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Humanin peptides are Synthesized and Lyophilized in the USA.
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FREE - 30ml bottle of bacteriostatic water
(Required for reconstitution)
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What is the Humanin peptide?
Humanin is a naturally occurring micropeptide that is unique in that it is encoded by mitochondrial DNA (mitochondria contain small amounts of DNA reserved exclusively for it). It appears to act as a cytoprotective protein and may protect cells from the process of apoptosis (programmed cell death) by interfering with the normal operation of the Bcl2-related X protein (Bax). Researchers report that Humanin “prevents the translocation of Bax from cytosol to mitochondria. Conversely, reducing Humanin expression by small interfering RNAs sensitizes cells to Bax and increases Bax translocation to membranes.” Studies suggest that Humanin may be important for protecting neurons, heart tissue, muscle cells, the retina of the eye, and the lining of blood vessels.
AKA: formyl humanin, HNGF6A protein
Molecular Formula: C119H204N34O32S2
Molecular Weight: 2687.3 g/mol
CAS Number: 330936-69-1
What Is a Micro-peptide?
Micropeptides are produced by a short open reading frame (sORF) and are not modified after production. Many sORFs have been identified in humans, measuring 100-150 amino acids in length. Their functions range from improving mRNA processing to assisting in repairing DNA damage and creating complex macro-proteins by interacting with other proteins. Humanin, one of the smallest micropeptides known to date, is only 24 amino acids long. It appears to interact with the Bcl2-related X protein (Bax) to regulate apoptosis and, if necessary, block Bax function and protect cells that would otherwise be destroyed.
Humanin and Neuroprotection
Studies in rats have suggested that micropeptides may protect Alzheimer’s disease neurons and prevent cell death caused by the formation of beta-amyloid plaques. The scientists note that “HN exhibits multiple intracellular and extracellular anti-cell death actions and antagonizes various AD-associated pathomechanisms including amyloid plaque accumulation.” Studies further suggest that peptides prevent the death of excitotoxic neurons in experiments with NMDA pulses. It is hoped that this function of Humanin may delay or stop neurodegenerative diseases such as Alzheimer’s disease and other forms of dementia. Under normal circumstances, Bcl2 family proteins signal the release of proteins from mitochondrial membranes, activating caspases and coordinating the orderly destruction and recycling of cells. This process is practically useful in many situations, such as when a virus invades, where a small number of cells can be destroyed to prevent widespread tissue damage. Unfortunately, the process can become dysregulated in certain medical conditions, leading to widespread unsuppressed cell death. Humanin appears to bind to the Bcl2-stimulating proteins Bid and tBid and block their function. This action would shut down the apoptotic pathway at its origin.
Humanin Interfaces with IGF-1
A recent study from the University of Southern California suggested that Humanin and insulin-like growth factor 1 (IGF1) may reduce the circulating levels of IGF1 and IGF1 and affect natural Humanin levels. Peptides are synergistic in many ways, working together to potentially suppress apoptosis, increase insulin sensitivity, reduce inflammation, and protect against certain forms of heart disease.
Humanin and Heart Disease
A study by the Mayo Clinic posited that Humanin may be expressed on the walls of the human vascular system and may interfere with the production of reactive oxygen species (free radicals) in response to LDL oxidation. It has the potential to reduce active oxygen species in the vascular system by 50% and may reduce apoptosis by 50%. Cardiology researchers have long sought blood markers that could be used to quantify how effectively mitochondria function in cardiovascular disease. It is an important measure of the patients’ health with heart disease and helps accurately estimate tissue ischemia and disease progression and determine when to intervene. According to a Russian study, the reduction is proportional to the severity of cardiovascular disease, so Humanin levels may be a good marker in this situation.
Humanin and Retinal Disease
Retinal pigment epithelium (RPE) is the layer of the retina that covers and nourishes the cells that cause vision. It plays a role in the absorption and scattering of light, filtering blood components that reach the inside of the retina. It also, above all, establishes the nature of immune privilege inside the eye. RPE damage is found in age-related macular degeneration, diabetic retinopathy, and other common serious eye conditions. Current studies have suggested that Humanin may be an important component of RPE and may reduce oxidative stress in this tissue. Humanin supplementation in cell culture appears to improve RPE function and increase tissue resistance to apoptosis. This may help scientists develop more effective treatment and prevention strategies for retinal disorders such as macular degeneration.
