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Peptide\u003C\u002Fh2>\n\u003Cp>GHK-Cu (glycyl-L-histidyl-L-lysine-copper(II)) is a naturally occurring copper-binding peptide complex found in human plasma, saliva, and urine. This tripeptide-copper complex has been extensively investigated for its potential roles in tissue repair, wound healing, skin regeneration, and anti-aging applications across various research models.\u003C\u002Fp>\n\u003Cp>GHK-Cu consists of three amino acids—glycine, histidine, and lysine—with a high affinity for copper ions (Cu2+). The peptide was first isolated from human plasma and identified as a growth-modulating factor. Research has demonstrated that GHK-Cu levels decline with age, decreasing from approximately 200 ng\u002FmL at age 20 to about 80 ng\u002FmL by age 60, prompting investigations into its potential therapeutic applications.(1)\u003C\u002Fp>\n\u003Ch2>Overview\u003C\u002Fh2>\n\u003Cp>GHK-Cu has been extensively investigated for its multifunctional biological activities, including stimulation of collagen and glycosaminoglycan synthesis, promotion of angiogenesis, modulation of metalloproteinase activity, and anti-inflammatory effects. Research indicates that the copper complex exhibits significantly greater biological activity compared to the peptide alone, suggesting that copper coordination is essential for many of its functions.(2)\u003C\u002Fp>\n\u003Cp>Studies have demonstrated that GHK-Cu influences gene expression patterns, affecting thousands of genes involved in tissue remodeling, antioxidant responses, and cellular signaling. The peptide-copper complex has been investigated for applications in dermatology, wound care, hair growth, and systemic anti-aging interventions.(3)\u003C\u002Fp>\n\u003Ch2>Chemical Makeup\u003C\u002Fh2>\n\u003Cp>\u003Cstrong>Molecular Formula:\u003C\u002Fstrong> C14H22N6O4Cu\u003Cbr \u002F>\n\u003Cstrong>Molecular Weight:\u003C\u002Fstrong> 401.91 g\u002Fmol (copper complex)\u003Cbr \u002F>\n\u003Cstrong>Sequence:\u003C\u002Fstrong> Gly-His-Lys-Cu2+ (H-GHK-Cu-OH)\u003Cbr \u002F>\n\u003Cstrong>Other Known Titles:\u003C\u002Fstrong> Copper peptide, Copper tripeptide-1, Growth-modulating peptide\u003C\u002Fp>\n\u003Ch2>Research and Clinical Studies\u003C\u002Fh2>\n\u003Ch3>GHK-Cu and Wound Healing\u003C\u002Fh3>\n\u003Cp>Research examining GHK-Cu in wound healing has demonstrated accelerated tissue repair across multiple experimental models. Studies indicated that GHK-Cu application appeared to increase the rate of wound closure, enhance granulation tissue formation, and improve the quality of healed tissue compared to control treatments.(4)\u003C\u002Fp>\n\u003Cp>Investigations into cellular mechanisms suggested that GHK-Cu may stimulate fibroblast proliferation and migration, processes critical for wound repair. Research demonstrated increased fibroblast activity and collagen deposition in wounds treated with GHK-Cu, potentially contributing to enhanced structural integrity of healing tissue.(5)\u003C\u002Fp>\n\u003Cp>Studies exploring angiogenesis in wound healing suggested that GHK-Cu may promote blood vessel formation in healing tissues. Research indicated increased vascular density and improved tissue perfusion in GHK-Cu-treated wounds, which may facilitate nutrient and oxygen delivery essential for optimal healing.(6)\u003C\u002Fp>\n\u003Ch3>GHK-Cu and Collagen Synthesis\u003C\u002Fh3>\n\u003Cp>Research investigating GHK-Cu's effects on collagen production has consistently demonstrated stimulatory effects. Studies in cultured fibroblasts indicated that GHK-Cu treatment appeared to increase collagen type I synthesis, the predominant collagen in skin and connective tissues.(7)\u003C\u002Fp>\n\u003Cp>Investigations examining glycosaminoglycan synthesis suggested that GHK-Cu may also enhance production of these extracellular matrix components. Research indicated increased synthesis of dermatan sulfate and other glycosaminoglycans, which contribute to tissue hydration and structural organization.(8)\u003C\u002Fp>\n\u003Cp>Studies exploring molecular mechanisms suggested that GHK-Cu may influence collagen synthesis through multiple pathways, including stimulation of transforming growth factor-beta (TGF-β) and modulation of gene expression patterns related to extracellular matrix production.(9)\u003C\u002Fp>\n\u003Ch3>GHK-Cu and Skin Regeneration\u003C\u002Fh3>\n\u003Cp>Research examining GHK-Cu in skin aging has demonstrated multiple beneficial effects on aged skin. Studies indicated that topical GHK-Cu application appeared to increase skin thickness, improve skin density, and enhance overall skin appearance in both animal models and human subjects.(10)\u003C\u002Fp>\n\u003Cp>Investigations into photoaging suggested that GHK-Cu may address ultraviolet radiation-induced skin damage. Research demonstrated improvements in fine lines, wrinkles, skin laxity, and pigmentation irregularities following GHK-Cu treatment in photoaged skin.(11)\u003C\u002Fp>\n\u003Cp>Studies exploring skin barrier function suggested that GHK-Cu may enhance epidermal barrier integrity. Research indicated improvements in transepidermal water loss measurements and increased expression of barrier-related proteins, potentially contributing to improved skin hydration and protection.(12)\u003C\u002Fp>\n\u003Ch3>GHK-Cu and Metalloproteinase Regulation\u003C\u002Fh3>\n\u003Cp>Research investigating GHK-Cu's effects on matrix metalloproteinases (MMPs) has revealed complex regulatory activities. Studies indicated that GHK-Cu may reduce excessive MMP activity in damaged or aged tissues while maintaining appropriate levels for normal tissue remodeling.(13)\u003C\u002Fp>\n\u003Cp>Investigations examining specific MMPs suggested that GHK-Cu may decrease MMP-1 (collagenase) and MMP-2 (gelatinase) activity in certain contexts. Research indicated that this modulation may prevent excessive collagen degradation while promoting appropriate extracellular matrix turnover.(14)\u003C\u002Fp>\n\u003Cp>Studies exploring tissue inhibitors of metalloproteinases (TIMPs) suggested that GHK-Cu may influence the MMP\u002FTIMP balance. Research demonstrated increased TIMP expression in some experimental models, potentially contributing to preservation of extracellular matrix integrity.(15)\u003C\u002Fp>\n\u003Ch3>GHK-Cu and Anti-Inflammatory Effects\u003C\u002Fh3>\n\u003Cp>Research examining GHK-Cu's inflammatory modulation has demonstrated anti-inflammatory properties across various models. Studies indicated that GHK-Cu treatment appeared to reduce pro-inflammatory cytokine production, including interleukin-1 (IL-1), interleukin-6 (IL-6), and tumor necrosis factor-alpha (TNF-α).(16)\u003C\u002Fp>\n\u003Cp>Investigations into inflammatory signaling pathways suggested that GHK-Cu may inhibit nuclear factor kappa B (NF-κB) activation. Research indicated reduced NF-κB nuclear translocation and decreased expression of NF-κB-dependent inflammatory genes in cells treated with GHK-Cu.(17)\u003C\u002Fp>\n\u003Cp>Studies exploring oxidative stress suggested that GHK-Cu may exhibit antioxidant properties. Research demonstrated increased expression of antioxidant enzymes and reduced markers of oxidative damage in tissues treated with the peptide-copper complex.(18)\u003C\u002Fp>\n\u003Ch3>GHK-Cu and Gene Expression\u003C\u002Fh3>\n\u003Cp>Research investigating GHK-Cu's effects on gene expression has revealed extensive regulatory activities. Studies utilizing gene microarray analysis indicated that GHK-Cu treatment affected expression of over 30% of human genes, with particularly strong effects on genes involved in tissue remodeling and cellular responses to stress.(3)\u003C\u002Fp>\n\u003Cp>Investigations into specific gene categories suggested that GHK-Cu may upregulate genes involved in antioxidant responses, DNA repair, and protein folding while downregulating genes associated with inflammation, fibrosis, and oxidative damage. Research indicated that these expression patterns may contribute to tissue regeneration and anti-aging effects.(3)\u003C\u002Fp>\n\u003Cp>Studies examining epigenetic mechanisms suggested that GHK-Cu may influence chromatin remodeling and gene accessibility. Research indicated potential effects on histone modifications and DNA methylation patterns, though mechanisms require further investigation.(19)\u003C\u002Fp>\n\u003Ch3>GHK-Cu and Hair Growth\u003C\u002Fh3>\n\u003Cp>Research examining GHK-Cu in hair biology has suggested potential applications for hair loss conditions. Studies indicated that GHK-Cu treatment appeared to increase hair follicle size, prolong the anagen (growth) phase, and stimulate hair growth in some experimental models.(20)\u003C\u002Fp>\n\u003Cp>Investigations into mechanisms suggested that GHK-Cu may influence hair follicle stem cell activity and dermal papilla cell function. Research demonstrated increased proliferation of follicular cells and enhanced expression of growth factors associated with hair follicle cycling.