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Free U.S. shipping on orders over $150MOTS-c is a mitochondrial-derived and exercise-induced peptide whose levels decrease with age [1]. It improves insulin sensitivity, glucose metabolism, and metabolic homeostasis [2]. Animal studies suggest that, by activating AMPK, it can mitigate obesity resulting from high-fat diets, aging, and menopause [3, 2]. It also regulates age-related inflammation and various aspects of age-related physical decline, such as bone and muscle losses [1].
In pancreatic cells, MOTS-c lowers insulin secretion and increases glucagon production [4]. In mice with aberrant lipid metabolism, MOTS-c treatment significantly reduced lipid buildup in liver cells [5].
In rodents, high-fat diet-induced obesity can promote insulin resistance and fat accumulation that triggers chronic inflammation. In mice, MOTS-c administration protects against both age-related and high-fat diet-induced insulin resistance, and diet-induced obesity [6].
Hormonal changes during pregnancy can affect insulin sensitivity and cause high blood sugar, leading to gestational diabetes. In pregnant women and mouse models of gestational diabetes, MOTS-c normalized blood sugar, and enhanced insulin sensitivity and glucose tolerance. The MOTS-c treatment lowered both the birth weight-associated complications and mortality of offspring caused by gestational diabetes [7].
Low estrogen during menopause can cause weight gain and fat redistribution in favor of white fats, which increases insulin resistance and the risk of metabolic disorders. In contrast, the more mitochondria-dense brown fats burn more calories, and improve glucose and lipid metabolisms. In ovarectomized mice, MOTS-c increases brown fat activation, and reduces fat accumulation and inflammation in white adipose tissue, which contributes to the lower level of fats in serum and liver [3].
In heart failure, fluid buildup and increased pressure in the lungs can cause lung injury. MOTS-c reduced heart dysfunction and remodeling caused by heart failure and lowered inflammation while boosting antioxidant activity in the hearts of sick mice [8]. It can also prolong injured heart and lung cells’ life cycle [9, 10].
Age-related sarcopenia can reduce overall healthspan and independence, while increasing various metabolic health risks. MOTS-c suppresses myostatin and lipid infiltration that contributes to muscle atrophy, even in immobilized animals [11, 12]. Older adults with higher circulating MOTS-c have better muscle performance and lean mass, while those with lower levels experienced more sarcopenia [13]. In a mouse model of aging, MOTS-c can significantly increase physical performance by activating genes related to skeletal muscle metabolism and myoblast adaptation to metabolic stress [1].
In an in vitro model of muscle development, MOTS-c peptide helps muscle cells to form properly, affecting their integral parts such as myotubes. It supports muscle cell formation at the expense of lipid accumulation while protecting muscle cells from the breakdown effects of inflammatory cytokine IL-6 [14].
Age-related bone loss often parallels muscle loss, and various anti-sacropenic stimuli also protect bone health. Importantly, metabolic dysfunction and inflammation tend to accelerate bone loss. MOTS-c mitigates age-related bone loss by stimulating osteoblasts and suppressing osteoclasts by modulating AMPK and inflammatory responses [15]. In a mouse bone damage model, MOTS-c treatment reduced bone loss and inflammation and prevented the formation of osteoclasts [16].
Sepsis is a potentially lethal condition characterized by systemic overactive immune reactions towards an infection or noninfectious agents. MOTS-c greatly improves survival and lowers bacterial counts in MRSA-infected experimental mice. It also reduces levels of pro-inflammatory cytokines like TNF-α, IL-6, and IL-1β, while increasing the anti-inflammatory cytokine IL-10 [17].
Type 1 diabetes patients have lower endogenous MOTS-c levels than healthy controls. In a mouse model of type 1 diabetes, exogenous MOTS-c prevents pancreatic β cell destruction by shifting CD4+ T cells towards a less self-destructive phenotype, suggesting that MOTS-c may be beneficial as an autoimmune treatment [18].
