Humanin

Humanin (HN) – Mitochondrial-Derived Peptide for Cellular Protection & Longevity Research

24-Amino-Acid Research Peptide for Mitochondrial Signaling, Neuroprotection, Apoptosis Regulation, Oxidative Stress & Metabolic Biology

Humanin (HN) is a naturally occurring, mitochondria-associated peptide that has attracted significant scientific interest because of its involvement in cellular stress responses, mitochondrial communication and cell survival signaling.

Humanin belongs to the growing family of mitochondrial-derived peptides (MDPs), a group of small signaling molecules associated with mitochondrial genetic sequences.

The commonly studied Humanin peptide contains 24 amino acid residues and is associated with a short open reading frame within the mitochondrial 16S ribosomal RNA gene region, MT-RNR2.

Humanin was first identified during research investigating cellular protection against insults associated with Alzheimer's disease.

Subsequent experimental studies have explored its potential roles in:

• Mitochondrial function and cellular stress responses

• Neuronal survival and neurodegeneration models

• Apoptosis-associated signaling

• Oxidative stress regulation

• Insulin signaling and glucose metabolism

• Cardiovascular and ischemia–reperfusion models

• Inflammation-associated pathways

• Cellular aging and stress resistance

• Kidney and retinal cell research

• Mitochondrial-to-nuclear communication

Although many preclinical findings are promising, Humanin has not been established as a clinically effective treatment for Alzheimer's disease, diabetes, cardiovascular disease or biological aging.

Its potential therapeutic applications remain investigational.

ICAME Pharmacy Humanin is intended strictly for laboratory research and development purposes. Not for human or veterinary use.

What Is Humanin?

Humanin is a small peptide associated with mitochondrial genetic information.

Mitochondria are cellular organelles best known for their role in energy metabolism. However, research has demonstrated that mitochondria also participate in intracellular communication, stress signaling and the regulation of cell survival.

Humanin is one of the first identified members of the mitochondrial-derived peptide family.

Unlike conventional mitochondrial proteins involved directly in oxidative phosphorylation, Humanin has been investigated primarily as a signaling peptide.

Experimental studies suggest that Humanin can influence cellular responses through both extracellular receptor interactions and intracellular protein associations.

Its biological activity has been studied in cultured cells and animal models, with additional observational research examining endogenous Humanin levels in humans.

The evidence supporting Humanin as an experimental signaling molecule is substantially stronger than the evidence supporting any proposed clinical treatment.

Humanin Molecular Structure

Humanin is commonly described as a 24-amino-acid peptide.

Amino Acid Sequence

H-MAPRGFSCLLLLTSEIDLPVKRRA-OH

The 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

Molecular Characteristics

Compound Name: Humanin

Abbreviation: HN

Classification: Mitochondrial-Derived Peptide

Commonly Studied Length: 24 Amino Acids

Amino Acid Sequence: MAPRGFSCLLLLTSEIDLPVKRRA

Approximate Molecular Weight: 2,687.3 Da

Genetic Association: MT-RNR2 / Mitochondrial 16S rRNA Region

Primary Research Fields: Mitochondrial Biology / Neurobiology / Cellular Stress Signaling

Reported Signaling Partners: FPRL1/FPR2 and CNTFR/WSX-1/gp130 receptor systems

Reported Intracellular Interaction Partners: BAX, BAK, tBID and IGFBP-3

Important Structural Considerations

Humanin has been described in both 24-amino-acid and 21-amino-acid forms in the scientific literature.

This distinction relates to differences in the genetic and translational context.

Researchers should not assume that all products labeled Humanin contain the same peptide sequence.

The molecular identity, terminal modifications, salt form and purity of a research preparation should be verified using batch-specific analytical documentation.

Discovery and Scientific Background

Humanin was discovered in 2001 during investigations into molecular mechanisms associated with Alzheimer's disease.

Researchers led by Yuichi Hashimoto identified a short peptide capable of reducing neuronal cell death caused by certain Alzheimer's disease-related experimental insults.

Early studies examined neuronal damage associated with amyloid precursor protein mutations and amyloid-beta exposure.

The discovery was important because it suggested that a small peptide associated with mitochondrial genetic information could influence cellular survival.

Subsequent research investigated Humanin's molecular origin, receptor interactions and possible functions in tissues beyond the nervous system.

These investigations helped establish the broader concept of mitochondrial-derived peptides as potential signaling molecules.

