Longevity 49 min read January 27, 2026

Humanin Research

Humanin is a mitochondrial-derived peptide with broad cytoprotective actions, protecting brain, heart, and pancreatic cells from stress and aging.

Humanin Research

Summary

Humanin is a small protein produced by the mitochondria, originally discovered in 2001 for its ability to protect brain cells from damage related to Alzheimer’s disease. Since then, it has been recognized as part of a larger group of mitochondrial-derived peptides that help cells survive under stress. Research has shown that Humanin plays a protective role in many tissues, including the brain, heart, blood vessels, and pancreas. It helps regulate metabolism, reduce inflammation, prevent cell death, and improve resilience to aging-related damage. Humanin levels decline with age, and lower levels are often seen in people with chronic diseases, while higher levels are found in long-lived individuals. Because of its broad protective effects and connection to longevity, Humanin is now being studied as a potential therapeutic tool to improve healthspan and reduce age-related decline.

Humanin Overview

Humanin (HN) is a 24–amino acid peptide encoded in the mitochondrial 16S ribosomal RNA gene (MT-RNR2) and was first identified in 2001 as a neuroprotective “rescue factor” that blocks neuronal death caused by Alzheimer’s disease (AD)-related insults. Subsequent studies revealed HN as a paradigm for mitochondrial-derived peptides with pleiotropic cytoprotective actions. HN exists in both intracellular and secreted forms, engaging multiple signal transduction pathways to promote cell survival. It binds pro-apoptotic proteins (e.g. Bax, Bid) to halt mitochondrial cell-death cascades and interacts with specific cell-surface receptors to activate pro-survival signaling (JAK/STAT3, PI3K/AKT, ERK1/2). In diverse in vitro and animal models, HN and more potent analogues (such as S14G-humanin) protect neurons, pancreatic β-cells, cardiomyocytes, endothelial cells and other cell types from oxidative stress, metabolic insults, and apoptotic injury. Moreover, HN improves physiological function in models of AD, atherosclerosis, diabetes, and aging, including extension of lifespan in C. elegans. These multifaceted benefits position HN as a compelling subject in basic and translational science. This review critically examines the current evidence on HN’s molecular mechanisms, preclinical efficacy, and unresolved questions, highlighting HN’s emerging role as a mitochondrial signal peptide with broad cytoprotective potential.

Molecular Origin & Structure

Humanin is encoded by a 75-base pair open reading frame within the mitochondrial 16S rRNA gene (MT-RNR2), making it a rare example of a “gene within a gene” in the mitochondrial genome. First identified by Hashimoto et al. during a screen for neuroprotective cDNAs in Alzheimer’s brain tissue, the resulting peptide is 24 amino acids long (MAPRGFSCLLLLTSEIDLPVKRRA), though mitochondrial translation may start with formyl- methionine. Humanin shares 92–100% sequence homology with 13 nuclear MTRNR2L loci, thought to be nuclear mitochondrial pseudogenes (Numts). Orthologs exist across species—for instance, “rattin” in rats is a 38-residue variant with a C-terminal extension—suggesting strong evolutionary conservation.

Sequence Variants and Analogs:

Structure–function analyses have identified critical residues in the Pro³–Ser¹⁴ core domain. Mutations at Ser⁷, Cys⁸, Leu⁹, Leu¹², Thr¹³, Ser¹⁴, or Pro¹⁹ abolish bioactivity. Replacing Ser¹⁴ with glycine produces HNG, a potent analogue that shows >1000-fold higher cytoprotective activity, likely due to greater conformational flexibility and target binding affinity. Other notable analogues include HNGF6A (S14G with Phe⁶→Ala), which enhances insulin secretion without binding IGFBP-3, and Colivelin, a chimeric peptide merging a truncated HNG with a neurotrophic factor segment that shows femtomolar efficacy in memory models. Recent work has yielded stabilized analogs—like cyclic D-Ser14 humanin (cHND14) and “HUJ” analogs—with enhanced resistance to proteolysis and potent protection in models of ischemia and excitotoxicity.

