Humanin is a mitochondria-encoded micro-peptide generated from a short open reading frame (sORF) within mitochondrial ribosomal RNA. Unlike canonical nuclear-encoded peptides, humanin is synthesized without post-translational processing and represents a distinct class of mitochondria-derived signaling molecules investigated in cellular stress-response and apoptosis-regulation research.

Homologous humanin sequences have been identified across multiple mammalian species, enabling comparative studies in cellular and animal model systems. Preclinical investigations commonly focus on humanin’s interaction with mitochondrial apoptosis regulators, oxidative stress pathways, and intracellular survival signaling networks under defined experimental conditions.

Source: PubChem

Sequence: Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala
Molecular Formula: C119H204N34O32S2
Molecular Weight: 2687.3 g/mol
PubChem SID: 16131438
CAS Number: 330936-69-1
Synonyms: Formyl humanin, HNGF6A protein

Humanin is utilized as a molecular tool in laboratory research to investigate mitochondrial stress signaling, apoptosis initiation thresholds, and micro-peptide–protein interaction networks. Experimental systems include neuronal, vascular, retinal, musculoskeletal, and endocrine-derived cell cultures, as well as in-vivo animal models.

Research applications frequently examine how humanin modulates intracellular signaling cascades associated with oxidative stress, mitochondrial membrane integrity, and programmed cell death regulation in controlled preclinical environments.

Humanin has been shown in preclinical models to interact with components of the intrinsic mitochondrial apoptosis pathway. Mechanistic studies describe binding interactions with Bcl-2 family proteins, including Bax, Bid, and tBid, resulting in altered mitochondrial outer membrane permeabilization dynamics and downstream caspase activation profiles.

Additional pathway analyses indicate interfaces between humanin signaling and insulin-like growth factor (IGF) axis components, AMP-activated protein kinase (AMPK), and reactive oxygen species–responsive signaling nodes. These interactions are examined to characterize cross-talk between mitochondrial peptides and nuclear-encoded metabolic and stress-response pathways.

Preclinical investigations in rodent and cell-based models have evaluated humanin-associated modulation of apoptosis markers, oxidative stress indicators, and mitochondrial function under experimentally induced stress conditions. These studies are commonly used to map tissue-specific expression patterns, signaling responsiveness, and mitochondrial resilience metrics.

Additional experimental literature explores humanin-related signaling in vascular endothelium, retinal pigment epithelial cells, chondrocytes, osteoclast precursor populations, and neural circuits, with emphasis on molecular endpoints rather than translational outcomes.

Humanin is supplied as a synthetic research peptide intended for controlled laboratory use. Identity and composition may be verified through sequence confirmation, mass spectrometry, and chromatographic purity analysis in accordance with standard peptide characterization workflows.

The above literature was researched, edited and organized by Dr. Logan, M.D. Dr. Logan holds a doctorate degree from Case Western Reserve University School of Medicine and a B.S. in molecular biology.

Pinchas Cohen, MD, is the dean of the USC Leonard Davis School of Gerontology, executive director of the Ethel Percy Andrus Gerontology Center, and holder of the William and Sylvia Kugel Dean’s Chair in Gerontology. He is an expert in the study of mitochondrial peptides and their possible therapeutic benefits for diabetes, Alzheimer’s, and other diseases related to aging. Cohen’s current research focus is on the emerging science of mitochondria-derived peptides, which he discovered. These peptides include humanin, a 24-amino acid peptide encoded from the mt-16S-rRNA. It is a novel, centrally acting insulin sensitizer and metaboloprotective factor representing a new therapeutic and diagnostic target in diabetes and related disease. Other mitochondrial peptides of interest include MOTS-c, a second peptide encoded from a small ORF in the 12S region of the mitochondrial chromosome that has potent anti-diabetes and anti-obesity effect and acts as an exercise-mimetic, and SHLP2, a peptide encoded from the light strand of the mt-16S-rRNA region whose levels correlate with prostate cancer.

Dr. Alfonso Eirin has received his MD in 2004 from the University of the Republic in Montevideo Uruguay. Currently, he is working as a senior research fellow in the Division of Nephrology and Hypertension at Mayo Clinic, Rochester, MN. Dr. Eirin’s research is focused on understanding the pathogenesis of renal and cardiac injury due to atherosclerotic renovascular disease (ARVD) and the developing of treatment strategies to improve blood pressure and renal outcomes after revascularization in these patients.

Dr. Pinchas Cohen and Dr. Alfonso Eirin are being referenced as leading scientists involved in the research and development of Humanin. In no way are these doctors/scientists endorsing or advocating the purchase, sale, or use of this product for any reason. There is no affiliation or relationship, implied or otherwise, between Peptide Sciences and these doctors. The purpose of citing the doctors is to acknowledge, recognize, and credit the exhaustive research and development efforts conducted by the scientists studying this peptide. Dr. Pinchas Cohen is listed in [9] and Dr. Alfonso Eirin is listed in [10] under the referenced citations.

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The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body.  These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease.  Bodily introduction of any kind into humans or animals is strictly forbidden by law.

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