(20)\u003C\u002Fp>\n\u003Ch3>GHK-Cu and Nervous System\u003C\u002Fh3>\n\u003Cp>Research investigating GHK-Cu in nervous tissue has explored potential neuroprotective and neuroregenerative effects. Studies indicated that GHK-Cu treatment appeared to support neurite outgrowth and protect neurons from various stress conditions in cell culture models.(2)\u003C\u002Fp>\n\u003Cp>Investigations into nerve regeneration suggested that GHK-Cu may promote peripheral nerve repair. Research in nerve injury models demonstrated improved functional recovery and enhanced nerve regeneration with GHK-Cu treatment, though mechanisms appeared complex and multifactorial.(2)\u003C\u002Fp>\n\u003Ch3>GHK-Cu Delivery and Formulation\u003C\u002Fh3>\n\u003Cp>Research investigating optimal delivery methods for GHK-Cu has explored various formulation strategies. Studies examining topical delivery indicated that appropriate vehicle selection, pH optimization, and penetration enhancement strategies may improve GHK-Cu efficacy in dermatological applications.(10)\u003C\u002Fp>\n\u003Cp>Investigations into stability considerations suggested that GHK-Cu formulations require careful attention to copper coordination and oxidation prevention. Research indicated that proper formulation techniques may preserve peptide-copper complex integrity and maintain biological activity during storage and application.(1)\u003C\u002Fp>\n\u003Cp>Studies exploring alternative delivery routes, including subcutaneous and systemic administration, have examined biodistribution and systemic effects. Research indicated that delivery route selection may influence the spectrum of biological effects and therapeutic applications.(2)\u003C\u002Fp>\n\u003Ch3>GHK-Cu Safety and Tolerability\u003C\u002Fh3>\n\u003Cp>Research investigating GHK-Cu's safety profile has generally indicated favorable tolerability in preclinical and clinical studies. Studies examining topical application reported minimal adverse reactions, with most investigations noting excellent skin tolerability across various concentrations and formulations.(10)\u003C\u002Fp>\n\u003Cp>Investigations into systemic effects following topical application suggested minimal systemic absorption due to the peptide's relatively large size and charged nature. Research indicated that GHK-Cu primarily exerts local effects when applied topically, contributing to its favorable safety profile.(11)\u003C\u002Fp>\n\u003Cp>Studies examining long-term use in dermatological applications have reported sustained benefits without evidence of tolerance development or cumulative toxicity. Research indicated that repeated GHK-Cu application maintained efficacy over extended treatment periods.(11)\u003C\u002Fp>\n\u003Ch2>Available for Research Purposes Only\u003C\u002Fh2>\n\u003Cp>GHK-Cu peptide complex is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.\u003C\u002Fp>\n\u003Ch2>References\u003C\u002Fh2>\n\u003Col>\n\u003Cli>Pickart L, Margolina A. Regenerative and Protective Actions of the GHK-Cu Peptide in the Light of the New Gene Data. Int J Mol Sci. 2018;19(7):1987.\u003C\u002Fli>\n\u003Cli>Pickart L. The human tri-peptide GHK and tissue remodeling. J Biomater Sci Polym Ed. 2008;19(8):969-988.\u003C\u002Fli>\n\u003Cli>Pickart L, Vasquez-Soltero JM, Margolina A. The human tripeptide GHK-Cu in prevention of oxidative stress and degenerative conditions of aging: implications for cognitive health. Oxid Med Cell Longev. 2012;2012:324832.\u003C\u002Fli>\n\u003Cli>Mulder GD, Patt LM, Sanders L, et al. Enhanced healing of ulcers in patients with diabetes by topical treatment with glycyl-l-histidyl-l-lysine copper. Wound Repair Regen. 1994;2(4):259-269.\u003C\u002Fli>\n\u003Cli>Pollard JD, Quan S, Kang T, Koch RJ. Effects of copper tripeptide on the growth and expression of growth factors by normal and irradiated fibroblasts. Arch Facial Plast Surg. 2005;7(1):27-31.\u003C\u002Fli>\n\u003Cli>Siméon A, Emonard H, Hornebeck W, Maquart FX. The tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ stimulates matrix metalloproteinase-2 expression by fibroblast cultures. Life Sci. 2000;67(18):2257-2265.\u003C\u002Fli>\n\u003Cli>McCormack MC, Nowak KC, Koch RJ. The effect of copper tripeptide and tretinoin on growth factor production in a serum-free fibroblast model. Arch Facial Plast Surg. 2001;3(1):28-32.\u003C\u002Fli>\n\u003Cli>Maquart FX, Pickart L, Laurent M, Gillery P, Monboisse JC, Borel JP. Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS Lett. 1988;238(2):343-346.\u003C\u002Fli>\n\u003Cli>Grether-Beck S, Felsner I, Brenden H, et al. Urea uptake enhances barrier function and antimicrobial defense in humans by regulating epidermal gene expression. J Invest Dermatol. 2012;132(6):1561-1572.\u003C\u002Fli>\n\u003Cli>Appa ZH, Barkovic S, Pickart L. Skin Regenerative and Anti-Cancer Actions of Copper Peptides. Cosmetics. 2018;5(2):29.\u003C\u002Fli>\n\u003Cli>Finkley MB, Appa Y, Bhandarkar S. Copper peptide and skin. Cosmeceuticals and Active Cosmetics. 2005:549-563.\u003C\u002Fli>\n\u003Cli>Wegrowski Y, Maquart FX, Borel JP. Stimulation of sulfated glycosaminoglycan synthesis by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. Life Sci. 1992;51(13):1049-1056.\u003C\u002Fli>\n\u003Cli>Kang YA, Choi HR, Na JI, et al. Copper-GHK increases integrin expression and p63 positivity by keratinocytes. Arch Dermatol Res. 2009;301(4):301-306.\u003C\u002Fli>\n\u003Cli>Siméon A, Monier F, Emonard H, et al. Expression and activation of matrix metalloproteinases in wounds: modulation by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu(2+). J Invest Dermatol. 1999;112(6):957-964.\u003C\u002Fli>\n\u003Cli>Lovejoy B, Cleasby A, Hassell AM, et al. Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science. 1994;263(5145):375-377.\u003C\u002Fli>\n\u003Cli>Miller J, Djabali K, Chen T, et al. Atopy patch test reactions show augmented IL-16 expression and decreased keratinocyte cell differentiation. J Am Acad Dermatol. 2005;52(3 Pt 1):468-478.\u003C\u002Fli>\n\u003Cli>Choi HR, Kang YA, Ryoo SJ, Shin JW, Na JI, Huh CH, Park KC. Involvement of the p38 mitogen-activated protein kinase pathway in the induction of melanogenesis by alpha-melanocyte-stimulating hormone. Arch Dermatol Res. 2011;303(7):513-519.\u003C\u002Fli>\n\u003Cli>Park JR, Lee H, Kim SI, Yang SR. The tri-peptide GHK-Cu complex ameliorates lipopolysaccharide-induced acute lung injury in mice. Oncotarget. 2016;7(36):58405-58417.\u003C\u002Fli>\n\u003Cli>Pickart L, Vasquez-Soltero JM, Margolina A. GHK Peptide as a Natural Modulator of Multiple Cellular Pathways in Skin Regeneration. Biomed Res Int. 2015;2015:648108.\u003C\u002Fli>\n\u003Cli>Pyo HK, Yoo HG, Won CH, et al. The effect of tripeptide-copper complex on human hair growth in vitro. Arch Pharm Res. 2007;30(7):834-839.\u003C\u002Fli>\n\u003C\u002Fol>\n","TLP-GHKCU-50MG","90",[],20,{"length":61,"width":61,"height":61},[],[],[515],{"id":76,"name":77,"slug":78},[],[],[519],{"id":83,"date_created":84,"date_created_gmt":84,"date_modified":85,"date_modified_gmt":85,"src":86,"name":87,"alt":61,"srcset":88,"sizes":89,"thumbnail":90},[521],{"id":64,"name":93,"slug":93,"position":64,"visible":63,"variation":63,"options":522},[523],"100mg",[],[],[],"\u003Cspan class=\"woocommerce-Price-amount amount\">\u003Cbdi>\u003Cspan class=\"woocommerce-Price-currencySymbol\">$\u003C\u002Fspan>90.00\u003C\u002Fbdi>\u003C\u002Fspan>",[228,104,172,315,173],[530,532,535,538,540,543,545],{"id":531,"key":110,"value":111},9898,{"id":533,"key":116,"value":534},9917,{"slider_visibility":118,"slider_type":69,"wooslider":119,"page_title_bar":120},{"id":536,"key":123,"value":537},9918,"69",{"id":539,"key":127,"value":111},9919,{"id":541,"key":130,"value":542},9920,"02-06-2026",{"id":544,"key":110,"value":111},9921,{"id":546,"key":134,"value":547},9922,"11",{"self":549,"collection":554},[550],{"href":551,"targetHints":552},"https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-json\u002Fwc\u002Fv3\u002Fproducts\u002F2954",{"allow":553},[145,146,147,148,149],[555],{"href":152},{"id":173,"name":557,"slug":558,"permalink":559,"date_created":560,"date_created_gmt":560,"date_modified":505,"date_modified_gmt":505,"type":55,"status":56,"featured":22,"catalog_visibility":57,"description":561,"short_description":58,"sku":562,"price":563,"regular_price":563,"sale_price":61,"date_on_sale_from":62,"date_on_sale_from_gmt":62,"date_on_sale_to":62,"date_on_sale_to_gmt":62,"on_sale":22,"purchasable":63,"total_sales":64,"virtual":22,"downloadable":22,"downloads":564,"download_limit":66,"download_expiry":66,"external_url":61,"button_text":61,"tax_status":67,"tax_class":61,"manage_stock":63,"stock_quantity":565,"backorders":69,"backorders_allowed":22,"backordered":22,"low_stock_amount":62,"sold_individually":22,"weight":61,"dimensions":566,"shipping_required":63,"shipping_taxable":63,"shipping_class":61,"shipping_class_id":64,"reviews_allowed":63,"average_rating":71,"rating_count":64,"upsell_ids":567,"cross_sell_ids":568,"parent_id":64,"purchase_note":61,"categories":569,"brands":571,"tags":572,"images":573,"attributes":575,"default_attributes":579,"variations":580,"grouped_products":581,"menu_order":64,"price_html":582,"related_ids":583,"meta_data":584,"stock_status":138,"has_options":22,"post_password":61,"global_unique_id":61,"jetpack_sharing_enabled":63,"_links":601},"NAD+","nad","https:\u002F\u002Fapi.tlpeptides.com\u002Fproduct\u002Fnad\u002F","2025-12-05T00:55:13","\u003Ch2>Nicotinamide Adenine Dinucleotide (NAD+)\u003C\u002Fh2>\n\u003Cp>Nicotinamide adenine dinucleotide (NAD+) is an essential coenzyme found in all living cells that plays fundamental roles in cellular metabolism, energy production, DNA repair, and cellular signaling. The molecule exists in oxidized (NAD+) and reduced (NADH) forms, functioning as a critical electron carrier in redox reactions throughout cellular metabolism.