Secretion and Localization:

Despite lacking a classical signal sequence, HN is secreted via a non-canonical mechanism. Yamagishi et al. identified two hydrophobic motifs (Leu⁹–Leu¹¹ and Pro¹⁹–Val²⁰) essential for secretion; mutating Leu10 abolished extracellular release without affecting intracellular levels. These motifs may serve as an internal secretion signal, facilitating export through unconventional pathways such as direct membrane translocation or vesicular trafficking. HN appears to localize first to the mitochondrial matrix or inner membrane before being released into the cytosol and then extracellular space. Dimerization, also governed by key residues like Ser7 and Leu9, correlates with enhanced activity, potentially by enabling high-avidity receptor interactions.

Stability and Expression Dynamics:

Intracellular HN is regulated by the ubiquitin–proteasome system. TRIM11, an E3 ubiquitin ligase, binds HN and promotes its degradation; its absence elevates HN levels, while proteasome inhibitors block turnover. MT-RNR2 mRNA is highly expressed in metabolically active tissues—heart, skeletal muscle, kidney, liver, testis—and HN peptide is detectable in these tissues as well as in plasma and cerebrospinal fluid. HN levels decline with age in rodents and humans, a trend thought to reflect diminishing cellular resilience with aging. These patterns suggest a regulated system in which HN acts as a mitochondria-derived signal peptide, coordinating stress responses across cellular compartments.

Preclinical Evidence — In Vivo (Animal Models)

Neurodegeneration Models: HN’s neuroprotective effects have been demonstrated across a variety of rodent neurodegeneration models. In triple-transgenic Alzheimer’s mice (mutant APP, PSEN1, Tau), intranasal HNG over 3 months reduced Aβ plaque burden, lowered glial inflammation, and improved maze performance. APP/PS1 mice treated peripherally with HNG also showed diminished brain amyloid load and cognitive recovery, indicating CNS penetration and functional rescue. In acute models, HNG blocked memory loss induced by Aβ_25–35 peptide and preserved performance in scopolamine-induced cholinergic impairment. HN has also countered non-amyloid insults: in rats, it protected neurons from toxicity, and in polyglutamine neurodegeneration models, HN reduced protein aggregates and ASK1-driven neuronal death. However, effects are not universal; in one Huntington’s disease model, HN showed no benefit, suggesting disease-specific variables modulate its action.

In ischemic stroke models, intracerebroventricular HNG post-MCAO reduced infarct size by ~50%, decreased apoptosis, and improved neurological scores. Mechanistically, HNG suppressed ERK and PARP activation while boosting AKT, with PI3K inhibition abolishing its effect. Combined HNG and Necrostatin-1 (a necroptosis inhibitor) yielded synergistic benefits—~80% infarct reduction and greater functional recovery versus monotherapy. In vitro oxygen-glucose deprivation studies confirmed enhanced dual-pathway protection. In hemorrhagic stroke, systemic HNG reduces brain edema and neuronal death while facilitating mitochondrial transfer from astrocytes to neurons—a possible endogenous repair response.

HN also shows promise in Parkinson’s disease models. In MPTP-exposed mice, peripheral HN treatment preserved motor function, dopaminergic neurons, and reduced oxidative stress in the striatum. Though early, these data support HN’s broader neuroprotective potential via anti-apoptotic and mitochondrial-preserving mechanisms.