Age-related inflammation and declining antioxidant capacity are key drivers of aging and related diseases. Older adults aged 70–81 years have 20% less MOTS-c than younger adults 18–30 years old [19]. In a mouse model of type 2 diabetes, MOTS-c administration increased antioxidant enzymes like SOD and CAT, protecting myocardial cells from oxidative stress [20].
Unlike acute pain, neuropathic pain is pain caused by nervous system dysfunction related to nerve damages, rather than by injury or inflammation. MOTS-c’s antinociceptive effects pertain to its ability to restore mitochondrial health, and inhibit microglial and pain signals in the spinal cord [21]. Furthermore, compared to morphine, MOTS-c has far fewer side effects such as gastrointestinal transit inhibition and motor incoordination [22].
Research Use Only. All findings described above are derived from preclinical studies (animal models and in vitro experiments). MOTS-c is not approved by the FDA for any diagnostic or therapeutic use in humans. Genesis Peptides makes no claims regarding human clinical efficacy. This product is sold exclusively for laboratory research.
Every lot undergoes six independent assays before release. Results are published in the lot-specific Certificate of Analysis.
Every lot undergoes our 6-panel testing protocol: identification by ESI-MS, purification by RP-HPLC, conformity, sterility screening, quantification of net peptide content, and LAL endotoxin screening. Full analytical data is published in the Certificate of Analysis for each lot.
Lyophilized peptides should be stored at -20°C or below for long-term stability. Once reconstituted, peptides should be stored at 2–8°C and used within a reasonable timeframe depending on the specific compound. Avoid repeated freeze-thaw cycles. Always store in a dry environment away from direct light.
Orders are processed within 1–3 business days after payment confirmation. Orders placed after 3:00 PM Pacific time or on weekends and holidays will begin processing the next business day. We offer free standard shipping on orders over $150. All orders are shipped in insulated packaging with ice packs when necessary. Standard delivery typically takes 2–4 business days within the continental US.
No. All compounds sold by Genesis Peptides are strictly for in vitro and preclinical laboratory research purposes only. They are not approved for human consumption, therapeutic use, or diagnostic purposes. By purchasing, you confirm the products will be used solely for legitimate research applications.
A Certificate of Analysis (COA) is a document issued by our analytical laboratory that reports the results of all quality control tests performed on a specific lot of product. Each COA includes HPLC chromatograms, mass spectra, endotoxin results, and quantification data where applicable. COAs are available in our COA Library for every lot we have shipped.
Yes. We offer volume pricing for universities, research institutions, and laboratories with recurring needs. Discounts begin at 100+ units and scale with volume. Contact our team for a custom quote tailored to your research requirements.
FOR RESEARCH USE ONLY — Products are sold exclusively for in vitro and preclinical laboratory research. Not for human consumption or administration. Not intended for diagnostic or therapeutic use. These statements have not been evaluated by the FDA.