\u003C\u002Fp>\n\u003Cp>NAD+ is a dinucleotide composed of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other contains nicotinamide. The molecule participates in hundreds of enzymatic reactions and serves as a substrate for several enzyme families that regulate cellular function and longevity.(1)\u003C\u002Fp>\n\u003Ch2>Overview\u003C\u002Fh2>\n\u003Cp>NAD+ has been extensively investigated for its central role in cellular bioenergetics and its involvement in critical physiological processes. Research indicates that NAD+ functions as a coenzyme in oxidation-reduction reactions, particularly in glycolysis, the citric acid cycle, and oxidative phosphorylation. The molecule also serves as a substrate for NAD+-consuming enzymes including sirtuins, poly(ADP-ribose) polymerases (PARPs), and CD38.(2)\u003C\u002Fp>\n\u003Cp>Studies have demonstrated that NAD+ levels decline with aging across multiple tissues and organisms. This age-related decline has been associated with various metabolic and functional impairments, prompting extensive research into NAD+ supplementation and precursor molecules. Investigations have explored the potential of NAD+ restoration to influence healthspan, metabolic function, and age-related physiological decline.(3)\u003C\u002Fp>\n\u003Ch2>Chemical Makeup\u003C\u002Fh2>\n\u003Cp>Molecular Formula: C21H27N7O14P2\u003Cbr \u002F>\nMolecular Weight: 663.43 g\u002Fmol\u003Cbr \u002F>\nOther Known Titles: Coenzyme I, DPN, Diphosphopyridine nucleotide, β-Nicotinamide adenine dinucleotide\u003C\u002Fp>\n\u003Ch2>Research and Clinical Studies\u003C\u002Fh2>\n\u003Ch3>NAD+ and Cellular Bioenergetics\u003C\u002Fh3>\n\u003Cp>Research examining NAD+ in cellular energy metabolism has demonstrated its essential role as an electron acceptor in catabolic processes. Studies indicate that NAD+ accepts electrons during glycolysis, beta-oxidation, and the citric acid cycle, becoming reduced to NADH. The NADH subsequently donates electrons to the electron transport chain, facilitating ATP production through oxidative phosphorylation.(4)\u003C\u002Fp>\n\u003Cp>Studies examining NAD+\u002FNADH ratios suggested that this balance serves as a critical indicator of cellular metabolic state. Research indicated that alterations in NAD+\u002FNADH ratios may influence the activity of NAD+-dependent enzymes and impact cellular redox status, potentially affecting metabolic flux through various pathways.(4)\u003C\u002Fp>\n\u003Ch3>NAD+ and Sirtuin Activation\u003C\u002Fh3>\n\u003Cp>Research investigating sirtuin enzymes has demonstrated their dependence on NAD+ as a substrate for their deacetylase activity. Studies indicated that sirtuins remove acetyl groups from target proteins while consuming NAD+ and producing nicotinamide and O-acetyl-ADP-ribose as byproducts.(5)\u003C\u002Fp>\n\u003Cp>Investigations examining SIRT1, the most extensively studied mammalian sirtuin, suggested its involvement in metabolic regulation, stress resistance, and longevity pathways. Research indicated that SIRT1 may deacetylate numerous substrates including PGC-1α, FOXO transcription factors, and p53, potentially influencing mitochondrial biogenesis, oxidative stress responses, and inflammatory signaling.(6)\u003C\u002Fp>\n\u003Cp>Studies exploring mitochondrial sirtuins suggested that SIRT3, localized primarily in mitochondria, may regulate mitochondrial protein acetylation and influence oxidative metabolism. Investigations into the relationship between NAD+ availability and sirtuin activity suggested that NAD+ levels may modulate sirtuin function.(7)\u003C\u002Fp>\n\u003Ch3>NAD+ Decline with Aging\u003C\u002Fh3>\n\u003Cp>Research investigating age-related changes in NAD+ levels has consistently demonstrated declines across multiple tissues and model organisms. Studies in rodents indicated that NAD+ concentrations in liver, skeletal muscle, adipose tissue, and brain tissue decreased significantly with advancing age, with some tissues showing reductions exceeding 50% between young and old animals.(8)\u003C\u002Fp>\n\u003Cp>Studies exploring mechanisms underlying NAD+ decline suggested multiple contributing factors. Research indicated that increased expression and activity of CD38, an NAD+-consuming enzyme, may contribute to age-related NAD+ depletion. Additional investigations suggested that decreased expression of NAD+ biosynthetic enzymes and increased NAD+ consumption by PARPs responding to accumulated DNA damage may also contribute.(9)\u003C\u002Fp>\n\u003Cp>Research examining consequences of age-related NAD+ decline suggested associations with mitochondrial dysfunction, reduced sirtuin activity, impaired cellular stress responses, and metabolic alterations. Studies indicated that these changes may contribute to various age-associated pathological conditions.(8)\u003C\u002Fp>\n\u003Ch3>NAD+ Precursors and Biosynthetic Pathways\u003C\u002Fh3>\n\u003Cp>Research has identified multiple pathways for NAD+ biosynthesis, utilizing different precursor molecules. Investigations into salvage pathways, which recycle NAD+ breakdown products, suggested these routes represent the primary mechanism for NAD+ maintenance in most tissues. Research indicated that nicotinamide mononucleotide (NMN) and nicotinamide riboside (NR) function as key intermediates, with specific enzymes catalyzing their conversion to NAD+.(10)\u003C\u002Fp>\n\u003Cp>Studies examining nicotinamide phosphoribosyltransferase (NAMPT), the rate-limiting enzyme in the salvage pathway from nicotinamide, suggested its critical role in maintaining NAD+ levels. Research indicated that NAMPT expression and activity may influence cellular NAD+ concentrations and downstream NAD+-dependent processes.(11)\u003C\u002Fp>\n\u003Cp>Investigations comparing different NAD+ precursors suggested varying efficacy in raising tissue NAD+ levels. Research indicated that NMN and NR, which bypass NAMPT in the biosynthetic pathway, may effectively increase NAD+ concentrations when administered exogenously.(3)\u003C\u002Fp>\n\u003Ch3>NAD+ and Mitochondrial Function\u003C\u002Fh3>\n\u003Cp>Research examining mitochondrial NAD+ has suggested its critical importance for oxidative metabolism. Studies indicated that mitochondrial NAD+ levels may influence the activity of NAD+-dependent dehydrogenases in the citric acid cycle and beta-oxidation pathways, potentially affecting mitochondrial ATP production capacity.(12)\u003C\u002Fp>\n\u003Cp>Studies examining NAD+ supplementation effects on mitochondrial function reported improvements in aged rodents. Research suggested that NAD+ precursor administration appeared to improve mitochondrial respiration capacity, increase mitochondrial protein content, and enhance oxidative metabolism in some tissues.(8)\u003C\u002Fp>\n\u003Ch3>NAD+ and Cardiovascular Function\u003C\u002Fh3>\n\u003Cp>Research examining NAD+ in cardiovascular tissues has suggested its involvement in cardiac metabolism and stress responses. Studies indicated that cardiac NAD+ levels may influence mitochondrial function and energy production in the metabolically demanding myocardium.(13)\u003C\u002Fp>\n\u003Cp>Studies examining vascular function suggested that NAD+-dependent pathways may influence endothelial cell function and vascular tone. Research indicated that SIRT1 activation in endothelial cells appeared to promote nitric oxide production and reduce inflammatory responses, potentially contributing to vascular health.(14)\u003C\u002Fp>\n\u003Cp>Investigations into age-related vascular dysfunction suggested that declining NAD+ levels might contribute to endothelial impairment. Research indicated that NAD+ precursor supplementation appeared to improve endothelial function and reduce arterial stiffness in aged animals.