Humanin and Bone Health
Bone loss is a serious condition that affects many people, especially women, with age. It is also the result of many medical conditions and is even caused by certain medical interventions. In the latter category, glucocorticoids used to treat severe inflammation (such as autoimmune inflammation) are the most notorious gamblers. They cause extreme bone loss when used at high doses or for long periods. Researchers in Sweden and South Korea have hypothesized that Humanin may benefit bones in two different ways. First, micropeptides were suggested to prevent chondrocytes (cells that produce the collagen matrix in which bone is built) from dying without affecting the anti-inflammatory effects of glucocorticoids such as dexamethasone. This effect would increase bone and cartilage growth and help offset some of the accelerated bone loss caused by glucocorticoids. At the same time as promoting chondrocyte development, Humanin appears to have the potential to reduce osteoclast formation. Osteoclasts are the cells that cause bone loss and remodeling. Overactivation of these cells is useful and important for normal physiologic function in pathological conditions, resulting in severe bone loss. By preventing osteoclast formation, Humanin may help to reduce excessive bone remodeling and loss.
- Guo B, Zhai D, Cabezas E, Welsh K, Nouraini S, Satterthwait AC, Reed JC. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature. 2003 May 22;423(6938):456-61. doi: 10.1038/nature01627. Epub 2003 May 4. PMID: 12732850.
- Sousa ME, Farkas MH. Micropeptide. PLoS Genet. 2018 Dec 13;14(12):e1007764. doi: 10.1371/journal.pgen.1007764. PMID: 30543625; PMCID: PMC6292567.
- Niikura T. Humanin and Alzheimer’s disease: The beginning of a new field. Biochim Biophys Acta Gen Subj. 2022 Jan;1866(1):130024. doi: 10.1016/j.bbagen.2021.130024. Epub 2021 Oct 7. PMID: 34626746.
- Xiao J, Kim SJ, Cohen P, Yen K. Humanin: Functional Interfaces with IGF-I. Growth Horm IGF Res. 2016 Aug;29:21-27. doi: 10.1016/j.ghir.2016.03.005. Epub 2016 Apr 7. PMID: 27082450; PMCID: PMC4961574.
- Qin Q, Mehta H, Yen K, Navarrete G, Brandhorst S, Wan J, Delrio S, Zhang X, Lerman LO, Cohen P, Lerman A. Chronic treatment with the mitochondrial peptide humanin prevents age-related myocardial fibrosis in mice. Am J Physiol Heart Circ Physiol. 2018 Nov 1;315(5):H1127-H1136. doi: 10.1152/ajpheart.00685.2017. Epub 2018 Jul 13. PMID: 30004252; PMCID: PMC6415743.
- Li Z, Sreekumar PG, Peddi S, Hinton DR, Kannan R, MacKay JA. The humanin peptide mediates ELP nanoassembly and protects human retinal pigment epithelial cells from oxidative stress. Nanomedicine. 2020 Feb;24:102111. doi: 10.1016/j.nano.2019.102111. Epub 2019 Oct 23. PMID: 31655204; PMCID: PMC7263384.
- Kang N, Kim KW, Shin DM. Humanin suppresses receptor activator of nuclear factor-κB ligand-induced osteoclast differentiation via AMP-activated protein kinase activation. Korean J Physiol Pharmacol. 2019 Sep;23(5):411-417. doi: 10.4196/kjpp.2019.23.5.411. Epub 2019 Aug 26. PMID: 31496878; PMCID: PMC6717796.
Dr. Usman (BSc, MBBS, MaRCP) completed his studies in medicine at the Royal College of Physicians, London. He is an avid researcher with more than 30 publications in internationally recognized peer-reviewed journals. Dr. Usman has worked as a researcher and a medical consultant for reputable pharmaceutical companies such as Johnson & Johnson and Sanofi.