Humanin remains an important research model for understanding the relationship between mitochondrial biology and cellular stress responses.

Humanin and Mitochondrial-Derived Peptides

Mitochondrial-derived peptides are small molecules associated with open reading frames within mitochondrial genetic sequences.

Humanin is among the earliest and most extensively studied members of this group.

Other mitochondrial-derived peptides include:

MOTS-c

Small Humanin-Like Peptides (SHLPs)

These compounds differ in sequence, molecular targets and experimental biological activity.

Humanin is particularly associated with research involving cell survival and apoptosis.

MOTS-c has attracted interest in metabolic stress signaling and cellular energy regulation.

The SHLP family includes additional short peptides investigated in mitochondrial and cellular physiology.

Findings involving one mitochondrial-derived peptide should not automatically be attributed to another.

How Does Humanin Work?

Humanin has been investigated through several molecular mechanisms rather than one universally established signaling pathway.

Its reported activities can be grouped into two broad categories:

1. Extracellular Receptor-Mediated Signaling

Humanin can interact with cell-surface receptor systems involved in intracellular signaling.

These include the CNTFR/WSX-1/gp130 complex and certain formyl peptide receptors.

2. Intracellular Protein Interactions

Humanin has also been investigated for interactions with proteins associated with programmed cell death and stress responses.

These include members of the BCL-2-associated apoptosis machinery.

Simplified Research Framework

Humanin (HN)

↓

Cell-Surface Receptor Signaling

CNTFR / WSX-1 / gp130

↓

JAK–STAT3-Associated Signaling

and

FPRL1 / FPR2-Associated Signaling

↓

ERK1/2 and Other Cellular Responses

Alongside:

Intracellular Humanin Interactions

↓

Apoptosis-Associated Protein Regulation

↓

Experimental Changes in Cell Survival and Stress Responses

These mechanisms have been characterized in selected experimental systems.

They should not be interpreted as proof that Humanin protects every cell type or provides clinical protection against disease.

Humanin and the CNTFR/WSX-1/gp130 Receptor Complex

One of the most frequently discussed Humanin signaling mechanisms involves a receptor complex containing:

CNTFR — Ciliary Neurotrophic Factor Receptor

WSX-1 — IL-27 Receptor Subunit Alpha

gp130 — Glycoprotein 130

Research has shown that these receptor components contribute to Humanin-associated signaling in neuronal experimental systems.

Activation of this pathway has been associated with STAT3 signaling.

STAT3 Research

STAT3 is a transcription factor involved in several cellular processes, including survival signaling, inflammatory responses and gene regulation.

Humanin-associated STAT3 activation has been investigated in neuronal cell protection models.

However, STAT3 has context-dependent functions, and its activation cannot automatically be described as universally beneficial.

Humanin and Formyl Peptide Receptor Research

Humanin has also been investigated in relation to formyl peptide receptors, including FPRL1, commonly designated FPR2/ALX.

These receptors belong to the G protein-coupled receptor family.

Experimental studies have examined Humanin-associated effects involving:

• Receptor activation

• Intracellular calcium signaling

• ERK1/2 phosphorylation

• Chemotactic responses

• Neuronal signaling

• Inflammation-associated pathways

Formyl peptide receptors interact with several endogenous and exogenous ligands.

Therefore, Humanin-associated receptor activity must be interpreted in the context of ligand specificity and experimental conditions.

Humanin and Apoptosis Regulation

Apoptosis is a regulated form of programmed cell death.

It is essential for normal development and tissue maintenance, but inappropriate activation can contribute to tissue injury and disease.

Humanin has been studied for its interactions with apoptosis-associated proteins.

Reported intracellular partners include:

BAX

BAK

tBID

These proteins participate in mitochondrial apoptosis pathways.

Experimental studies suggest that Humanin can interfere with selected protein interactions associated with apoptotic signaling.

Simplified Apoptosis Research Model

Cellular Stress

↓

Pro-Apoptotic Signaling

↓

Mitochondrial Membrane Changes

↓

Downstream Cell Death Pathways

Humanin has been investigated as a potential modulator of certain steps in this process.

However, inhibiting apoptosis is not always desirable.

Programmed cell death is important for removing damaged or potentially malignant cells.

This context is particularly relevant when evaluating long-term safety.

Humanin and Mitochondrial Function

Mitochondria participate in energy production, metabolic regulation and cellular signaling.