Metabolic Regulation: HN modulates metabolism in rodent models, particularly insulin sensitivity and glucose homeostasis. Central HN delivery enhanced insulin action during hyper insulinemic–euglycemic clamps, primarily through suppressed hepatic glucose output and increased muscle uptake. This effect depended on hypothalamic STAT3 activation. Peripherally, intravenous HNGF6A improved glucose disposal and reduced gluconeogenesis in diabetic rats. Chronically, mid-life HNG administration improved glucose tolerance, reduced inflammatory cytokines, and lowered adiposity. HN also supports pancreatic β-cell integrity: in streptozotocin-treated mice, HNG preserved islet architecture and delayed hyperglycemia onset. Transgenic mice overexpressing HN were more insulin sensitive and resistant to diet-induced insulin resistance. Long-lived Ames dwarf mice exhibit high HN levels, while short-lived GH-transgenic mice have low levels, paralleling favorable metabolic traits (low insulin, high sensitivity). Collectively, these models position HN as a metabolic regulator with anti-diabetic potential.

Cardioprotection and Vasoprotection:

HN exerts protective effects in the cardiovascular system. In myocardial ischemia/reperfusion models, HNG reduced infarct size by over 40%, improved ejection fraction and cardiac output, and diminished cardiomyocyte apoptosis. HN expression increased in ischemic tissue, and human coronary plaques showed HN immunoreactivity—hinting at an adaptive stress response. In ApoE⁻/⁻ mice, HNGF6A treatment preserved endothelial function, halved aortic plaque area, and reduced oxidative stress markers in lesions. It also protected against microvascular damage in the kidneys, suggesting end-organ benefits. Corroborating this, patients with endothelial dysfunction have lower circulating HN and reduced flow-mediated dilation. HN also limited vascular remodeling: in rat carotid injury, it reduced smooth muscle proliferation and inflammatory signaling. Altogether, these findings underscore HN’s role in vascular homeostasis and ischemic resilience.

Lifespan and Healthspan:

HN is linked to longevity in several models. In C. elegans, HN expression extended lifespan in a DAF-16-dependent manner and conferred stress resistance. In mammals, HNG- treated mice maintained superior glucose metabolism, lower cytokine levels, and increased late- life activity. Offspring of human centenarians’ exhibit ~30% higher plasma HN, while patients with age-related diseases (e.g., AD, MELAS) show reduced levels. Notably, naked mole rats—remarkably long-lived rodents—maintain youthful HN levels into old age, unlike typical rodents. While elevated HN has been detected in some cancers (see later section), in aging models, HN consistently delays decline without observed trade-offs. These findings suggest that persistent HN expression enhances cellular resilience, supporting its candidacy as a longevity- associated factor in geroscience research.

Comparative & Synergistic Biology

Humanin (HN) is the first discovered member of a now-expanding class of mitochondrial- derived peptides (MDPs), short peptides encoded within mitochondrial rRNA loci that exert cytoprotective effects. Among the most studied MDPs alongside HN are the small humanin-like peptides (SHLPs 1–6) and MOTS-c, each with distinct but sometimes overlapping roles in stress adaptation.

The SHLPs were identified from ORFs within the 16S rRNA region that also encodes HN. SHLP2 and SHLP3, for instance, show pro-survival, anti-apoptotic functions in vitro, with SHLP3 improving glucose tolerance and reducing adiposity in vivo. Conversely, SHLP6 exhibits pro-apoptotic effects, possibly serving as a counter-regulatory factor that induces mitophagy or inhibits unchecked proliferation. These findings suggest SHLPs form a network with both synergistic and antagonistic actions, modulating cell fate under stress.

MOTS-c, a 16-amino acid peptide encoded in the mitochondrial 12S rRNA, complements HN’s actions. It translocates to the nucleus during metabolic stress and activates genes involved in homeostasis via AMPK. Like HN, MOTS-c enhances insulin sensitivity and protects against diet-induced obesity in mice. Notably, both peptides decline with age and are elevated in long-lived models, implying that MDPs collectively sustain stress resistance across tissues throughout youth, waning with aging. Given these overlaps, combined interventions involving HN are being explored. A clear example is HN (HNG) co-administered with the necroptosis inhibitor Necrostatin-1 in stroke models, where simultaneous targeting of apoptotic and necrotic pathways resulted in superior neuroprotection. Similar additive effects have been reported with anti-oxidants or neurotrophic peptides. Colivelin, a hybrid of HN and a fragment of activity-dependent neurotrophic factor (ADNF), outperformed HN alone in memory rescue and ischemia protection models. Another study combining HN with a peptide derived from an integrin-binding domain (HV) showed enhanced neural adhesion and survival compared to either alone.