(15)\u003C\u002Fp>\n\u003Ch3>NAD+ and Skeletal Muscle Function\u003C\u002Fh3>\n\u003Cp>Research investigating skeletal muscle NAD+ has demonstrated its importance for muscle metabolism and function. Studies indicated that NAD+ levels in skeletal muscle decline with aging and may be reduced in various muscle pathologies.(16)\u003C\u002Fp>\n\u003Cp>Studies exploring NAD+ supplementation effects on muscle function reported improvements in aged animals. Research suggested that NAD+ precursor administration appeared to improve muscle mitochondrial function, increase muscle mass, and enhance exercise capacity in some experimental protocols. Investigations into muscle regeneration suggested that NAD+-dependent pathways may influence satellite cell function and muscle repair, with potential benefits for muscle stem cell activation.(17)\u003C\u002Fp>\n\u003Ch3>NAD+ and Neurodegenerative Processes\u003C\u002Fh3>\n\u003Cp>Research investigating NAD+ in neuronal function has suggested its importance for neuronal energy metabolism and stress resistance. Studies indicated that neurons, with their high energy demands and limited regenerative capacity, may be particularly vulnerable to NAD+ depletion.(18)\u003C\u002Fp>\n\u003Cp>Investigations into neurodegenerative disease models suggested potential protective effects of NAD+ restoration. Research in animal models of Alzheimer's disease indicated that NAD+ precursor supplementation appeared to reduce pathology, improve mitochondrial function, and enhance cognitive performance in some experimental paradigms.(18)\u003C\u002Fp>\n\u003Ch3>NAD+ Supplementation Strategies\u003C\u002Fh3>\n\u003Cp>Research investigating different approaches to increase NAD+ levels has examined various precursor molecules and administration routes. Studies comparing oral supplementation with NMN, NR, nicotinamide, and nicotinic acid suggested varying efficacy in raising tissue NAD+ concentrations.(19)\u003C\u002Fp>\n\u003Cp>Investigations into NMN supplementation indicated that oral administration appeared to increase NAD+ levels in multiple tissues in rodent studies. Research suggested that NMN may be absorbed and subsequently converted to NAD+ through tissue-specific pathways.(20)\u003C\u002Fp>\n\u003Cp>Studies examining NR supplementation suggested its ability to increase tissue NAD+ levels following oral administration. Research indicated that NR may utilize specific transporters for cellular uptake and is subsequently phosphorylated to form NMN, which is then converted to NAD+.(10)\u003C\u002Fp>\n\u003Cp>Investigations into human supplementation studies with NAD+ precursors have reported varying outcomes. Research indicated that NR and NMN supplementation appeared to increase blood NAD+ metabolite levels in humans, though tissue-specific effects and functional outcomes have shown variable results across studies.(19)\u003C\u002Fp>\n\u003Cp>Available for Research Purposes Only\u003C\u002Fp>\n\u003Cp>NAD+ and its precursors are available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.\u003C\u002Fp>\n\u003Ch2>References\u003C\u002Fh2>\n\u003Cp>1. Belenky P, Bogan KL, Brenner C. NAD+ metabolism in health and disease. Trends Biochem Sci. 2007;32(1):12-19.\u003C\u002Fp>\n\u003Cp>2. Verdin E. NAD+ in aging, metabolism, and neurodegeneration. Science. 2015;350(6265):1208-1213.\u003C\u002Fp>\n\u003Cp>3. Yoshino J, Baur JA, Imai SI. NAD+ Intermediates: The Biology and Therapeutic Potential of NMN and NR. Cell Metab. 2018;27(3):513-528.\u003C\u002Fp>\n\u003Cp>4. Ying W. NAD+\u002FNADH and NADP+\u002FNADPH in cellular functions and cell death: regulation and biological consequences. Antioxid Redox Signal. 2008;10(2):179-206.\u003C\u002Fp>\n\u003Cp>5. Imai S, Guarente L. NAD+ and sirtuins in aging and disease. Trends Cell Biol. 2014;24(8):464-471.\u003C\u002Fp>\n\u003Cp>6. Chang HC, Guarente L. SIRT1 and other sirtuins in metabolism. Trends Endocrinol Metab. 2014;25(3):138-145.\u003C\u002Fp>\n\u003Cp>7. Haigis MC, Sinclair DA. Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol. 2010;5:253-295.\u003C\u002Fp>\n\u003Cp>8. Gomes AP, Price NL, Ling AJ, et al. Declining NAD+ induces a pseudohypoxic state disrupting nuclear-mitochondrial communication during aging. Cell. 2013;155(7):1624-1638.\u003C\u002Fp>\n\u003Cp>9. Camacho-Pereira J, Tarragó MG, Chini CC, et al. CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism. Cell Metab. 2016;23(6):1127-1139.\u003C\u002Fp>\n\u003Cp>10. Bieganowski P, Brenner C. Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Preiss-Handler independent route to NAD+ in fungi and humans. Cell. 2004;117(4):495-502.\u003C\u002Fp>\n\u003Cp>11. Revollo JR, Grimm AA, Imai S. The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J Biol Chem. 2004;279(49):50754-50763.\u003C\u002Fp>\n\u003Cp>12. Yang Y, Sauve AA. NAD+ metabolism: Bioenergetics, signaling and manipulation for therapy. Biochim Biophys Acta. 2016;1864(12):1787-1800.\u003C\u002Fp>\n\u003Cp>13. Diguet N, Trammell SAJ, Tannous C, et al. Nicotinamide Riboside Preserves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy. Circulation. 2018;137(21):2256-2273.\u003C\u002Fp>\n\u003Cp>14. Mattagajasingh I, Kim CS, Naqvi A, et al. SIRT1 promotes endothelium-dependent vascular relaxation by activating endothelial nitric oxide synthase. Proc Natl Acad Sci U S A. 2007;104(37):14855-14860.\u003C\u002Fp>\n\u003Cp>15. de Picciotto NE, Gano LB, Johnson LC, et al. Nicotinamide mononucleotide supplementation reverses vascular dysfunction and oxidative stress with aging in mice. Aging Cell. 2016;15(3):522-530.\u003C\u002Fp>\n\u003Cp>16. Frederick DW, Loro E, Liu L, et al. Loss of NAD Homeostasis Leads to Progressive and Reversible Degeneration of Skeletal Muscle. Cell Metab. 2016;24(2):269-282.\u003C\u002Fp>\n\u003Cp>17. Zhang H, Ryu D, Wu Y, et al. NAD+ repletion improves mitochondrial and stem cell function and enhances life span in mice. Science. 2016;352(6292):1436-1443.\u003C\u002Fp>\n\u003Cp>18. Long AN, Owens K, Schlappal AE, Kristian T, Fishman PS, Schuh RA. Effect of nicotinamide mononucleotide on brain mitochondrial respiratory deficits in an Alzheimer's disease-relevant murine model. BMC Neurol. 2015;15:19.\u003C\u002Fp>\n\u003Cp>19. Martens CR, Denman BA, Mazzo MR, et al. Chronic nicotinamide riboside supplementation is well-tolerated and elevates NAD+ in healthy middle-aged and older adults. Nat Commun. 2018;9(1):1286.\u003C\u002Fp>\n\u003Cp>20. Mills KF, Yoshida S, Stein LR, et al. Long-Term Administration of Nicotinamide Mononucleotide Mitigates Age-Associated Physiological Decline in Mice. 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Tripeptide\u003C\u002Fh2>\n\u003Cp>KPV (Lys-Pro-Val) is a naturally occurring tripeptide derived from the C-terminal sequence of the anti-inflammatory hormone alpha-melanocyte stimulating hormone (α-MSH). This bioactive peptide has been investigated for its potential anti-inflammatory and immunomodulatory properties across various research models and tissue systems.\u003C\u002Fp>\n\u003Cp>KPV represents the smallest active fragment of α-MSH that retains anti-inflammatory activity. The tripeptide consists of three amino acids—lysine, proline, and valine—arranged in a specific sequence that appears critical for its biological activity. Research has explored KPV's potential mechanisms of action and therapeutic applications in inflammatory conditions.(1)\u003C\u002Fp>\n\u003Ch2>Overview\u003C\u002Fh2>\n\u003Cp>KPV has been extensively investigated for its anti-inflammatory properties independent of melanocortin receptor activation. Research indicates that KPV may exert its effects through multiple mechanisms, including modulation of inflammatory signaling pathways, inhibition of pro-inflammatory transcription factors, and direct effects on immune cell function.(2)\u003C\u002Fp>\n\u003Cp>Studies have demonstrated that KPV exhibits anti-inflammatory activity in various experimental models, including inflammatory bowel disease, dermatological conditions, and other inflammatory disorders. The peptide has been investigated for both systemic and topical applications, with research exploring optimal delivery methods and formulations.(3)\u003C\u002Fp>\n\u003Ch2>Chemical Makeup\u003C\u002Fh2>\n\u003Cp>Molecular Formula: C16H30N4O4\u003Cbr \u002F>\nMolecular Weight: 342.44 g\u002Fmol\u003Cbr \u002F>\nSequence: Lys-Pro-Val (H-KPV-OH)\u003Cbr \u002F>\nOther Known Titles: α-MSH(11-13), Melanocortin tripeptide\u003C\u002Fp>\n\u003Ch2>Research and Clinical Studies\u003C\u002Fh2>\n\u003Ch3>KPV and Anti-Inflammatory Mechanisms\u003C\u002Fh3>\n\u003Cp>Research examining KPV's anti-inflammatory mechanisms has suggested multiple pathways of action. Studies indicated that KPV may inhibit nuclear factor kappa B (NF-κB) translocation, a critical transcription factor involved in pro-inflammatory gene expression. Investigations demonstrated that KPV appeared to prevent NF-κB nuclear entry in activated immune cells, potentially reducing the expression of inflammatory cytokines.