They also contribute to the regulation of oxidative stress and programmed cell death.

Humanin has been investigated in models involving mitochondrial dysfunction and cellular injury.

Relevant research endpoints include:

Mitochondrial membrane integrity

Reactive oxygen species production

Cellular energy metabolism

Mitochondrial stress responses

Apoptosis-associated signaling

Mitochondrial-to-nuclear communication

These findings have generated interest in Humanin as a mitochondrial signaling peptide.

However, it would be inaccurate to describe Humanin as a proven method of restoring mitochondrial function in humans.

Humanin and Oxidative Stress Research

Oxidative stress occurs when the production of reactive species exceeds the capacity of cellular defense systems.

Reactive oxygen species (ROS) participate in normal signaling, but excessive or poorly regulated ROS can contribute to cellular damage.

Humanin has been investigated in experimental models involving oxidative injury.

Research topics include:

Reactive oxygen species

Mitochondrial oxidative stress

Glutathione-associated defenses

Cellular antioxidant responses

Stress-induced apoptosis

Mitochondrial membrane integrity

Several preclinical studies have reported protective effects under selected experimental conditions.

These findings do not establish Humanin as a clinically validated antioxidant treatment.

Humanin and Neuroprotection Research

Humanin was initially identified through research involving neuronal survival.

This remains one of its most important scientific applications.

Researchers have investigated Humanin in models of:

• Amyloid-beta-associated neuronal injury

• Familial Alzheimer's disease-related cellular stress

• Oxidative neuronal damage

• Apoptosis-associated neurotoxicity

• Mitochondrial dysfunction

• Neuroinflammatory signaling

Some cell and animal studies have reported reduced neuronal injury or changes in survival-associated pathways.

However, Humanin has not been shown in adequate clinical trials to prevent or treat neurodegenerative disease in humans.

Humanin and Alzheimer's Disease Research

Alzheimer's disease is a complex neurodegenerative disorder associated with multiple pathological processes.

These include amyloid-beta accumulation, tau pathology, synaptic dysfunction, neuroinflammation and neuronal loss.

Early Humanin research examined its ability to reduce cell death caused by Alzheimer's disease-related experimental insults.

These findings helped establish Humanin as a candidate for further investigation.

Research Areas

Amyloid-beta-associated toxicity

Neuronal apoptosis

Mitochondrial stress

Cell survival signaling

Synaptic biology

Neuroinflammatory pathways

Experimental neurodegeneration

Evidence Limitations

Cell survival in an experimental model is not equivalent to preventing cognitive decline in humans.

Humanin has not been established as an effective treatment for Alzheimer's disease, dementia or memory impairment.

Humanin and Amyloid-Beta Research

Amyloid-beta (Aβ) is a peptide associated with Alzheimer's disease pathology.

Certain forms of amyloid-beta can produce cellular stress in experimental models.

Humanin has been investigated for its ability to influence neuronal responses to amyloid-beta-associated insults.

Research endpoints include:

Cell viability

Apoptosis markers

Receptor signaling

Oxidative stress

Mitochondrial function

Neuronal survival

Early studies demonstrated that Humanin could reduce certain amyloid-beta-associated toxic effects in cultured neuronal cells.

However, these results cannot be generalized to all forms or stages of Alzheimer's disease.

Humanin and Cognitive Function Research

Cognitive function depends on coordinated activity across neural networks.

Researchers have examined Humanin and Humanin analogues in animal models involving learning and memory.

Some experimental studies have reported changes in cognitive performance or neuronal injury markers.

However, the evidence is predominantly preclinical.

Humanin has not been established as a safe or effective cognitive enhancer in healthy humans.

Claims involving improved memory, intelligence or concentration require controlled human clinical evidence.

Humanin and Neuroinflammation

Neuroinflammation involves immune-associated signaling within the nervous system.

Microglia and other cellular populations contribute to inflammatory responses in the brain.

Humanin has been investigated in experimental systems examining inflammatory mediators and cellular stress.

Relevant research areas include:

Microglial signaling

Inflammatory cytokines

Oxidative stress

Neuronal survival

Mitochondrial dysfunction

Stress-responsive signaling pathways

However, the effects of Humanin may differ according to cell type and inflammatory conditions.

It should not be described as a proven treatment for neuroinflammatory disorders.

Humanin and Metabolic Research

Humanin has attracted scientific interest beyond neurobiology.

