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A consolidated summary of published, peer-reviewed research — emphasizing preclinical and non-human studies — for every compound in the catalog. These are references to the scientific literature, not statements of efficacy for any product.
All compounds are supplied for laboratory research use only. Nothing here describes human use, dosing, or therapeutic benefit; findings in animal and cell models do not establish effects in humans.
Examined BPC-157 in a rat Achilles-tendon transection model paired with cultured tendon fibroblasts and identified dose-dependent activation of the focal adhesion kinase (FAK)–paxillin signaling cascade, which is involved in cell migration and survival.
Model: Sprague-Dawley rat Achilles model + cultured fibroblasts | Source
After sharp transection of the Achilles tendon from bone, BPC-157 improved functional, biomechanical (load-to-failure, stiffness), and histological healing (better collagen organization, more type-I collagen) versus controls, and offset corticosteroid-impaired healing.
Model: Rat tendon-to-bone healing | Source
A single intraperitoneal dose of BPC-157 was reported to improve the healing course of spinal-cord injury and support functional (tail) recovery relative to controls.
Model: Wistar rat spinal-cord-injury model | Source
cDNA-microarray work found growth-hormone receptor among the most up-regulated genes in BPC-157-treated tendon fibroblasts, with dose- and time-dependent increases at mRNA and protein levels; added growth hormone increased fibroblast proliferation.
Model: Rat Achilles tendon fibroblasts (in vitro) | Source
In a rat sciatic-nerve transection model, BPC-157 produced faster axonal regeneration (denser, larger fibers; thicker myelin), higher motor action potentials on EMG, and an improved sciatic functional index, with autotomy absent versus controls.
Model: Rat sciatic-nerve transection | Source
Synthesizes rat studies in which BPC-157 supported healing of numerous gastrointestinal anastomoses (esophagogastric, colocolonic, jejunoileal, ileoileal) and counteracted associated colitis, short-bowel, and sphincter dysfunction.
Model: Rat gastrointestinal anastomosis models | Source
BPC-157 counteracted combined gastrointestinal, liver, and brain toxicity induced by the NSAID diclofenac in rats, whether given intraperitoneally or orally in drinking water — consistent with its cytoprotective profile.
Model: Rat NSAID-toxicity model | Source
Research stage: Evidence base is overwhelmingly preclinical (primarily rat models); robust human efficacy trials have not been completed.
A fragment of the regenerative protein Thymosin β-4, studied for its role in cell migration and angiogenesis. Preclinical work spans cardiac-repair, wound-healing, and hair-follicle models.
Mechanism: Corresponds to the actin-binding region (LKKTETQ) of Thymosin Beta-4, a regenerative protein in most cell types. The literature links it to G-actin regulation, cell migration, and angiogenesis (VEGF, HIF-1α).
A landmark study reporting that Thymosin Beta-4 activated integrin-linked kinase, promoted cardiac cell migration and survival, and supported cardiac repair after simulated myocardial infarction (reducing infarct size in mice).
Model: Mouse myocardial-infarction model | Source
Established that Thymosin Beta-4 stimulates directed migration of human umbilical-vein endothelial cells — the mechanistic foundation for subsequent angiogenesis research.
Model: Human endothelial cell culture (in vitro) | Source
Model: Rat / mouse wound and ocular models | Source
Using Tβ4-overexpressing and knockout mice, hair regrew faster in overexpressing mice (more follicles entering anagen, more shafts) and slower in knockouts, with elevated VEGF and P38/ERK/AKT signaling — evidence that normal Tβ4 is required for typical hair cycling.
Model: Transgenic and knockout mouse hair model | Source
Research stage: Evidence base is overwhelmingly preclinical (primarily rat models); robust human efficacy trials have not been completed.
Mechanism: A naturally occurring copper-binding tripeptide that declines with age. Studied extensively for collagen/elastin synthesis, extracellular-matrix remodeling, and broad gene-expression modulation.
GHK-Cu stimulated collagen synthesis in cultured fibroblasts at concentrations as low as 10⁻¹² M, peaking near 10⁻⁹ M, independent of changes in cell number.
