How to read this library.
Each compound section follows the same structure: Identity — sequence, class, primary research domain. Mechanism — receptor or molecular target, the primary signaling cascade, and the key downstream effectors documented in the literature. Pathway diagram — a simplified inline schematic of the canonical signaling axis. Preclinical evidence — selected primary citations with PubMed or PMC identifiers. Storage and reconstitution context — typical handling per published protocol literature.
Where a citation is referenced in the body, it is also indexed at the bottom under Full reference index with a stable PMID/PMCID/DOI. Researchers are encouraged to verify each claim against the cited source. If you find an error, please email [email protected].
Nothing here is medical advice. Nothing here describes human dosing, human use, or therapeutic application. All material is intended for in-vitro and non-clinical laboratory research conducted by qualified investigators 21 or older.
Terms used on this page.
A regulatory designation. Material sold "RUO" is a research reagent — not a food, drug, supplement, or cosmetic. It cannot legally be marketed for human use.
"In vitro" = in a dish (cell culture). "In vivo" = in a living organism, typically a rodent in preclinical work. Both are pre-human research.
A receptor is a protein on or inside a cell that binds a specific molecule. GPCR = G-protein-coupled receptor (a major class). RTK = receptor tyrosine kinase (another class). Different receptor types use different intracellular signaling.
When a receptor is activated, it triggers a chain of internal reactions ("cascade") that ultimately changes gene expression or cell behavior. cAMP/PKA, PI3K/Akt, MAPK/ERK are common cascades.
How a molecule moves through a system over time — absorption, distribution, metabolism, elimination. "Half-life" is how long it takes for half a dose to clear.
A document verifying a batch's identity (mass spec) and purity (HPLC). Every X Factor lot ships with the supplier's per-lot certificate of analysis (reversed-phase HPLC purity and LC-MS identity confirmation).
Freeze-dried into a stable powder for shipping. Researchers reconstitute lyophilized peptide in bacteriostatic water before use in their experiments.
Stable identifiers for primary literature. PMID = PubMed ID. PMCID = PubMed Central ID (full text often free). DOI = digital object identifier.
BPC-157
Body Protection Compound — a synthetic 15-amino-acid sequence derived from a partial sequence of a protein found in human gastric juice. Studied extensively in rodent injury, inflammation, and gastrointestinal models since the early 1990s by Sikiric and colleagues at the University of Zagreb.
- Sequence: Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val (15 aa)
- Origin: partial sequence of a protein isolated from human gastric juice
- Stability: reportedly stable in human gastric juice >24h [1]
- Primary domains: GI cytoprotection · tendon & muscle injury models · vasomotor research
Mechanism of action
Published preclinical literature documents BPC-157 modulating VEGFR2 → Akt → eNOS and Src → Caveolin-1 → eNOS signaling axes, leading to nitric-oxide production, vasodilation, and angiogenesis in cell-culture and rodent models. Hsieh et al. (2020, Scientific Reports) demonstrated that BPC-157 enhances expression and endocytosis of VEGFR2 with subsequent phosphorylation of AKT and eNOS, supporting both VEGF-dependent and VEGF-independent NO pathways [2]. Sikiric and colleagues have published extensively on the NO-system relationship, showing nitric-oxide modulation contributes to BPC-157's healing effect across multiple tissue-injury models [3,4].
Additional preclinical work documents upregulation of growth-factor receptors at injury sites [5], fibroblast and tendon-cell migration via FAK-paxillin signaling [6], and effects on dopaminergic and serotonergic systems in CNS models [4]. A 2025 narrative review in Pharmaceuticals by Józwiak et al. summarizes the multifunctionality and patent landscape [7].