Experimental studies have investigated its relationship with insulin signaling and glucose regulation.

Reported research areas include:

Insulin sensitivity

Glucose metabolism

Pancreatic beta-cell function

Metabolic stress

Mitochondrial signaling

Energy homeostasis

Some preclinical studies have reported favorable changes in selected metabolic endpoints.

However, Humanin has not been established as an approved treatment for diabetes, insulin resistance or obesity.

Humanin and Insulin Signaling

Insulin is a central regulator of glucose metabolism.

Its biological effects involve receptor-mediated pathways influencing glucose transport, nutrient storage and cellular metabolism.

Humanin has been investigated in experimental models of insulin resistance.

Research has explored whether Humanin-associated signaling influences insulin responsiveness under certain conditions.

Potential research endpoints include:

Insulin receptor-associated signaling

Glucose uptake

Metabolic stress

Mitochondrial function

Glucose homeostasis

These observations do not establish Humanin as a clinically effective insulin-sensitizing medication.

Humanin and Pancreatic Beta-Cell Research

Pancreatic beta cells produce and secrete insulin.

Their function depends on nutrient sensing, mitochondrial metabolism and regulated secretory mechanisms.

Humanin has been investigated in experimental models involving beta-cell stress.

Research topics include:

Glucose-stimulated insulin secretion

Beta-cell viability

Oxidative stress

Apoptosis-associated pathways

Mitochondrial function

Metabolic regulation

Certain preclinical findings suggest Humanin-associated effects on beta-cell survival or function.

However, these results do not establish that Humanin can prevent or reverse diabetes in humans.

Humanin and Cardiovascular Research

Cardiovascular tissues are highly dependent on mitochondrial function.

Cardiac cells require substantial energy to maintain contractile activity.

Humanin has been investigated in experimental cardiovascular models involving:

Ischemia–reperfusion injury

Oxidative stress

Cardiomyocyte survival

Mitochondrial dysfunction

Inflammatory signaling

Vascular biology

Some preclinical studies have reported protective effects under specific experimental conditions.

However, Humanin has not been established as a treatment for heart failure, coronary artery disease or myocardial infarction.

Humanin and Ischemia–Reperfusion Injury

Ischemia occurs when tissue receives insufficient blood flow.

Reperfusion restores circulation but can also trigger additional cellular stress.

Ischemia–reperfusion injury may involve oxidative stress, inflammation and mitochondrial dysfunction.

Humanin has been investigated in experimental models of ischemia-associated injury.

Researchers have examined:

Cell viability

Mitochondrial function

Oxidative stress markers

Apoptosis-associated proteins

Inflammatory signaling

Tissue injury endpoints

The results remain model-dependent and do not establish clinical therapeutic efficacy.

Humanin and Kidney Research

The kidneys are metabolically active organs containing cells with substantial mitochondrial requirements.

Humanin has been investigated in experimental models involving renal cellular stress.

Potential research areas include:

Renal oxidative injury

Tubular cell survival

Mitochondrial dysfunction

Apoptosis-associated signaling

Ischemia–reperfusion models

Inflammatory pathways

Findings from cell cultures and animal studies cannot be assumed to predict improved kidney function in humans.

Humanin is not an established treatment for chronic kidney disease or acute kidney injury.

Humanin and Retinal Cell Research

Retinal cells are exposed to significant metabolic and oxidative demands.

Humanin has been investigated in retinal pigment epithelial cells and other ocular research models.

Relevant research areas include:

Retinal oxidative stress

Mitochondrial dysfunction

Cellular survival

Endoplasmic reticulum stress

Inflammatory signaling

Retinal degeneration models

Certain preclinical investigations have reported protective responses.

However, Humanin has not been established as a treatment for age-related macular degeneration or other retinal diseases.

Humanin and Endoplasmic Reticulum Stress

The endoplasmic reticulum (ER) is involved in protein synthesis, folding and cellular homeostasis.

Disruption of ER function can trigger the unfolded protein response.

Prolonged or severe ER stress may contribute to apoptosis.

Humanin has been investigated in experimental systems involving ER stress.

Research endpoints include:

Protein-folding stress

Cell survival

Mitochondrial interactions

Oxidative injury

Stress-response signaling

Apoptosis-associated pathways

These findings contribute to understanding cellular stress adaptation but do not establish clinical efficacy.