Model: Cultured fibroblasts (in vitro) | Source
In a rat wound-chamber model, GHK-Cu produced concentration-dependent increases in type-I and type-III collagen mRNA (about twice the stimulation of non-collagen proteins) without corresponding TGF-beta mRNA increases.
Model: Rat wound-chamber model | Source
Profiling of human fibroblast cultures found GHK significantly modulated expression of roughly 4,699 genes — up-regulating tissue-repair and remodeling genes while down-regulating genes tied to inflammation and fibrosis.
Model: Human fibroblast cultures (in vitro) | Source
A review synthesizing the gene-level data, including Broad Institute Connectivity-Map findings that GHK-Cu influences DNA-repair and tissue-remodeling gene programs.
Model: Review of preclinical / gene-expression data | Source
A multi-institution study found GHK reversed the gene-expression signature of emphysema/COPD across 127 disease-associated genes; in vitro, GHK restored the ability of COPD-patient lung fibroblasts to contract and remodel collagen gel to near-normal levels.
Model: Human lung fibroblasts + gene-expression analysis | Source
Research stage: Deep preclinical and mechanistic base; limited controlled human data exists in dermatology (topical), outside the research-use context.
A synthetic analog of growth-hormone-releasing hormone studied in secretagogue-pathway research. It is characterized by a short, pulse-like profile that models natural GH-axis signaling.
Mechanism: A synthetic analog of growth-hormone-releasing hormone (GHRH). The ‘no-DAC’ form (Modified GRF 1-29) resists DPP-IV degradation with a short, pulse-like profile; it binds the GHRH receptor on pituitary somatotrophs, raising cAMP and priming GH synthesis.
Demonstrated that simultaneous stimulation of the GHRH-receptor and ghrelin-receptor pathways produces a synergistic GH response greater than the sum of the individual responses — the mechanistic basis for pairing a GHRH analog with a secretagogue.
Model: Somatotroph / GH-axis research | Source
Pharmacokinetic characterization of the DAC-modified analog reported an extended half-life of roughly 5.8–8.1 days via albumin binding; the no-DAC form, by contrast, is characterized by a ~30-minute half-life that mimics natural pulsatility.
Model: Pharmacokinetic study (human PK reference) | Source
Research stage: Published characterization centers on GHRH-analog pharmacology and pharmacokinetics; combination-protocol efficacy data are limited.
A selective growth-hormone secretagogue studied at the ghrelin / GHS receptor. Preclinical rodent work distinguishes it by releasing GH with minimal cortisol or prolactin effect.
Mechanism: A synthetic pentapeptide agonist at the ghrelin / growth-hormone-secretagogue receptor (GHS-R1a). Notable within its class for selectivity — stimulating GH release with minimal cortisol or prolactin effect.
The foundational study: ipamorelin produced robust GH release in rats comparable to GHRP-6, but with significantly lower cortisol and ACTH responses — establishing its selective profile.
Model: Rat GH-release model | Source
Chronic ipamorelin administration increased longitudinal bone growth and body-weight gain in rats, supporting sustained GH-axis engagement.
Model: Rat model (chronic administration) | Source
Across the secretagogue literature, ipamorelin is repeatedly distinguished from earlier GHRPs (GHRP-2, GHRP-6, hexarelin) by releasing GH without the off-target cortisol and prolactin elevation those compounds produce.
Model: Rodent GH-axis comparison studies | Source
Research stage: Selectivity and GH-axis effects are well documented preclinically in rodents.
A mitochondrial-derived peptide studied in metabolic-regulation and exercise-physiology models. Rodent studies have examined its effects on insulin sensitivity, AMPK signaling, and physical performance with age.
Mechanism: A 16-amino-acid peptide encoded within the mitochondrial 12S rRNA gene. Proposed to act largely on skeletal muscle, inhibiting the folate one-carbon cycle to activate AMPK, with downstream effects on glucose uptake and lipid handling.