What is NAD+? Nicotinamide adenine dinucleotide (oxidized form), commonly abbreviated as NAD⁺, is a naturally occurring coenzyme found in all living cells. It has gained interest in research due to its roles in mediating various cellular anti-aging processes. It plays a central role in redox reactions, acting as an electron carrier in metabolic processes such as glycolysis, the Krebs cycle, and oxidative phosphorylation [1, 2, 3]. Structurally, NAD⁺ consists of two nucleotides joined through their phosphate groups: one nucleotide contains an adenine base, and the other contains nicotinamide [4]. Image source [4] NAD+ functions In cellular systems, NAD⁺ functions as a substrate for a range of enzymes, including: Sirtuins: deacetylases and ADP-ribosyltransferases responsible for the regulation of metabolism, cellular stress response, and aging [5] Poly(ADP-ribose) polymerases (PARPs): enzymes responsible for DNA repair, genomic stability, and programmed cell death [6] CD38/CD157: cell surface proteins found in immune cells [7] In its oxidized form (NAD⁺), the molecule accepts electrons and is converted into its reduced counterpart, NADH, which subsequently donates those electrons to the mitochondrial electron transport chain for ATP production [8]. However, NAD⁺ itself remains a molecule of focus for research exploring its direct biochemical interactions within various intracellular compartments, including the cytoplasm, nucleus, and mitochondria. NAD+ and anti-aging Intracellular NAD⁺ levels decline with cellular aging, demonstrated in several mammalian tissues [9]. Various anti-aging hormeses, such as caloric restriction and cold exposure, work partly by increasing cellular NAD+. This observation has created interest in longevity research and has launched multiple investigations into NAD⁺ precursors such as nicotinamide riboside (NR) and nicotinamide mononucleotide (NMN) in both animals and humans [10], [11]. Age-associated declines in NAD⁺ levels have been linked to impaired mitochondrial function, increased oxidative stress, and reduced sirtuin activity [9]. Lower NAD⁺ concentrations correlate with diminished autophagy, shortened telomeres, and lowered PARP DNA repair activity [12, 13]. Age-related NAD⁺ depletion also impairs endothelial function and contribute to chronic low-grade inflammation [14]. NAD+ and DNA repair Although NAD+ is a PARP substrate, it’s unclear whether increasing physiologic NAD+ concentration can meaningfully improve DNA repair. A clinical trial with 21 healthy smokers orally supplemented nicotinic acid (0, 50, or 100 mg/day) over 14 weeks to track various biological and DNA associated parameters. After 14 weeks, results found [15]: Supplementation with 50 and 100 mg/day of nicotinic acid elevated blood nicotinamide and lymphocyte NAD⁺ concentrations. The rise in NAD⁺ was most pronounced in individuals with initially low NAD⁺ levels. There was no significant reduction in HPRT variant frequencies or micronuclei induction, common measures of DNA damage. Although nicotinamide supplementation did not activate markers of DNA repair, larger sample size studies and comparison to healthy individuals are needed. NAD+ and metabolic health NAD+ supplementation can tangibly improve whole-body metabolic health. An RCT of 30 overweight or obese adults over 45 received 1,000 mg/day of β-nicotinamide mononucleotide (MIB-626) (2 x 500 mg tablets twice daily) vs. placebo for 28 days to see whether NAD⁺ levels could be safely boosted and improve markers of cardiometabolic health [16]. Results showed that MIB-626 supplementation: Significantly increased circulating levels of NAD⁺ and related metabolites significantly increased (p < 0.05). Increased body weight by ~1.9 kg (p = .008). Reduced diastolic blood pressure by ~7 mmHg (p = .034). Significantly reduced total cholesterol by ~27 mg/dL (p = .004) and LDL by ~19 mg/dL (p = .007). NAD+ and addiction NAD+ supplementation is a powerful way to curb addictive behaviors. A pilot study investigated the effects of intravenous NAD+ and enkephalinase combination infusions on cravings and psychological outcomes in 50 individuals with Substance Use Disorder (SUD) [17]. The cohort included a diverse group of poly-drug-dependent individuals. Behavioral changes were evaluated using Likert scales, measuring craving, anxiety, and depression levels before and after infusion therapy. IV NAD+ infusions resulted in: A significant reduction in withdrawal symptoms such as craving, anxiety, and depression (p < 0.0005) Reduced relapse risks as participants had no detectable illicit substances based on the urine tests All reductions followed a dose-dependent linear trend, with greater improvements observed over time. The study shows the potential application of NAD/NADH as a stand-alone treatment in attenuating symptoms of addiction.