The interplay between HN and other MDPs can also be regulatory. VSTM2L, a secreted protein, binds and antagonizes both HN and MOTS-c, suggesting coordinated regulation of their availability. Their expression appears to be temporally aligned—MOTS-c rises early in response to metabolic stress to modulate cellular energetics, while HN follows to limit apoptotic damage. Exercise exemplifies this relationship: endurance training elevates both peptides in muscle, correlating with improved insulin sensitivity and reduced apoptosis. In mouse models, combining exercise with MDP analogs enhanced metabolic health more than either intervention alone.

Such synergy has spurred interest in pairing HN analogs with caloric restriction mimetics or IGF-1 modulators, given HN’s influence on the insulin/IGF axis. Additionally, HN analogs are being evaluated as adjuvants in cancer therapy to reduce chemotherapy toxicity. In preclinical studies, HNG preserved bone and germ cell integrity during cisplatin treatment without shielding tumor tissue. However, this protective potential also raises concerns: HN could, under some conditions, aid tumor survival, making dosage and context critical variables. Some reports suggest HN may sensitize tumors to TNF-α, while others associate elevated HN with malignancy.

Overall, HN functions not in isolation but as part of a broader signaling ensemble. Its interactions with MDPs and exogenous agents position it as a keystone in adaptive responses to cellular stress. However, the presence of antagonists like SHLP6 and VSTM2L underscores the importance of understanding the timing, tissue-specificity, and balance among mitochondrial peptides. Future studies should continue to map this network, define synergy and redundancy, and determine how HN-based strategies might best be integrated into multifactorial approaches to enhance stress resilience and prevent degenerative decline.

Conclusion

Humanin (HN) exemplifies the power of mitochondria-encoded microproteins in regulating cell fate. Initially discovered for its neuroprotective effects in Alzheimer’s models, HN is now recognized as a broadly cytoprotective, pleiotropic peptide. Its dual mechanism—blocking apoptosis intracellularly and activating survival signaling extracellularly—allows it to counteract key drivers of aging such as oxidative stress, protein aggregation, and metabolic dysfunction. Across diverse preclinical models, HN and its analogues have repeatedly preserved tissue viability, from neurons and cardiomyocytes to pancreatic β-cells. Its integration into a broader network of mitochondrial-derived peptides (MDPs) underscores its role as part of an intrinsic cellular defense system.

While promising, HN biology is not without complexities. Its context-specific effects, potential interactions in cancer models, and unresolved mechanistic questions reflect the nuanced reality of mitochondrial signaling. Nevertheless, the weight of evidence favors HN as a net positive modulator of cellular resilience. As a therapeutic candidate, HN stands out for its multi-targeted effects an advantage in treating complex, multifactorial diseases like Alzheimer’s, myocardial infarction, and metabolic syndrome. Rather than acting on a single receptor or pathway, HN shifts cells into a survival-promoting state across multiple axes, offering a systems-level approach to protection.

The challenge ahead is delivery. Native HN is short-lived, and optimizing stability, potency, and tissue targeting will be critical. Potent analogues, or gene therapy approaches that locally enhance HN expression, represent the most viable paths forward. If successful, HN- based interventions could redefine treatment strategies for age-related diseases and potentially extend healthspan.

More broadly, HN’s discovery represents a shift in how we view the mitochondrial genome, from a static catalog of respiratory genes to a dynamic source of regulatory peptides. Humanin helped open the door to this new field, revealing that mitochondria are not just energy producers but central players in stress signaling and intercellular communication. The path forward will require advanced tools, careful study design, and rigorous validation. But the foundation is already strong.