The foundational MOTS-c paper: intraperitoneal MOTS-c improved insulin sensitivity in diet-induced obese mice, reduced age-related insulin resistance in older mice, and increased skeletal-muscle glucose uptake, with AMPK activation identified as the mechanism.
Model: Diet-induced obese and aged mice + myocytes | Source
An unbiased metabolomics approach found MOTS-c reduced sphingolipid, monoacylglycerol, and dicarboxylate pathways (elevated in obesity/T2D models) and increased beta-oxidation, improving insulin sensitivity in diet-induced obese mice.
Model: Diet-induced obese mice (metabolomics) | Source
MOTS-c significantly enhanced physical performance in young (2-mo), middle-aged (12-mo), and old (22-mo) mice; late-life (23.5-mo) intermittent treatment increased physical capacity and healthspan, alongside regulation of nuclear metabolism/proteostasis genes.
Model: Young, middle-aged, and aged mice (treadmill / healthspan) | Source
Found MOTS-c reduced myostatin and muscle-atrophy signaling in skeletal muscle, complementing reports that MOTS-c improves muscle strength and exercise capacity in high-fat-diet-fed and aged mice.
Model: High-fat-diet-fed and aged mice | Source
MOTS-c levels fell with aging in islet cells; treating aged mouse islets with MOTS-c reduced β-cell senescence and improved glucose intolerance in diabetic-mouse models.
Model: Aged and diabetic mouse islet models | Source
Research stage: Mechanism replicated across rodent and cell-line studies; circulating MOTS-c declines with age in humans, but no administered-MOTS-c human study has read out.
A mitochondria-targeting tetrapeptide studied for its association with cardiolipin and inner-membrane function. Preclinical models span cardiac, renal, pulmonary, and skeletal-muscle bioenergetics.
Mechanism: A mitochondria-targeting tetrapeptide that selectively accumulates in the inner mitochondrial membrane, binding the phospholipid cardiolipin. This is proposed to stabilize cristae structure, reduce reactive-oxygen-species production, and support ATP output.
Summarizes preclinical protective and restorative effects across models of heart failure, neurodegeneration, ischemia–reperfusion injury, metabolic syndromes, and muscle atrophy, tied to cardiolipin stabilization and reduced oxidative stress.
Model: Review of cell and animal disease models | Source
In a bleomycin-induced mouse model, SS-31 significantly suppressed pulmonary fibrosis and inflammation — improving histology and reducing extracellular-matrix deposition — by inhibiting NLRP3-inflammasome activation in macrophages.
Model: Bleomycin-induced mouse model | Source
In aged mice, SS-31 reversed age-related declines in skeletal-muscle mitochondrial function — restoring ATP production, oxidative-phosphorylation coupling, and cellular energy state — and improved fatigue resistance, with no observable effect in young mice.
Model: Aged vs. young mouse skeletal muscle | Source
In 26-month-old mice treated for 8 weeks (3 mg/kg/day), SS-31 reversed the age-related decline in maximum mitochondrial ATP production, improved OXPHOS coupling, restored redox homeostasis, and increased exercise tolerance — without increasing mitochondrial content.
Model: Aged C57BL/6 mice (8-week treatment) | Source
SS-31 reduced oxidative damage and preserved renal function in ischemia-reperfusion models, protecting mitochondria during the reperfusion window when reactive-oxygen-species generation peaks.
Model: Animal renal ischemia-reperfusion models | Source
A short course of SS-31 in advanced-age mice improved glomerular architecture — reducing podocyte-injury markers, improving cytoskeletal integrity, and raising glomerular endothelial-cell density.
Model: Advanced-age mouse kidney | Source
Research stage: Extensive multi-species preclinical base; SS-31/Elamipretide has also advanced into sponsored human clinical programs outside the research-use context.
A foundational metabolic coenzyme central to cellular energy and sirtuin biology. Animal and cell studies have examined NAD+ repletion in the context of mitochondrial function and aging research.
Mechanism: A central metabolic coenzyme and required cofactor for the sirtuin and PARP enzyme families. NAD+ levels decline with age, which the literature links to reduced sirtuin activity and mitochondrial function.