Humanin and Inflammation Research

Inflammation is a complex biological response involving immune cells, signaling proteins and tissue-specific processes.

Humanin has been investigated in models examining inflammatory responses.

Research areas include:

Cytokine-associated signaling

Cellular stress

Mitochondrial communication

Immune cell responses

Oxidative stress

Inflammation-associated tissue injury

Because inflammatory signaling can be protective or harmful depending on context, changes in inflammatory markers should not automatically be described as beneficial.

Humanin and Aging Research

Humanin has attracted considerable interest in aging biology.

Mitochondrial dysfunction, cellular stress and altered metabolic signaling are frequently investigated in relation to aging.

Humanin has been studied in models examining these processes.

Research topics include:

Cellular stress resistance

Mitochondrial function

Metabolic regulation

Age-associated signaling

Cell survival pathways

Longevity-related biomarkers

Some observational studies have examined associations between endogenous Humanin levels and age or health-related characteristics.

However, observational associations cannot establish that increasing Humanin improves health or extends lifespan.

Humanin and Longevity Research

Longevity research investigates biological factors associated with lifespan and healthspan.

Humanin has been explored because of its potential roles in mitochondrial signaling and stress resistance.

Experimental studies have examined Humanin-related pathways in cellular and animal systems.

These findings provide a basis for further research.

However:

Humanin has not been demonstrated to extend human lifespan.

Humanin has not been established as a treatment for normal aging.

Humanin has not been shown to reverse biological age in controlled clinical trials.

Any claims of human longevity benefits remain speculative.

Humanin and Cellular Senescence

Cellular senescence refers to a state in which cells undergo a relatively stable cell-cycle arrest accompanied by changes in signaling and metabolism.

Senescence can participate in normal biological processes as well as age-associated tissue dysfunction.

Humanin has been discussed in research examining cellular stress and aging-related pathways.

Potential research areas include:

Mitochondrial signaling

Oxidative stress

Cellular survival

Stress-associated gene expression

Age-related metabolic changes

However, Humanin is not an established senolytic agent.

It should not be described as a compound proven to eliminate senescent cells.

Humanin and Cancer Biology

Humanin's association with cell survival and apoptosis makes cancer biology an important area of scientific caution.

Apoptosis is one mechanism by which organisms remove damaged or abnormal cells.

A peptide that modifies apoptosis-associated pathways may have different effects depending on the cellular context.

Research questions include:

Cell survival signaling

Apoptosis regulation

Mitochondrial protein interactions

Growth-associated signaling

Cancer cell stress responses

The long-term consequences of manipulating Humanin pathways are not adequately understood.

Humanin should not be marketed as an anticancer treatment, nor should its anti-apoptotic properties automatically be assumed safe in the presence of malignancy.

Humanin and IGFBP-3 Research

Insulin-like growth factor-binding protein 3 (IGFBP-3) participates in the regulation of IGF-associated signaling and has additional cellular functions.

Humanin has been investigated for interactions with IGFBP-3.

These interactions are relevant to research involving:

Cell survival

Stress signaling

IGF-associated regulation

Protein–protein interactions

Apoptosis-associated mechanisms

However, the presence of an interaction does not establish a universal biological effect across all tissues.

Humanin Analogues and S14G-Humanin

Researchers have developed Humanin analogues to investigate structure–activity relationships.

One frequently studied analogue is S14G-Humanin, also called HNG.

In this analogue, serine at position 14 is replaced with glycine.

This substitution has been associated with substantially increased activity in certain experimental assays.

Humanin vs. S14G-Humanin

Results from S14G-Humanin studies should not automatically be attributed to unmodified Humanin.

The two compounds are structurally distinct.

Humanin vs. MOTS-c

Humanin and MOTS-c are both mitochondrial-derived peptides.

However, their molecular sequences and research histories differ.

The compounds should not be considered interchangeable.

Humanin vs. SS-31 (Elamipretide)

Humanin and SS-31 are different research peptides.

Humanin is a naturally occurring mitochondria-associated signaling peptide.

SS-31, also known as elamipretide, is a synthetic tetrapeptide developed for research involving mitochondrial membrane interactions.

The clinical and regulatory status of elamipretide must be evaluated separately from Humanin.

Humanin vs. GHK-Cu

Humanin and GHK-Cu are structurally and biologically different compounds.

Humanin is a 24-amino-acid mitochondria-associated peptide.