What is P21 peptide? P21 is a synthetic peptide designed as a mimetic of ciliary neurotrophic factor (CNTF), a neurotrophin involved in neuronal survival, synaptic maintenance, and central repair pathways. While native CNTF is a large protein with limited permeability and complex receptor interactions, P21 distills CNTF’s key functional domains into a short, bioactive sequence engineered for stability and targeted signaling [1]. One of the biggest advantages of P21 is its ability to cross the blood–brain barrier (BBB). Its small molecular size allows it to access central nervous system tissues more efficiently than full-length neurotrophic proteins [2]. This distinguishes P21 from broader neurotrophic blends such as cerebrolysin, which rely on multi-peptide mixtures and indirect peripheral effects [3]. Cerebrolysin contains fragments derived from porcine brain proteins and act through diffuse signaling. P21, in contrast, is a receptor-specific mimetic designed to emulate a single neurotrophin’s core actions. P21 Peptide Benefits Neurogenesis and Synaptic Plasticity P21’s ability to activate CNTF-related neurotrophic pathways can help support neuronal growth, differentiation, and long-term structural adaptability. A core feature of P21’s activity is promoting neurogenesis, especially within brain regions where adult neural stem cells remain active [4]. P21 also interacts with pathways involved in synaptic plasticity, the process by which neurons strengthen, weaken, or remodel their connections in response to new information [2]. Because P21 is small enough to cross the blood–brain barrier, these effects occur in a more targeted and timely fashion. Alzheimer's Disease P21 has attracted scientific interest for its potential relevance to pathways implicated in Alzheimer’s disease. P21’s interaction with STAT3 and other CNTF-responsive intracellular cascades may help reinforce processes that protect neurons from [5]: Oxidative strain Impaired energy metabolism Synaptic deterioration all hallmarks frequently in Alzheimer’s models. Another area of interest is P21’s potential influence on amyloid- and tau-associated stress responses. An in vivo study in a 3xTg-AD transgenic mouse model of Alzheimer’s disease evaluated effects of 12 months of chronic oral P21. Female 3xTg-AD mice and wild-type controls were given P21 in their diet for 12 months, starting at 9-10 months of age when AD symptoms developed [6]. P21 diets resulted in: Significantly decreased accumulation of abnormal hyperphosphorylated tau Significant reduction in soluble Aβ levels and plaque load Elevated brain-derived neurotrophic factor (BDNF) and decreased GSK3β activity Restored cognitive performance and neurogenesis These findings support P21 as a promising neurotrophic peptide mimetic with therapeutic potential to shift Alzheimer’s disease pathology from neurodegeneration toward regeneration. Developmental disorders P21 has also generated interest in research exploring neurodevelopmental pathways, because CNTF signaling plays a role in neuronal differentiation, axonal guidance, and early circuit formation [7]. During development, CNTF influences how neural progenitors mature into functional neurons and how connections between brain regions are refined. A combined in vitro/in vivo study evaluated the therapeutic potential of P21 in a mouse model of CDKL5 deficiency disorder (CDD) [8]. CDD is an X-linked disorder that results in seizures, developmental and intellectual delays, and usually requires lifelong care. P21 administration resulted in: Successful rescue of multiple CDKL5-related cellular deficits in neurons: Restored proliferation Normalized cell survival Improved neuronal maturation Corrected abnormalities in GSK3β signaling There were limited effects in vivo, as P21 resulted in minimal behavioral improvement. This could be due to differences in bioavailability, timing, or developmental windows between in vitro and in vivo systems. P21 is not just limited to rare neurodevelopmental disorders. Prenatal to early postnatal treatment with the CNTF-derived peptide mimetic P021 was tested in Ts65Dn mice, a Down syndrome model that also develops Alzheimer’s-like memory deficits [9]. Early P021 intervention rescued developmental delays in pups and restored hippocampus-dependent memory in adulthood. The treatment: Prevented presynaptic protein loss Reduced GSK3β activity Increased neuroplasticity markers including BDNF and phosphorylated CREB in both young (3 weeks) and adult mice These results demonstrate that enhancing neurotrophic support during critical periods of early brain development can prevent lifelong cognitive impairment and Alzheimer’s-like pathology associated with trisomy 21.