In short, Humanin is no longer just an Alzheimer’s curiosity, it is now a leading candidate in geroscience, with far-reaching implications for how we understand and intervene in the aging process. As research continues, HN may become one of the first mitochondrial peptides to transition from molecular discovery to practical intervention in age-related disease. Its future lies not only in what it can do alone, but how it can be integrated into the broader orchestration of cellular longevity mechanisms.

References

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[Terashita K., Hashimoto Y., Niikura T., et al. Two serine residues distinctly regulate the rescue function of Humanin, an inhibiting factor of Alzheimer’s disease-related neurotoxicity: functional potentiation by isomerization and dimerization. J Neurochem. 2003;85(6):1521–1534.](https://doi.org/10.1046/j.1471-4159.2003.01797.x "Two serine residues distinctly regulate the rescue function of Humanin, an inhibiting factor of Alzheimer's disease-related neurotoxicity: functional potentiation by isomerization and dimerization")

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[Chiba T., Yamada M., Hashimoto Y., et al. Development of a femtomolar-acting Humanin derivative named colivelin by attaching activity-dependent neurotrophic factor to its N-terminus: characterization of colivelin-mediated neuroprotection against Alzheimer’s disease-relevant insults in vitro and in vivo. J Neurosci. 2005;25(52):10252–10261.](https://doi.org/10.1523/JNEUROSCI.3348-05.2005 "Development of a Femtomolar-Acting Humanin Derivative Named Colivelin by Attaching Activity-Dependent Neurotrophic Factor to Its N Terminus: Characterization of Colivelin-Mediated Neuroprotection against Alzheimer's Disease-Relevant Insults In Vitro and In Vivo")

[Gilon C., Gitlin-Domagalska A., Lazarovici P., et al. Novel Humanin analogs confer neuroprotection in vitro and in vivo by mutations that stabilize the peptide in an active conformation. Neuropharmacology. 2020;168:108013.](https://doi.org/10.1016/j.peptides.2020.170399 "Novel humanin analogs confer neuroprotection and myoprotection to neuronal and myoblast cell cultures exposed to ischemia-like and doxorubicin-induced cell death insults")

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[Muzumdar R.H., Huffman D.M., Atzmon G., et al. Humanin: a novel central regulator of peripheral insulin action. PLoS ONE. 2009;4(7):e6334.](https://doi.org/10.1371/journal.pone.0006334 "Humanin: A Novel Central Regulator of Peripheral Insulin Action")

[Ying G., Iribarren P., Zhou Y., et al. Humanin, a newly identified neuroprotective factor, uses the G-protein-coupled formylpeptide receptor-like-1 (FPRL1) as a functional receptor. J Exp Med. 2004;199(5):621–627.](https://doi.org/10.1016/10.4049/jimmunol.172.11.7078 "Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor")

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TO THE FULL EXTENT NOT PRECLUDED BY APPLICABLE LAW THEIR MEDICAL ADVISORS, SUPPLIERS, CONSULTANTS, DIRECTORS AND EMPLOYEES DISCLAIM AND EXCLUDE ALL WARRANTIES WITH RESPECT TO ALL CONTENT, EXPRESS, IMPLIED OR STATUTORY. THIS DISCLAIMER INCLUDES, BUT IS NOT LIMITED TO, ANY AND ALL WARRANTIES OR MERCHANTABILITY, FITNESS FOR A PARTICULAR PURPOSE, AND NON-INFRINGEMENT. DOES NOT WARRANT THE CONTENT TO BE ACCURATE, COMPLETE OR CURRENT. DOES NOT WARRANT THAT THIS WEB SITE WILL OPERATE WITHOUT ERROR, THAT DEFECTS WILL BE CORRECTED OR THAT THIS WEB SITE OR THE WEB SITE SERVER MAKING IT AVAILABLE ARE FREE OF VIRUSES OR OTHER HARMFUL COMPONENTS. PRICE AND AVAILABILITY CONTENT, AS WELL AS OTHER CONTENT CONTAINED IN THIS WEB SITE OR ACCESSIBLE THEREFROM, IS SUBJECT TO CHANGE WITHOUT NOTICE.