(4)\u003C\u002Fp>\n\u003Cp>Studies exploring intracellular mechanisms suggested that KPV may enter cells and exert direct intracellular effects. Research indicated that the peptide's anti-inflammatory activity may not depend entirely on cell surface receptor activation, distinguishing it from the parent hormone α-MSH, which primarily acts through melanocortin receptors.(5)\u003C\u002Fp>\n\u003Cp>Investigations into inflammatory mediator production suggested that KPV may reduce levels of pro-inflammatory cytokines including tumor necrosis factor-alpha (TNF-α), interleukin-1 beta (IL-1β), and interleukin-6 (IL-6). Research demonstrated dose-dependent reductions in these inflammatory markers across various cell types and experimental models.(6)\u003C\u002Fp>\n\u003Ch3>KPV and Inflammatory Bowel Disease\u003C\u002Fh3>\n\u003Cp>Research investigating KPV in inflammatory bowel disease (IBD) models has demonstrated potential therapeutic effects. Studies utilizing experimental colitis models indicated that KPV administration appeared to reduce intestinal inflammation, decrease disease severity scores, and improve histological outcomes.(7)\u003C\u002Fp>\n\u003Cp>Investigations examining oral and local administration routes suggested that KPV may exert beneficial effects on intestinal inflammation when delivered directly to affected tissues. Research indicated improvements in colonic inflammation markers, reduced immune cell infiltration, and preservation of intestinal barrier integrity in some experimental protocols.(8)\u003C\u002Fp>\n\u003Cp>Studies exploring KPV's effects on intestinal epithelial cells suggested potential protective mechanisms. Research indicated that the peptide may reduce epithelial cell apoptosis, enhance barrier function, and modulate tight junction protein expression, potentially contributing to improved intestinal homeostasis.(9)\u003C\u002Fp>\n\u003Ch3>KPV and Dermatological Applications\u003C\u002Fh3>\n\u003Cp>Research examining KPV in dermatological conditions has explored its potential for treating inflammatory skin disorders. Studies investigating contact dermatitis models indicated that topical KPV application appeared to reduce skin inflammation, decrease edema formation, and improve clinical inflammation scores.(10)\u003C\u002Fp>\n\u003Cp>Investigations into atopic dermatitis suggested that KPV may influence immune responses in skin tissue. Research demonstrated reductions in inflammatory cell infiltration, decreased expression of inflammatory markers, and improvements in skin barrier function parameters in some experimental models.(11)\u003C\u002Fp>\n\u003Cp>Studies exploring wound healing suggested that KPV may influence tissue repair processes. Research indicated potential effects on inflammatory phase regulation, with some investigations suggesting improved healing outcomes when KPV was incorporated into wound treatment protocols.(12)\u003C\u002Fp>\n\u003Ch3>KPV and Immune Cell Modulation\u003C\u002Fh3>\n\u003Cp>Research investigating KPV's effects on specific immune cell populations has demonstrated various immunomodulatory activities. Studies examining macrophages, key mediators of inflammatory responses, indicated that KPV appeared to shift macrophage polarization from pro-inflammatory M1 phenotypes toward anti-inflammatory M2 phenotypes.(13)\u003C\u002Fp>\n\u003Cp>Investigations into neutrophil function suggested that KPV may modulate neutrophil activation and migration. Research indicated potential effects on neutrophil chemotaxis and inflammatory mediator release, which may contribute to reduced tissue inflammation in various experimental models.(14)\u003C\u002Fp>\n\u003Cp>Studies exploring T cell responses suggested that KPV may influence lymphocyte activation and cytokine production. Research indicated potential modulatory effects on T helper cell differentiation and effector functions, though mechanisms appeared complex and context-dependent.(15)\u003C\u002Fp>\n\u003Ch3>KPV and Oxidative Stress\u003C\u002Fh3>\n\u003Cp>Research examining KPV's relationship with oxidative stress has suggested potential antioxidant properties. Studies indicated that KPV administration appeared to reduce markers of oxidative damage in some inflammatory models, including decreased lipid peroxidation and improved antioxidant enzyme activity.(16)\u003C\u002Fp>\n\u003Cp>Investigations into reactive oxygen species (ROS) production suggested that KPV may influence cellular redox balance. Research demonstrated reduced ROS generation in activated immune cells treated with KPV, potentially contributing to its anti-inflammatory effects through oxidative stress reduction.(17)\u003C\u002Fp>\n\u003Ch3>KPV Delivery and Formulation\u003C\u002Fh3>\n\u003Cp>Research investigating optimal delivery methods for KPV has explored various formulation strategies. Studies examining topical delivery indicated that appropriate vehicle selection and penetration enhancers may improve KPV's effectiveness in dermatological applications.(10)\u003C\u002Fp>\n\u003Cp>Investigations into oral delivery for intestinal applications suggested challenges related to peptide stability and absorption. Research explored protective formulations and targeted delivery systems designed to enhance KPV stability in the gastrointestinal environment and improve local bioavailability at sites of intestinal inflammation.(8)\u003C\u002Fp>\n\u003Cp>Studies examining nanoparticle and liposomal formulations suggested potential advantages for KPV delivery. Research indicated that encapsulation strategies may protect the peptide from degradation, enhance cellular uptake, and improve therapeutic efficacy in some experimental protocols.(18)\u003C\u002Fp>\n\u003Ch3>KPV and Melanocortin Receptor Independence\u003C\u002Fh3>\n\u003Cp>Research distinguishing KPV's mechanisms from melanocortin receptor-dependent pathways has provided important mechanistic insights. Studies utilizing melanocortin receptor antagonists indicated that KPV retained anti-inflammatory activity even when melanocortin receptors were blocked, suggesting receptor-independent mechanisms.(5)\u003C\u002Fp>\n\u003Cp>Investigations comparing KPV with full-length α-MSH demonstrated similar anti-inflammatory potency despite KPV's lack of melanocortin receptor binding affinity. Research suggested that KPV's ability to enter cells and act intracellularly may account for its melanocortin receptor-independent effects.(4)\u003C\u002Fp>\n\u003Ch3>KPV Structure-Activity Relationships\u003C\u002Fh3>\n\u003Cp>Research examining structural requirements for KPV's biological activity has investigated amino acid sequence importance and potential modifications. Studies exploring sequence variations indicated that the specific Lys-Pro-Val arrangement appeared critical for optimal anti-inflammatory activity, with altered sequences showing reduced potency.(1)\u003C\u002Fp>\n\u003Cp>Investigations into peptide modifications aimed at improving stability and bioavailability have explored various chemical alterations. Research examined D-amino acid substitutions, N-terminal modifications, and C-terminal amidation, with varying effects on peptide stability and biological activity.(19)\u003C\u002Fp>\n\u003Ch3>KPV Safety and Tolerability\u003C\u002Fh3>\n\u003Cp>Research investigating KPV's safety profile in preclinical models has generally indicated favorable tolerability. Studies examining acute and subchronic administration reported minimal adverse effects across various dose ranges and administration routes.(3)\u003C\u002Fp>\n\u003Cp>Investigations into potential systemic effects suggested that KPV, particularly when administered topically or locally, exhibited minimal systemic absorption and associated effects. Research indicated that the peptide's small size and specific delivery to target tissues may contribute to its favorable safety profile in experimental models.(20)\u003C\u002Fp>\n\u003Cp>Available for Research Purposes Only\u003C\u002Fp>\n\u003Cp>KPV tripeptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.\u003C\u002Fp>\n\u003Ch2>References\u003C\u002Fh2>\n\u003Cp>1. Brzoska T, Luger TA, Maaser C, Abels C, Böhm M. Alpha-melanocyte-stimulating hormone and related tripeptides: biochemistry, antiinflammatory and protective effects in vitro and in vivo, and future perspectives for the treatment of immune-mediated inflammatory diseases. Endocr Rev. 2008;29(5):581-602.\u003C\u002Fp>\n\u003Cp>2. Colombo G, Gatti S, Sordi A, et al. Production and effects of α-melanocyte-stimulating hormone during acute lung injury. Shock. 2007;27(3):326-333.\u003C\u002Fp>\n\u003Cp>3. Hiltz ME, Lipton JM. Antiinflammatory activity of a COOH-terminal fragment of the neuropeptide alpha-MSH. FASEB J. 1989;3(11):2282-2284.\u003C\u002Fp>\n\u003Cp>4. Kannengiesser K, Maaser C, Heidemann J, et al. Melanocortin-derived tripeptide KPV has anti-inflammatory potential in murine models of inflammatory bowel disease. Inflamm Bowel Dis. 2008;14(3):324-331.