Snapshot: PEG-MGF (PEGylated Mechano-Growth Factor) is a regulated IGF-1 Ec-derived peptide used in preclinical research to study IGF-1R, PI3K/Akt, and MAPK/ERK signaling in tissue-repair and regeneration models. Experimental studies have explored its roles in skeletal muscle recovery, periodontal ligament remodeling, bone and cartilage repair, and injury-response pathways. What Is PEG-MGF? PEG-MGF (Polyethylene Glycol–Modified Mechano-Growth Factor) is a chemically-modified peptide related to the IGF-1 Ec splice-variant sequence (also called MGF). In research settings, it is used as a pathway probe to study IGF-axis signaling, skeletal muscle regeneration programs, and injury-response biology in both in vitro and in vivo models [1, 2, 3]. Pegylation is applied to increase peptide persistence and stability, allowing for longer exposure windows compared with non-pegylated fragments in time-course and distribution studies [4]. Experimental studies most often evaluate PEG-MGF in contexts including skeletal muscle injury and repair, cardiac ischemia and hypoxia, bone healing and osteoblast activity, cartilage and chondrocyte migration, and periodontal ligament cell differentiation. Mechanistically, its actions are linked to IGF-1 receptor activation and downstream PI3K/Akt and MAPK/ERK signaling pathways, which are associated with cell growth, migration, and survival responses [3]. PEG-MGF Peptide Benefits & Side Effects PEG-MGF has been investigated in preclinical and mechanistic research models, with findings suggesting potential roles in muscle repair and regeneration [5], modulation of inflammatory mediator expression and immune-cell clearance kinetics [6], osteoblast proliferation [7], chondrocyte migration and mechanotransduction pathways [2], and apoptosis and remodeling in cardiac injury models [8]. In experimental settings, key considerations include the fact that IGF-axis activation is linked to cell-proliferation signaling, which warrants caution in models involving abnormal or uncontrolled cell growth [2]. Effects may also vary depending on delivery method and PEGylation format, and current evidence remains largely limited to controlled preclinical studies. These findings are model-specific and should be interpreted within a lab-research context. Hypertrophy and Muscle Damage Repair PEG-MGF and related MGF-derived peptides are frequently studied in models of muscle injury and repair. These experiments typically measure changes in inflammation, oxidative stress, and expression of genes involved in tissue recovery and remodelling [2]. Cell-based studies using myoblasts and muscle-cell cultures also study cell growth, migration, and IGF-1R-linked PI3K/Akt and MAPK/ERK signaling, which are pathways associated with hypertrophy and regeneration rather than performance enhancement [2]. Across multiple studies, MGF peptides support satellite-cell activation, proliferation, and fusion, which are key steps in muscle maintenance and repair [5, 3]. In primary human muscle cell cultures, the MGF-24aa-E peptide increased the proliferative lifespan of satellite cells and delayed cellular aging in younger tissue, while promoting hypertrophy across all age groups [5]. These effects are interpreted as enhanced regenerative capacity, particularly relevant to age-related muscle loss and sarcopenia [5]. Other experimental models show that early increases in MGF splice-variant expression tend to coincide with the initial, proliferation-focused phase of muscle repair, followed later by differentiation and myofiber maturation [3]. MGF-related peptides have also been studied in cardiac injury settings. In animal models of myocardial infarction, delivery of MGF E-domain peptides has been associated with better preservation of cardiac function, smaller regions of compromised tissue, reduced cell-death signaling, and slower progression of adverse remodeling [8, 9]. In some studies, localized delivery using peptide-eluting biomaterial structures further improved hemodynamic recovery following injury [9]. Overall findings suggest benefits for repair, survival, and regeneration-linked