoptotic Bcl-2 family proteins and signals through STAT3. SS-31 is a synthetic four-amino acid peptide that researchers have reported binds cardiolipin in the inner mitochondrial membrane to support electron transport. Humanin is chosen for apoptosis and survival signaling studies and SS-31 for membrane and bioenergetics studies.
Humanin is supplied as a lyophilized powder and is reconstituted with bacteriostatic water or sterile water. The diluent is added slowly down the inside wall of the vial and the vial is swirled gently until the Humanin powder dissolves. The vial should never be shaken. Humanin contains two cysteine residues, so care should be taken to avoid prolonged air exposure of the solution that could encourage oxidation.
Lyophilized Humanin should be stored frozen at minus 20 C and protected from light and moisture. After reconstitution, Humanin should be kept refrigerated at 2 to 8 C, protected from light, and used within the timeframe set by the research protocol. Repeated freeze and thaw cycles should be avoided. Research studies have reported that native Humanin has a short half-life in circulation, which is one reason stabilized analogs were developed for animal work.
Humanin has a molecular weight of about 2687.3 g/mol and a molecular formula of C119H204N34O32S2. It is a 24-amino acid peptide. Biotech Compounds supplies Humanin as a lyophilized powder with a purity of 99 percent or higher, confirmed by third-party testing. The Certificate of Analysis for each lot of Humanin is available on the product page so researchers can verify identity and purity before ordering.
No. Humanin is sold strictly as a research material for laboratory and in vitro research by qualified researchers and research organizations. Purchasers must be 21 years of age or older. Humanin from Biotech Compounds is not a drug, a food, or a dietary supplement, and it is not for human or animal consumption.
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