YOU ACKNOWLEDGE AND AGREE THAT DOES NOT ENDORSE THE CONTENT OF ANY SITE ACCESSED VIA LINKS OR OTHER MEANS FROM THIS WEB SITE AND IT IS NOT RESPONSIBLE OR LIABLE FOR SUCH CONTENT EVEN THOUGH IT MAY BE UNLAWFUL, HARASSING, LIBELOUS, PRIVACY INVADING, ABUSIVE, THREATENING, HARMFUL, OBSCENE, OR OTHERWISE OBJECTIONABLE, OR THAT IT INFRINGES OR MAY INFRINGE THE INTELLECTUAL PROPERTY OR OTHER RIGHTS OF ANOTHER PERSON.

THIS WEB SITE INCLUDES CONTENT PROVIDED BY THIRD PARTIES AND YOU, OUR CUSTOMER. IS A DISTRIBUTOR OF SUCH CONTENT AND NOT ITS PUBLISHER. EDITORIAL CONTROL OF SUCH CONTENT IS THE SAME AS THAT OF A PUBLIC LIBRARY OR NEWSSTAND. THIRD PARTY SUPPLIERS MAY EXPRESS CERTAIN OPINIONS OR PROVIDE CERTAIN INFORMATION AND OFFERS. MAKES NO WARRANTIES AS TO THE COMPLETENESS, ACCURACY, TIMELINESS, OR RELIABILITY OF INFORMATION OR OFFERS SUPPLIED BY THIRD PARTIES. DOES NOT GUARANTEE OR WARRANT THE PERFORMANCE OF ANY THIRD PARTY, INCLUDING ANY SUCH THIRD PARTY’S CONFORMANCE TO ANY LAW, RULE, REGULATION OR POLICY.

DOES NOT WARRANT THAT INFORMATION, SERVICES, AND PRODUCTS CONTAINED IN THIS WEB SITE WILL SATISFY YOUR REQUIREMENTS OR THAT THEY ARE ERROR OR DEFECT-FREE. BEFORE USING ANY PRODUCT YOU SHOULD CONFIRM ANY INFORMATION OF IMPORTANCE TO YOU ON THE PRODUCT PACKAGING. YOU ASSUME RESPONSIBILITY FOR THE ACCURACY, APPROPRIATENESS AND LEGALITY OF ANY INFORMATION YOU SUPPLY

AS PARTIAL CONSIDERATION FOR YOUR ACCESS TO THIS WEB SITE AND USE OF ITS CONTENT, YOU AGREE THAT IS NOT LIABLE TO YOU IN ANY MANNER WHATSOEVER FOR DECISIONS YOU MAY MAKE OR YOUR ACTIONS OR NON-ACTIONS IN RELIANCE UPON THE CONTENT. YOU ALSO AGREE THAT THE AGGREGATE LIABILITY OF ARISING FROM OR RELATED TO YOUR USE AND ACCESS REGARDLESS OF THE FORM OF ACTION OR CLAIM (FOR EXAMPLE, CONTRACT, WARRANTY, TORT, NEGLIGENCE, STRICT LIABILITY, PROFESSIONAL MALPRACTICE, FRAUD, OR OTHER BASES FOR CLAIMS), IS LIMITED TO THE PURCHASE PRICE OF ANY ITEMS YOU PURCHASED FROM IN THE APPLICABLE TRANSACTION. SHALL NOT IN ANY CASE BE LIABLE FOR ANY DIRECT, INDIRECT, SPECIAL, INCIDENTAL, CONSEQUENTIAL, OR PUNITIVE DAMAGES EVEN IF HAS BEEN ADVISED OF THE POSSIBILITY OF SUCH DAMAGES. THIS IS A COMPREHENSIVE LIMITATION OF LIABILITY THAT APPLIES TO ALL LOSES AND DAMAGES OF ANY KIND. IF YOU ARE DISSATISFIED WITH THIS WEB SITE OR ITS CONTENT (INCLUDING TERMS OF USE), YOUR SOLE EXCLUSIVE REMEDY IS TO DISCONTINUE USING THIS WEB SITE. BECAUSE SOME JURISDICTIONS DO NOT ALLOW THE EXCLUSION OR LIMITATION OF LIABILITY FOR INCIDENTAL OR CONSEQUENTIAL DAMAGES, SUCH LIMITATION MAY NOT BE APPLICABLE TO YOU.