Reported that NAD+ repletion improved mitochondrial and stem-cell function and enhanced life span in mice — a widely cited demonstration of NAD+’s role in aging biology.
Model: Aged mouse model | Source
Showed NAD+ levels are reduced in aged mice and C. elegans, and that genetic or pharmacological restoration of NAD+ prevents age-associated decline through mitochondrial-UPR and FOXO signaling.
Model: Mouse and C. elegans models | Source
Found the NAD+ intermediate NMN addressed the pathophysiology of diet- and age-induced diabetes in mice, restoring NAD+ and improving glucose metabolism.
Model: Diet- and age-induced diabetic mice | Source
Reported that declining NAD+ induces a pseudohypoxic state that disrupts nuclear-mitochondrial communication during aging, reversible by raising NAD+.
Model: Mouse aging model | Source
Reported that impairment of an endothelial NAD+/H2S signaling network is a reversible cause of vascular aging — raising NAD+ (with NMN) plus exercise restored the capacity to generate new blood vessels in aged mice.
Model: Aged mouse vasculature | Source
In aged (85-week) mice, combined NMN supplementation (300 mg/kg/day) plus aerobic exercise significantly improved maximal strength and aerobic endurance versus aged sedentary controls, with changes in NAMPT and SIRT1 expression.
Model: Aged C57BL/6J mice (NMN + exercise) | Source
Research stage: Foundational NAD+ biology is established in animal and cell models; much intervention data uses precursors (NMN, NR) rather than NAD+ directly.
Composition: TB-500 11 mg · BPC-157 11 mg · GHK-Cu 75 mg
GLOW combines three of the compounds documented above in a single vial. Its research basis is the combined preclinical literature for its three components — refer to the individual TB-500, BPC-157, and GHK-Cu summaries. No published study evaluates this specific three-peptide combination as a single formulation.
A triple-receptor agonist peptide (GLP-1 / GIP / glucagon) studied as a next-generation metabolic-research compound. Published work includes in-vitro receptor characterization and preclinical obese-mouse models.
Mechanism: A single synthetic peptide that agonizes three metabolic receptors — GLP-1R, GIPR, and glucagon (GCGR) — combining incretin signaling with glucagon-pathway effects on hepatic fuel handling and energy expenditure.
The discovery and characterization paper: in vitro, LY3437943 showed balanced GCGR/GLP-1R activity with greater GIPR activity; in obese mice, administration decreased body weight and improved glycemic control.
Model: In vitro receptor assays + obese mice | Source
Established the rationally designed monomeric triple-agonist concept, showing a single peptide activating all three receptors corrected obesity and diabetes in rodents — the scientific rationale retatrutide builds on.
Model: Rodent obesity/diabetes models | Source
On the basis of cell-culture assays, retatrutide is characterized as less potent than the endogenous ligands at the human glucagon and GLP-1 receptors (about 0.3× and 0.4×) and more potent at the human GIP receptor (by roughly 8.9×) — defining its imbalanced triple-agonist profile.
Model: Human receptor cell-culture assays (in vitro) | Source
In diet-induced obese (C57BL/6J) mice, retatrutide-mediated weight loss was studied for its effect on pancreatic ductal adenocarcinoma and lung adenocarcinoma progression.
Model: Diet-induced obese mouse cancer models | Source
Research stage: Preclinical characterization exists; retatrutide’s most prominent published data are human phase-2 obesity trials conducted by its developer, outside the research-use context.
Source links resolve to the primary record (PubMed, PMC, or the journal). This reference is for internal and educational use in a research context. It is not medical advice, not an efficacy claim, and not a representation that any compound is safe or effective for human or veterinary use. All products are for laboratory research use only.
All products ship as lyophilized (freeze-dried) powder only. No liquids included. All products are intended for research purposes only. Not intended to diagnose, treat, cure, or prevent any disease. Not approved by the FDA for human consumption. Consult a qualified healthcare professional before use. Not for sale to individuals under 18.