\u003C\u002Fp>\n\u003Cp>5. Getting SJ, Riffo-Vasquez Y, Pitchford S, et al. A role for MC3R in modulating lung inflammation. Pulm Pharmacol Ther. 2008;21(6):866-873.\u003C\u002Fp>\n\u003Cp>6. Galimberti D, Fenoglio C, Lovati C, et al. Serum MCP-1 levels are increased in mild cognitive impairment and mild Alzheimer's disease. Neurobiol Aging. 2006;27(12):1763-1768.\u003C\u002Fp>\n\u003Cp>7. Maaser C, Kannengiesser K, Specht C, et al. Crucial role of the melanocortin receptor MC1R in experimental colitis. Gut. 2006;55(10):1415-1422.\u003C\u002Fp>\n\u003Cp>8. Dalmasso G, Charrier-Hisamuddin L, Nguyen HT, Yan Y, Sitaraman S, Merlin D. PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation. Gastroenterology. 2008;134(1):166-178.\u003C\u002Fp>\n\u003Cp>9. Demers A, McNicoll N, Febbraio M, et al. Identification of the growth hormone-releasing peptide binding site in CD36: a photoaffinity cross-linking study. Biochem J. 2004;382(Pt 2):417-424.\u003C\u002Fp>\n\u003Cp>10. Böhm M, Apel M, Schiller M, et al. Effect of topical application of the melanocortin peptide [Nle4, D-Phe7]-alpha-MSH on experimentally-induced immediate and delayed type hypersensitivity in skin. Exp Dermatol. 2006;15(7):551-558.\u003C\u002Fp>\n\u003Cp>11. Raap U, Brzoska T, Sohl S, et al. Alpha-melanocyte-stimulating hormone inhibits allergic airway inflammation. J Immunol. 2003;171(1):353-359.\u003C\u002Fp>\n\u003Cp>12. Kapas S, Cammas FM, Hinson JP, Clark AJ. Agonist and receptor binding properties of adrenomedullin 22-52, the NH2-terminal truncating analog of human adrenomedullin. Endocrinology. 1996;137(6):2456-2461.\u003C\u002Fp>\n\u003Cp>13. Si J, Ge Y, Zhuang S, Wang LJ, Chen S, Gong R. Adrenocorticotropic hormone ameliorates acute kidney injury by steroidogenic-dependent and -independent mechanisms. Kidney Int. 2013;83(4):635-646.\u003C\u002Fp>\n\u003Cp>14. Luger TA, Scholzen TE, Brzoska T, Böhm M. New insights into the functions of alpha-MSH and related peptides in the immune system. Ann N Y Acad Sci. 2003;994:133-140.\u003C\u002Fp>\n\u003Cp>15. Catania A, Gatti S, Colombo G, Lipton JM. Targeting melanocortin receptors as a novel strategy to control inflammation. Pharmacol Rev. 2004;56(1):1-29.\u003C\u002Fp>\n\u003Cp>16. Ichiyama T, Sakai T, Catania A, Barsh GS, Furukawa S, Lipton JM. Systemically administered alpha-melanocyte-stimulating peptides inhibit NF-kappaB activation in experimental brain inflammation. Brain Res. 1999;836(1-2):31-37.\u003C\u002Fp>\n\u003Cp>17. Delgado R, Carlin A, Airaghi L, et al. Melanocortin peptides inhibit production of proinflammatory cytokines and nitric oxide by activated microglia. J Leukoc Biol. 1998;63(6):740-745.\u003C\u002Fp>\n\u003Cp>18. Hartmeyer M, Scholzen T, Becher E, Bhardwaj RS, Schwarz T, Luger TA. Human dermal microvascular endothelial cells express the melanocortin receptor type 1 and produce increased levels of IL-8 upon stimulation with alpha-melanocyte-stimulating hormone. J Immunol. 1997;159(4):1930-1937.\u003C\u002Fp>\n\u003Cp>19. Taherzadeh S, Sharma S, Chhajlani V, Gantz I, Rajora N, Demitri MT, Kelly L, Zhao H, Ichiyama T, Catania A, Lipton JM. alpha-MSH and its receptors in regulation of tumor necrosis factor-alpha production by human monocyte\u002Fmacrophages. Am J Physiol. 1999;276(5):R1289-R1294.\u003C\u002Fp>\n\u003Cp>20. Holloway PM, Durrenberger PF, Kashefi SN, et al. Both MC1 and MC3 receptors provide protection from cerebral ischemia-reperfusion-induced neutrophil recruitment and barrier disruption in vivo. 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Peptide\u003C\u002Fh2>\n\u003Cp>Semaglutide is a synthetic peptide that has been investigated in various research studies for its potential effects on glucose metabolism, body weight regulation, and cardiovascular parameters. The compound functions as a glucagon-like peptide-1 (GLP-1) receptor agonist with an extended half-life profile.\u003C\u002Fp>\n\u003Cp>Semaglutide is a synthetic analog of human GLP-1 composed of 31 amino acids with structural modifications designed to enhance pharmacokinetic properties. The peptide is approximately 94% homologous to native GLP-1 and incorporates specific amino acid substitutions to resist enzymatic degradation.(1)\u003C\u002Fp>\n\u003Ch2>Overview\u003C\u002Fh2>\n\u003Cp>Semaglutide has been investigated for its potential in metabolic regulation through its GLP-1 receptor agonism mechanism. Studies suggest that the peptide may stimulate insulin secretion from pancreatic beta cells in a glucose-dependent manner while modulating glucagon release. The compound appears to bind with GLP-1 receptors expressed throughout various tissues, potentially initiating signaling cascades that influence metabolic function.(2)\u003C\u002Fp>\n\u003Cp>Research has explored semaglutide's action across multiple physiological pathways. The peptide has been studied for its potential effects on glucose homeostasis, body weight regulation, appetite control, and cardiovascular function. Laboratory investigations indicate the compound may influence energy balance through both central and peripheral mechanisms.(3)\u003C\u002Fp>\n\u003Cp>Studies have suggested the peptide may enhance beta-cell function and improve markers of insulin sensitivity. The GLP-1 receptor activation appears to provide effects on glucose-dependent insulin secretion, appetite regulation through central pathways, and modulation of gastric motility.(4)\u003C\u002Fp>\n\u003Ch2>Chemical Makeup\u003C\u002Fh2>\n\u003Cp>\u003Cstrong>Molecular Formula:\u003C\u002Fstrong> C187H291N45O59\u003Cbr \u002F>\n\u003Cstrong>Molecular Weight:\u003C\u002Fstrong> 4113.58 g\u002Fmol\u003Cbr \u002F>\n\u003Cstrong>Other Known Titles:\u003C\u002Fstrong> GLP-1 analog, NN9535\u003C\u002Fp>\n\u003Ch2>Research and Clinical Studies\u003C\u002Fh2>\n\u003Ch3>Semaglutide Peptide and Glucose Metabolism\u003C\u002Fh3>\n\u003Cp>In research studies examining metabolic function, semaglutide was investigated for its potential effects on glucose regulation and insulin secretion. The compound appeared to enhance glucose-dependent insulin secretion, suggesting it may preferentially stimulate insulin release when blood glucose levels are elevated while maintaining a low risk of hypoglycemia during normoglycemic conditions.(5)\u003C\u002Fp>\n\u003Cp>Studies utilizing intravenous glucose tolerance tests indicated that semaglutide administration appeared to increase both first- and second-phase insulin secretion. Research suggested that first-phase insulin response increased approximately threefold, while second-phase response increased approximately twofold compared to control groups.(6)\u003C\u002Fp>\n\u003Cp>Investigations also suggested that semaglutide may reduce fasting and postprandial glucose concentrations. The peptide appeared to decrease glucagon levels in a glucose-dependent manner, potentially contributing to improved glucose regulation. Research indicated that 24-hour meal tests showed reduced overall glucose responses with semaglutide administration.(6)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Beta-Cell Function\u003C\u002Fh3>\n\u003Cp>A study examining beta-cell function markers in research models with type 2 diabetes investigated semaglutide's potential effects on pancreatic beta-cell responsiveness. The research suggested that maximal insulin secretory capacity appeared to increase following semaglutide treatment, as demonstrated through arginine stimulation tests under hyperglycemic conditions.(7)\u003C\u002Fp>\n\u003Cp>Researchers observed that semaglutide administration appeared to improve insulin secretion rates during graded glucose infusion tests. The compound appeared to increase beta-cell responsiveness to levels comparable to those observed in healthy research participants, suggesting potential protective or restorative effects on beta-cell function.(7)\u003C\u002Fp>\n\u003Cp>Research evaluating homeostatic model assessment indices suggested that semaglutide may improve HOMA-B (beta-cell function) while decreasing HOMA-IR (insulin resistance). Studies indicated that fasting proinsulin-to-insulin ratios, which are typically elevated in models with type 2 diabetes, appeared to decrease significantly with semaglutide treatment, supporting potential improvements in beta-cell function.(8)\u003C\u002Fp>\n\u003Cp>Investigations into the molecular mechanisms suggested that semaglutide may enhance glucose-dependent insulin biosynthesis and secretion through cAMP-dependent protein kinase A pathways. Research indicated the peptide may activate signaling pathways including PI3K\u002FPKA\u002FmTOR in beta cells, potentially promoting insulin synthesis and secretion.(9)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Appetite Regulation\u003C\u002Fh3>\n\u003Cp>Studies investigating appetite and energy intake suggested that semaglutide may reduce food consumption through multiple mechanisms. Research utilizing ad libitum meal tests indicated that semaglutide appeared to reduce energy intake by 24-39% compared to control groups across various study durations and doses.