Your Agreement to Abide by All Applicable Laws

By using this Web Site you agree to comply with any and all local, state, or federal laws, statutes, and regulations that relate in any manner to the use of this Web Site and the associated services or products contained thereon.

Relationship between and Users.

and users of our Site are independent contractors, and no agency, partnership, employment or other relationship is created or is intended to be created by the use of our Web Site.

Governing Law and Jurisdiction

This Web Site (excluding linked sites, if any) is administered and controlled by and its affiliates, subsidiaries, officers, directors, employees or agents from its offices in the accordance with the laws of Nevis. You agree that this Terms and Conditions of Use Agreement and this Web Site will be governed by and construed in accordance Nevis law without giving effect to any principles of conflicts of laws. You access this Web Site and/or associated services of at your own risk, and remain responsible for complying with the laws of the jurisdiction within which you are located.

Prices; Payment Terms; Interest

The prices for the products and services on this Web Site are quoted, for convenience, in United States dollars and shall be as set forth in this Web Site as at the time of acceptance of an order by Prices for Products shall be subject to change without any further notice. Credit terms are within sole discretion, and unless otherwise specified in invoice, payment must be received by prior to acceptance of an order.

Consequences

reserves the right to suspend or terminate your account if you violate the Terms of Use Agreement. If your violation causes harm to others, you agree to indemnify and hold harmless from and against any and all loss, damage, or expense. If any dispute arises between us regarding this Agreement or your use of this Web Site, it shall be resolved through good faith negotiations between the parties.

Entire Agreement

These Terms and Conditions and any terms incorporated or referred to herein constitute the entire agreement between and you relating to your use of this Web Site and the subject matter hereof, and supersede any prior understandings or agreements (whether electronic, oral or written) regarding the subject matter, and may not be amended or modified except in writing, or by making such amendments or modifications in accordance with this Terms and Conditions of Use Agreement.

Severability

If any part of this Terms and Conditions of Use Agreement is deemed or determined to be unenforceable, then such part shall be eliminated or limited to the minimum extent necessary. The remainder of this Terms and Conditions of Use Agreement, including any revised portion, shall remain and be in full force and effect. This Terms and Conditions of Use Agreement are the entire agreement between us governing your use of this Web Site.

Headings

The headings contained in this Terms and Conditions of Use Agreement and the Privacy Policy are for reference only.

Force Majeure

shall not be liable for any delay or failure in performance caused by circumstances beyond its reasonable control, including, without limitation, delays due to backorders of requested products, mail delays, customs delays or lost shipments. shall not be responsible to notify the Customer in the event of such delays. The Customer shall be solely responsible to make other arrangements to purchase alternative products and any costs incurred in connection with such purchases.

Thank you again for visiting the Web Site.

Complete Agreement

Except as expressly provided in a particular "legal notice" on this Site, these Terms and Conditions constitute the entire agreement between you and this Site with respect to the use of this Site, and Content. By clicking “I agree” when placing your order, you agree with ALL OF OUR TERMS and CONDITIONS as stated above as well as our Shipping and refunds Policy.

Thank you for your cooperation.

Terms and Conditions of Purchase

Your Use of Our Web Site

Use of Information

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