GHK-Cu is a copper-binding tripeptide complex.

Humanin has been investigated primarily in cellular stress, neurobiology and metabolic signaling.

GHK-Cu has been investigated in extracellular matrix biology, skin research and tissue remodeling.

Their mechanisms and research applications should not be treated as equivalent.

Humanin and Peptide Structure–Activity Relationships

Structure–activity relationship (SAR) research investigates how changes in molecular structure influence biological function.

Humanin contains regions with different physicochemical properties.

These include:

An N-terminal region

A central hydrophobic region

A C-terminal region

Researchers have investigated how individual amino acid substitutions affect:

Cellular protection

Peptide secretion

Receptor interactions

Protein binding

Molecular stability

Experimental potency

Humanin analogues provide useful models for studying how peptide structure influences biological signaling.

Humanin and Research Methodology

Humanin research may involve several experimental approaches.

Cell Culture Models

Used to investigate cellular stress responses, apoptosis and receptor signaling.

Neuronal Models

Used to examine responses to neurodegeneration-associated insults.

Mitochondrial Function Assays

Used to investigate oxidative stress, membrane function and cellular metabolism.

Protein Interaction Studies

Used to examine associations with intracellular or membrane-associated binding partners.

Animal Models

Used to investigate systemic physiological responses under controlled experimental conditions.

Analytical Characterization

Used to verify peptide identity, purity and stability.

Experimental findings should be interpreted according to the model, compound identity and measured endpoints.

Humanin Research Evidence: What Is Established?

Humanin has a substantial preclinical research history.

However, evidence quality differs considerably across proposed applications.

Established Scientific Findings

• Humanin is associated with mitochondrial genetic sequences.

• The commonly studied peptide contains 24 amino acids.

• Humanin was identified during Alzheimer's disease-related neuroprotection research.

• Humanin can influence cellular survival in selected experimental systems.

• Multiple receptor and intracellular interaction partners have been reported.

• Humanin analogues can exhibit different experimental activity.

• Humanin has been investigated in metabolic, cardiovascular and mitochondrial research.

Important Limitations

• Humanin has no established clinical efficacy for Alzheimer's disease.

• Humanin is not a proven treatment for diabetes or cardiovascular disease.

• Humanin has not been shown to reverse aging in humans.

• Human lifespan extension has not been demonstrated.

• Long-term systemic safety is not adequately characterized.

• Experimental potency varies between Humanin and its analogues.

• Research-grade products are not equivalent to authorized medicines.

• Changes in cell survival markers do not guarantee improved clinical outcomes.

Potential Research Applications

Humanin may be relevant to appropriately controlled scientific investigations involving:

• Mitochondrial-derived peptide biology

• Mitochondrial-to-nuclear communication

• Cellular stress responses

• Apoptosis regulation

• BAX and BAK protein interactions

• tBID-associated signaling

• CNTFR/WSX-1/gp130 receptor research

• JAK–STAT3 signaling

• FPRL1/FPR2 receptor pharmacology

• ERK1/2 signaling

• Neuronal survival

• Amyloid-beta-associated cellular stress

• Neurodegeneration models

• Oxidative stress

• Endoplasmic reticulum stress

• Insulin signaling

• Glucose metabolism

• Pancreatic beta-cell biology

• Cardiovascular cellular physiology

• Ischemia–reperfusion models

• Kidney cell biology

• Retinal pigment epithelial cell research

• Inflammation-associated signaling

• Aging-associated cellular stress

• Peptide structure–activity relationships

These are scientific research applications rather than established therapeutic benefits.

Humanin Research Overview

Compound Name: Humanin

Abbreviation: HN

Classification: Mitochondrial-Derived Peptide

Commonly Studied Peptide Length: 24 Amino Acids

Sequence: MAPRGFSCLLLLTSEIDLPVKRRA

Approximate Molecular Weight: 2,687.3 Da

Genetic Association: MT-RNR2 / Mitochondrial 16S rRNA Region

Reported Receptor Systems: CNTFR/WSX-1/gp130 and FPRL1/FPR2

Reported Intracellular Partners: BAX / BAK / tBID / IGFBP-3

Main Research Fields: Mitochondrial Biology / Neurobiology / Metabolic Signaling

Related Analogue: S14G-Humanin (HNG)

Established Clinical Therapeutic Benefits: None

Intended Product Use: Laboratory Research Only

Product Information

Product Name: Humanin

Alternative Name: HN

Brand: ICAME Pharmacy

Product Category: Research Peptide

Research Classification: Mitochondrial-Derived Peptide

Research Areas: Mitochondrial Signaling / Neuroprotection / Apoptosis / Cellular Stress

Intended Use: Laboratory Research & Development Only

The exact identity and specifications of the supplied material should be confirmed through manufacturer documentation.