(10)\u003C\u002Fp>\n\u003Cp>Investigations examining participant-reported appetite ratings suggested that semaglutide may reduce hunger while increasing sensations of fullness and satiety. Research indicated improvements in overall appetite suppression scores, with participants reporting reduced prospective food consumption and better control of eating.(11)\u003C\u002Fp>\n\u003Cp>Studies exploring food preferences and cravings suggested that semaglutide may influence hedonic aspects of eating behavior. Research indicated that the compound appeared to reduce food cravings and alter preferences, with participants showing lower relative preference for high-fat, energy-dense foods.(12)\u003C\u002Fp>\n\u003Cp>Central nervous system research suggested that GLP-1 receptors in brain regions involved in appetite regulation may mediate semaglutide's effects on food intake. Studies indicated that the compound may access specific areas of the hypothalamus and brainstem, regions critical for controlling hunger and satiety.(13)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Body Weight Regulation\u003C\u002Fh3>\n\u003Cp>Research examining body weight changes suggested that semaglutide may influence weight through reduced energy intake as a primary mechanism. Long-term investigations spanning 68-208 weeks indicated substantial body weight reductions ranging from 9.8% to 15.2% depending on the dose and duration of administration.(14)\u003C\u002Fp>\n\u003Cp>Studies examining body composition suggested that semaglutide-induced weight loss appeared to derive predominantly from body fat mass rather than lean mass. Research indicated approximately a threefold greater reduction in fat mass compared to lean body mass, suggesting preferential fat loss.(12)\u003C\u002Fp>\n\u003Cp>Investigations into weight loss sustainability suggested that reductions continued over extended periods. Research indicated that weight loss plateaus were reached around 60-65 weeks of treatment, with sustained reductions maintained for up to 4 years in long-term studies.(15)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Gastric Emptying\u003C\u002Fh3>\n\u003Cp>Research examining gastric motility suggested complex temporal patterns of semaglutide's effects on gastric emptying. Initial studies indicated potential delays in gastric emptying after early doses, though longer-term investigations suggested these effects may diminish over time, potentially due to tachyphylaxis.(16)\u003C\u002Fp>\n\u003Cp>Studies utilizing paracetamol absorption tests as indirect measures of gastric emptying reported variable findings depending on treatment duration. Research indicated that while some early-phase delays were observed, longer treatment periods (20 weeks) showed minimal to no significant delays in overall gastric emptying when assessed over 5-hour periods.(17)\u003C\u002Fp>\n\u003Cp>Investigations in specific populations suggested that gastric emptying delays may persist in some contexts. Research in models with polycystic ovary syndrome indicated that semaglutide retained approximately 37% of solid meal content in the stomach after 4 hours compared to no retention in control groups.(18)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Cardiovascular Outcomes\u003C\u002Fh3>\n\u003Cp>Research examining cardiovascular parameters suggested that semaglutide may influence multiple markers relevant to cardiovascular health. Large-scale investigations including the SUSTAIN and SELECT trials evaluated cardiovascular outcomes in diverse populations.(19)\u003C\u002Fp>\n\u003Cp>The SUSTAIN-6 trial, conducted in research models with type 2 diabetes at high cardiovascular risk, suggested that semaglutide may reduce the rate of major adverse cardiovascular events. Research indicated significantly lower rates of cardiovascular death, nonfatal myocardial infarction, or nonfatal stroke compared to control groups.(20)\u003C\u002Fp>\n\u003Cp>The SELECT trial, investigating participants with overweight or obesity and established cardiovascular disease but without diabetes, suggested that semaglutide may reduce cardiovascular risk in non-diabetic populations. Research indicated a 20% reduction in major adverse cardiovascular events, with hazard ratios of 0.80 for the primary composite endpoint.(21)\u003C\u002Fp>\n\u003Cp>Investigations suggested that cardiovascular benefits appeared independent of baseline glycemic status. Research analyzing outcomes by baseline HbA1c levels indicated consistent cardiovascular risk reduction across the entire glycemic spectrum, including normoglycemic participants.(22)\u003C\u002Fp>\n\u003Cp>Studies examining the relationship between weight loss and cardiovascular outcomes suggested that benefits may extend beyond adiposity reduction alone. Research indicated that cardiovascular event reductions emerged early in trials, potentially suggesting mechanisms beyond weight loss magnitude.(23)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Lipid Metabolism\u003C\u002Fh3>\n\u003Cp>Research examining lipid parameters suggested that semaglutide may influence various aspects of lipid metabolism. Studies indicated potential reductions in total cholesterol, LDL cholesterol, and triglyceride levels with semaglutide administration.(24)\u003C\u002Fp>\n\u003Cp>Investigations suggested that systolic and diastolic blood pressure measurements appeared to decrease with semaglutide treatment. Research indicated clinically meaningful reductions in blood pressure that may contribute to overall cardiovascular risk reduction.(19)\u003C\u002Fp>\n\u003Cp>Studies examining inflammatory markers suggested that semaglutide may influence pro-inflammatory cytokine levels. Research indicated potential reductions in markers of oxidative stress and inflammation, though the mechanisms underlying these effects require further investigation.(9)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Renal Function\u003C\u002Fh3>\n\u003Cp>Research examining kidney function markers suggested that semaglutide may influence renal parameters. Studies indicated potential improvements in albuminuria and other markers of kidney function in research models with diabetes and chronic kidney disease.(25)\u003C\u002Fp>\n\u003Cp>Investigations suggested that semaglutide may reduce the risk of clinically important kidney outcomes. Research indicated potential benefits on composite renal endpoints including sustained decline in estimated glomerular filtration rate, progression to end-stage kidney disease, and death from kidney-related causes.(25)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Hepatic Parameters\u003C\u002Fh3>\n\u003Cp>Studies investigating liver function suggested that semaglutide may influence hepatic fat content and related parameters. Research indicated potential reductions in markers associated with metabolic dysfunction-associated steatotic liver disease.(26)\u003C\u002Fp>\n\u003Cp>Investigations examining liver enzymes suggested that semaglutide may improve transaminase levels in research models with elevated baseline values. Studies indicated improvements in hepatic steatosis markers and potential benefits for liver health.(26)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Tissue-Specific Effects\u003C\u002Fh3>\n\u003Cp>Research examining adipose tissue suggested that semaglutide may modulate white adipose tissue browning processes. Studies indicated potential upregulation of uncoupling protein 1 (UCP1) and other markers associated with thermogenic activity, though most supporting evidence derives from preclinical models.(9)\u003C\u002Fp>\n\u003Cp>Investigations into skeletal muscle suggested that semaglutide may influence glucose transport through AMPK\u002FSIRT1 activation and GLUT4 upregulation. Research indicated potential effects on mitochondrial biogenesis and anti-inflammatory pathways in muscle tissue.(9)\u003C\u002Fp>\n\u003Cp>Studies examining autophagy regulation suggested that semaglutide may influence cellular quality control mechanisms. Research indicated potential activation of autophagy pathways and upregulation of transcriptional responses to oxidative stress.(9)\u003C\u002Fp>\n\u003Ch3>Semaglutide Peptide and Molecular Signaling\u003C\u002Fh3>\n\u003Cp>Research investigating intracellular signaling pathways suggested that semaglutide activates multiple downstream cascades following GLP-1 receptor binding. Studies indicated that the compound may increase intracellular cyclic AMP levels through adenylate cyclase activation.(27)\u003C\u002Fp>\n\u003Cp>Investigations suggested that elevated cAMP levels may activate protein kinase A (PKA) and exchange protein directly activated by cAMP 2 (EPAC2). Research indicated these pathways may be essential for insulin release and beta-cell function, promoting both immediate insulin secretion and gene transcription changes that enhance beta-cell survival.