signaling programs both in skeletal and cardiac muscle, with applications focused on tissue-healing rather than performance outcomes. Periodontal Regeneration MGF-related peptides have also been studied in periodontal ligament (PDL) regeneration models, particularly under mechanical loading conditions such as occlusal force. In vitro and in vivo studies show that MGF produced in response to mechanical stimulation can enhance PDL remodelling and promote periodontal ligament stem-cell proliferation and fibrogenic differentiation [10, 11]. These effects are linked to Fyn-FAK-mediated mechanochemical signaling, activation of ERK1/2 and p38 pathways, and the Fyn-RhoA-YAP phosphorylation axis, which together support matrix remodeling and fibroblast-like differentiation [10]. Collectively, these findings suggest a potential role for MGF-centered signaling as an adjunct approach in periodontal regeneration research. Anabolic and Regenerative Effects PEG-MGF peptides have been studied in multiple injury- and regeneration-focused models. In cardiac ischemia, MGF expression rises rapidly and peptide delivery has been associated with reduced apoptosis, preservation of myocardium, improved hemodynamics, and possible stimulation of precursor cell recruitment [4]. In neural and hypoxia-ischemia models, MGF shows neuroprotective activity independent of IGF-1R signaling, supporting cell survival pathways [4]. MGF has also been reported to influence chondrocyte and mesenchymal-cell differentiation, matrix remodelling, and cytoskeletal dynamics under stress or damage conditions [4]. References 1 Liu, X., Zeng, Z., Zhao, L., Chen, P. and Xiao, W. (2019) Impaired skeletal muscle regeneration induced by macrophage depletion could be partly ameliorated by MGF injection. Front. Physiol., Frontiers Media SA 10, 601 2 Liu, Y., Duan, M., Zhang, D. and Xie, J. (2023) The role of mechano growth factor in chondrocytes and cartilage defects: a concise review. Acta Biochim. Biophys. Sin. (Shanghai), China Science Publishing & Media Ltd. 55, 701–712 3 Matheny, R. W., Jr, Nindl, B. C. and Adamo, M. L. (2010) Minireview: Mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration. Endocrinology, The Endocrine Society 151, 865–875 4 Zabłocka, B., Goldspink, P. H., Goldspink, G. and Górecki, D. C. (2012) Mechano-Growth Factor: an important cog or a loose screw in the repair machinery? Front. Endocrinol. (Lausanne), Frontiers Media SA 3, 131 5 Kandalla, P. K., Goldspink, G., Butler-Browne, G. and Mouly, V. (2011) Mechano Growth Factor E peptide (MGF-E), derived from an isoform of IGF-1, activates human muscle progenitor cells and induces an increase in their fusion potential at different ages. Mech. Ageing Dev. 132, 154–162 6 Lin, Y.-C., Chen, B.-M., Tran, T. T. M., Chang, T.-C., Al-Qaisi, T. S. and Roffler, S. R. (2023) Accelerated clearance by antibodies against methoxy PEG depends on pegylation architecture. J. Control. Release, Elsevier BV 354, 354–367 7 Deng, M., Zhang, B., Wang, K., Liu, F., Xiao, H., Zhao, J., et al. (2011) Mechano growth factor E peptide promotes osteoblasts proliferation and bone-defect healing in rabbits. Int. Orthop., Springer Science and Business Media LLC 35, 1099–1106 8 Carpenter, V., Matthews, K., Devlin, G., Stuart, S., Jensen, J., Conaglen, J., et al. (2008) Mechano-growth factor reduces loss of cardiac function in acute myocardial infarction. Heart Lung Circ., Elsevier BV 17, 33–39 9 Peña, J. R., Pinney, J. R., Ayala, P., Desai, T. A. and Goldspink, P. H. (2015) Localized delivery of mechano-growth factor E-domain peptide via polymeric microstructures improves cardiac function following myocardial infarction. Biomaterials, Elsevier BV 46, 26–34 10 Feng, F., Tu, T., Wang, H., Song, R., Li, J., Zhu, Y., et al. (2024) Mechano-growth factor regulates periodontal ligament stem cell proliferation and differentiation through Fyn-RhoA-YAP signaling. Biochem. Biophys. Res. Commun., Elsevier BV 733, 150450 11 Zhao, Y., Zhang, S., Cheng, B., Feng, F., Zhu, Y., Liu, Y., et al. (2024) Mechanochemical coupling of MGF mediates periodontal regeneration. Bioeng. Transl. Med., Wiley 9, e10603