Relevant batch-specific information includes:

• Verified amino acid sequence

• Molecular identity

• Peptide length

• Terminal modifications

• Chemical form and counterion

• Analytical purity

• Peptide content

• Certificate of Analysis (COA)

• Batch/lot identification

• Validated storage conditions

The name Humanin should not be used interchangeably with S14G-Humanin or other modified analogues without confirming the actual molecular structure.

No claims of pharmaceutical quality, sterility, injectable suitability or clinical efficacy should be made without appropriate supporting documentation and regulatory authorization.

Important Research Use Notice

FOR RESEARCH USE ONLY (RUO)

This ICAME Pharmacy product is intended exclusively for legitimate laboratory, analytical and scientific research purposes.

Not for human or veterinary use. Not for diagnostic, therapeutic, anti-aging, cognitive enhancement, disease prevention or other clinical purposes. Not for direct administration to humans or animals.

Humanin is a biologically active peptide associated with cellular stress and survival signaling.

Although preclinical studies have reported neuroprotective, metabolic and cytoprotective effects, these findings do not establish clinical safety or efficacy.

Humanin has not been established as a treatment for Alzheimer's disease, diabetes, cardiovascular disease, mitochondrial disorders or aging-related conditions.

Long-term systemic safety remains insufficiently characterized.

Information presented on this page is intended solely for scientific and educational purposes and does not constitute medical advice, prescribing information, dosage guidance or instructions for human use.

About ICAME Pharmacy

ICAME Pharmacy provides specialized research products for professional laboratory and scientific applications.

Our portfolio focuses on compounds relevant to peptide science, mitochondrial biology, molecular signaling, experimental pharmacology and life sciences research.

We emphasize accurate product identification, responsible research use, scientific transparency and clear communication of evidence limitations.

For batch-specific analytical documentation and product inquiries, please contact ICAME Pharmacy.

Frequently Asked Questions About Humanin

What is Humanin?

Humanin is a naturally occurring mitochondria-associated peptide investigated for its involvement in cellular stress responses, cell survival and mitochondrial signaling.

How many amino acids does Humanin contain?

The commonly studied Humanin sequence contains 24 amino acids. A 21-amino-acid form is also discussed in the scientific literature.

What is the amino acid sequence of Humanin?

MAPRGFSCLLLLTSEIDLPVKRRA.

What is the molecular weight of Humanin?

The commonly studied 24-amino-acid peptide has an approximate molecular weight of 2,687.3 Da.

Is Humanin a mitochondrial-derived peptide?

Yes. Humanin is one of the earliest identified mitochondrial-derived peptides and is associated with a short open reading frame in the mitochondrial 16S rRNA gene region.

What receptors are associated with Humanin?

Reported receptor systems include the CNTFR/WSX-1/gp130 complex and formyl peptide receptors such as FPRL1/FPR2.

Does Humanin protect neurons?

Humanin has demonstrated protective effects in selected neuronal cell and animal models. Clinical neuroprotection in humans has not been established.

Can Humanin treat Alzheimer's disease?

No. Humanin has not been established as an effective treatment for Alzheimer's disease.

Is Humanin an anti-aging peptide?

Humanin is studied in aging-related biology, but it has not been shown to reverse aging or extend human lifespan.

Does Humanin improve insulin sensitivity?

Some preclinical studies have reported effects on insulin-associated signaling. Clinical efficacy for insulin resistance or diabetes has not been established.

Is Humanin the same as S14G-Humanin?

No. S14G-Humanin is a modified analogue containing a serine-to-glycine substitution at position 14.

Is Humanin the same as MOTS-c?

No. Humanin and MOTS-c are distinct mitochondrial-derived peptides with different sequences and research applications.

Is Humanin approved for human treatment?

Humanin is not an established approved therapeutic agent for the conditions discussed in this article.

Is ICAME Pharmacy Humanin intended for human use?

No. ICAME Pharmacy Humanin is intended strictly for laboratory research and development purposes.