(27)\u003C\u002Fp>\n\u003Cp>Studies examining cardiovascular tissues suggested that semaglutide may stimulate cardioprotective signaling pathways. Research indicated potential activation of PKG\u002FPKCε\u002FERK1\u002F2 pathways, potentially reducing ischemia-induced apoptosis in cardiomyocytes.(27)\u003C\u002Fp>\n\u003Ch2>Available for Research Purposes Only\u003C\u002Fh2>\n\u003Cp>Semaglutide peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.\u003C\u002Fp>\n\u003Chr \u002F>\n\u003Ch2>References\u003C\u002Fh2>\n\u003Col>\n\u003Cli>Lau J, Bloch P, Schäffer L, et al. Discovery of the Once-Weekly Glucagon-Like Peptide-1 (GLP-1) Analogue Semaglutide. J Med Chem. 2015;58(18):7370-7380.\u003C\u002Fli>\n\u003Cli>Nauck MA, Quast DR, Wefers J, Meier JJ. GLP-1 receptor agonists in the treatment of type 2 diabetes - state-of-the-art. Mol Metab. 2021;46:101102.\u003C\u002Fli>\n\u003Cli>Gabery S, Salinas CG, Paulsen SJ, et al. Semaglutide lowers body weight in rodents via distributed neural pathways. JCI Insight. 2020;5(6):e133429.\u003C\u002Fli>\n\u003Cli>Aroda VR, Blonde L, Pratley RE. A new era for oral peptides: SNAC and the development of oral semaglutide for the treatment of type 2 diabetes. Rev Endocr Metab Disord. 2022;23(5):979-994.\u003C\u002Fli>\n\u003Cli>Kapitza C, Nosek L, Jensen L, Hartvig H, Jensen CB, Flint A. Semaglutide, a once-weekly human GLP-1 analog, does not reduce the bioavailability of the combined oral contraceptive, ethinylestradiol\u002Flevonorgestrel. J Clin Pharmacol. 2015;55(5):497-504.\u003C\u002Fli>\n\u003Cli>Kapitza C, Zdravkovic M, Hindsberger C, Flint A. Semaglutide improves measures of beta-cell function in subjects with type 2 diabetes. Diabetologia. 2017;60(8):1390-1399.\u003C\u002Fli>\n\u003Cli>Hjerpsted JB, Flint A, Brooks A, Axelsen MB, Kvist T, Blundell J. Semaglutide improves postprandial glucose and lipid metabolism, and delays first-hour gastric emptying in subjects with obesity. Diabetes Obes Metab. 2018;20(3):610-619.\u003C\u002Fli>\n\u003Cli>Blonde L, Jendle J, Gross J, et al. Once-weekly dulaglutide versus bedtime insulin glargine, both in combination with liraglutide and metformin, in patients with type 2 diabetes (AWARD-4): a randomised, double-blind, phase 3 trial. Lancet. 2015;385(9982):2057-2066.\u003C\u002Fli>\n\u003Cli>Pappachan JM, Fernandez CJ, Chacko EC. Spotlight on the Mechanism of Action of Semaglutide. Curr Issues Mol Biol. 2024;46(12):13939-13952.\u003C\u002Fli>\n\u003Cli>Wilding JPH, Batterham RL, Davies M, et al. Weight regain and cardiometabolic effects after withdrawal of semaglutide: The STEP 1 trial extension. Diabetes Obes Metab. 2022;24(8):1553-1564.\u003C\u002Fli>\n\u003Cli>Friedrichsen M, Breitschaft A, Tadayon S, Wizert A, Skovgaard D. The effect of semaglutide 2.4 mg once weekly on energy intake, appetite, control of eating, and gastric emptying in adults with obesity. Diabetes Obes Metab. 2021;23(3):754-762.\u003C\u002Fli>\n\u003Cli>Blundell J, Finlayson G, Axelsen M, et al. Effects of once-weekly semaglutide on appetite, energy intake, control of eating, food preference and body weight in subjects with obesity. Diabetes Obes Metab. 2017;19(9):1242-1251.\u003C\u002Fli>\n\u003Cli>van Bloemendaal L, IJzerman RG, Ten Kulve JS, et al. GLP-1 receptor activation modulates appetite- and reward-related brain areas in humans. Diabetes. 2014;63(12):4186-4196.\u003C\u002Fli>\n\u003Cli>Wilding JPH, Batterham RL, Calanna S, et al. Once-Weekly Semaglutide in Adults with Overweight or Obesity. N Engl J Med. 2021;384(11):989-1002.\u003C\u002Fli>\n\u003Cli>Lincoff AM, Brown-Frandsen K, Colhoun HM, et al. Long-term weight loss effects of semaglutide in obesity without diabetes in the SELECT trial. Nat Med. 2024;30(6):1836-1844.\u003C\u002Fli>\n\u003Cli>Nauck MA, Meier JJ. The incretin effect in healthy individuals and those with type 2 diabetes: physiology, pathophysiology, and response to therapeutic interventions. Lancet Diabetes Endocrinol. 2016;4(6):525-536.\u003C\u002Fli>\n\u003Cli>Hjerpsted JB, Flint A, Brooks A, Axelsen MB, Kvist T, Blundell J. Semaglutide improves postprandial glucose and lipid metabolism, and delays first-hour gastric emptying in subjects with obesity. Diabetes Obes Metab. 2018;20(3):610-619.\u003C\u002Fli>\n\u003Cli>Jensterle M, Rizzo M, Haluzik M, Janez A. Semaglutide delays 4-hour gastric emptying in women with polycystic ovary syndrome and obesity. Diabetes Obes Metab. 2023;25(4):975-984.\u003C\u002Fli>\n\u003Cli>Marso SP, Bain SC, Consoli A, et al. Semaglutide and Cardiovascular Outcomes in Patients with Type 2 Diabetes. N Engl J Med. 2016;375(19):1834-1844.\u003C\u002Fli>\n\u003Cli>Marso SP, Daniels GH, Brown-Frandsen K, et al. Liraglutide and Cardiovascular Outcomes in Type 2 Diabetes. N Engl J Med. 2016;375(4):311-322.\u003C\u002Fli>\n\u003Cli>Lincoff AM, Brown-Frandsen K, Colhoun HM, et al. Semaglutide and Cardiovascular Outcomes in Obesity without Diabetes. N Engl J Med. 2023;389(24):2221-2232.\u003C\u002Fli>\n\u003Cli>Lingvay I, Deanfield J, Kahn SE, et al. Semaglutide and Cardiovascular Outcomes by Baseline HbA1c and Change in HbA1c in People With Overweight or Obesity but Without Diabetes in SELECT. Diabetes Care. 2024;47(8):1360-1369.\u003C\u002Fli>\n\u003Cli>Lincoff AM, Deanfield J, Kahn SE, et al. Semaglutide and cardiovascular outcomes by baseline and changes in adiposity measurements: a prespecified analysis of the SELECT trial. Lancet. 2025;405(10455):935-947.\u003C\u002Fli>\n\u003Cli>Nauck MA, Muus Ghorbani ML, Kreiner E, Saevereid HA, Buse JB; PIONEER 4 investigators. Effects of semaglutide on beta-cell function and glycaemic control in participants with type 2 diabetes. Diabetologia. 2019;62(5):808-818.\u003C\u002Fli>\n\u003Cli>Perkovic V, Tuttle KR, Rossing P, et al. Effects of Semaglutide on Chronic Kidney Disease in Patients with Type 2 Diabetes. N Engl J Med. 2024;391(2):109-121.\u003C\u002Fli>\n\u003Cli>Newsome PN, Buchholtz K, Cusi K, et al. A Placebo-Controlled Trial of Subcutaneous Semaglutide in Nonalcoholic Steatohepatitis. N Engl J Med. 2021;384(12):1113-1124.\u003C\u002Fli>\n\u003Cli>Drucker DJ. Mechanisms of Action and Therapeutic Application of Glucagon-like Peptide-1. Cell Metab. 2018;27(4):740-756.\u003C\u002Fli>\n\u003C\u002Fol>\n","TLP-SEMA-10MG","94",[],18,"yes",{"length":61,"width":61,"height":61},[],[],[915],{"id":76,"name":77,"slug":78},[],[918],{"id":919,"name":900,"slug":901},73,[921,922],{"id":83,"date_created":84,"date_created_gmt":84,"date_modified":85,"date_modified_gmt":85,"src":86,"name":87,"alt":61,"srcset":88,"sizes":89,"thumbnail":90},{"id":923,"date_created":924,"date_created_gmt":924,"date_modified":924,"date_modified_gmt":924,"src":925,"name":926,"alt":61,"srcset":927,"sizes":217,"thumbnail":928},3044,"2026-02-03T22:47:37","https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d.png","be166d19b503e2b5172d","https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-200x295.png 200w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-203x300.png 203w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-400x590.png 400w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-500x738.png 500w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-600x885.png 600w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-694x1024.png 694w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-700x1033.png 700w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-768x1133.png 768w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-800x1180.png 800w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-1041x1536.png 1041w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-1200x1770.png 1200w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-1388x2048.png 1388w, https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d.png 1600w","https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-content\u002Fuploads\u002F2025\u002F12\u002Fbe166d19b503e2b5172d-500x738.png",[930],{"id":64,"name":93,"slug":93,"position":64,"visible":63,"variation":63,"options":931},[282],[933],{"id":64,"name":93,"option":282},[935],2942,[],"\u003Cspan class=\"woocommerce-Price-amount amount\">\u003Cbdi>\u003Cspan class=\"woocommerce-Price-currencySymbol\">$\u003C\u002Fspan>94.00\u003C\u002Fbdi>\u003C\u002Fspan>",[105,172,315,104,289],[940,943,946,948,950,952],{"id":941,"key":116,"value":942},8839,{"slider_visibility":118,"slider_type":69,"wooslider":119,"page_title_bar":120},{"id":944,"key":123,"value":945},8841,"117",{"id":947,"key":127,"value":111},8842,{"id":949,"key":130,"value":245},8843,{"id":951,"key":134,"value":617},9689,{"id":953,"key":110,"value":111},9691,{"self":955,"collection":960},[956],{"href":957,"targetHints":958},"https:\u002F\u002Fapi.tlpeptides.com\u002Fwp-json\u002Fwc\u002Fv3\u002Fproducts\u002F2777",{"allow":959},[145,146,147,148,149],[961],{"href":152},1781040691243]