Canonical signaling diagram
Selected preclinical evidence
- Sikiric P, et al. Novel cytoprotective mediator BPC 157 — vascular recruitment and gastrointestinal tract healing. Curr Pharm Des (2018). [1]PMID 29879879 →
- Hsieh MJ, et al. Modulatory effects of BPC 157 on vasomotor tone & Src-Cav-1-eNOS pathway. Sci Rep 10:17078 (2020). [2]DOI 10.1038/s41598-020-74022-y →
- Sikiric P, et al. BPC 157 — Robert's stomach cytoprotection / adaptive cytoprotection. Curr Pharm Des 26(25):2855-2866 (2020). [3]PMCID PMC7096228 →
- Sikiric P, et al. Pentadecapeptide BPC 157 and the central nervous system. Neural Regen Res 17(3):482-487 (2022). [4]PMCID PMC8504390 →
- Chang CH, et al. BPC 157 promotes tendon-fibroblast outgrowth. J Appl Physiol (2011). [5]PMID 21030672 →
- Sikiric P, et al. Stable gastric pentadecapeptide BPC 157 and wound healing. Front Pharmacol 12:627533 (2021). [6]DOI 10.3389/fphar.2021.627533 →
- Józwiak M, et al. Multifunctionality and possible medical application of the BPC 157 peptide — literature and patent review. Pharmaceuticals 18(2):185 (2025). [7]DOI 10.3390/ph18020185 →
- Sikiric P, et al. BPC 157 therapy: targeting angiogenesis and NO's cytotoxic vs protective actions (Comment). Pharmaceuticals (2025). [8]PMCID PMC12567428 →
Storage & reconstitution literature
Lyophilized peptide is typically stored at −20 °C, light-protected. Reconstitution, handling, and stability parameters are determined by the end researcher; we provide no reconstitution, use-window, or dosing guidance. Repeated freeze-thaw cycles are generally avoided for peptide reference standards.
TB-500 (Thymosin-β4 active fragment)
Synthetic peptide containing the active actin-binding motif (LKKTETQ) of the 43-amino-acid protein thymosin-β4 — the principal G-actin sequestering molecule in mammalian cells. Studied since the 1980s in cell-migration, wound-healing, and cardiac-injury models.
- Active motif: LKKTETQ (within the parent 43-aa Tβ4)
- Class: intracellular actin-sequestering peptide; β-thymosin family
- Domains: wound-healing models · cardiac-cell migration · ligament/tendon repair models
Mechanism of action
Thymosin-β4 sequesters monomeric G-actin at a 1:1 stoichiometry through the LKKTETQ motif, regulating the G/F-actin equilibrium and influencing cytoskeletal dynamics, cell migration, and tissue-remodeling processes [9,10]. Beyond actin sequestration, preclinical literature documents activation of integrin-linked kinase (ILK), modulation of NF-κB pathways, and upregulation of VEGF expression in angiogenesis models [11].
Bock-Marquette et al. (2004, Nature) demonstrated that Tβ4 activates ILK and Akt, promoting cardiac cell migration and survival in a rodent myocardial infarction model [11]. Malinda et al. (1999, J Invest Dermatol) reported topical or intraperitoneal Tβ4 increased re-epithelialization by 42% at day 4 and 61% at day 7 versus saline controls in a rat full-thickness wound model [12]. Goldstein et al. (2012) provide a comprehensive mechanistic review [10].
Canonical signaling diagram
Selected preclinical evidence
- Goldstein AL, Hannappel E, Kleinman HK. Thymosin β4: actin-sequestering protein moonlights to repair injured tissues. Trends Mol Med 11(9):421-9 (2005). [9]PMID 16099219 →
- Goldstein AL, et al. Thymosin β4: a multifunctional regenerative peptide. Ann NY Acad Sci 1270:1-9 (2012). [10]PMID 23050815 →
- Bock-Marquette I, et al. Thymosin β4 activates ILK and promotes cardiac repair. Nature 432:466-472 (2004). [11]PMID 15565145 →
- Malinda KM, et al. Thymosin β4 accelerates wound healing. J Invest Dermatol 113(3):364-368 (1999). [12]PMID 10469335 →
- Smart N, et al. Thymosin β4 induces adult epicardial progenitor mobilization and neovascularization. Nature (2007). [13]PMID 17108969 →
GHK-Cu
Glycyl-L-histidyl-L-lysine bound to a copper(II) ion. Naturally occurring in human plasma; isolated by Loren Pickart in 1973 while studying age-related differences in tissue-repair activity in human albumin fractions. Extensively studied in dermal-research and ECM-remodeling preclinical models.
- Sequence: Gly-L-His-L-Lys (3 aa) · 1:1 Cu(II) complex
- Origin: isolated from human plasma (Pickart, 1973)
- Domains: dermal-fibroblast research · ECM remodeling · antioxidant gene expression
Mechanism of action
GHK forms a stable 1:1 complex with Cu(II). The peptide-copper complex modulates expression of a broad set of ECM and antioxidant genes. Pickart and Margolina (2018, Int J Mol Sci) reviewed transcriptomic evidence indicating GHK-Cu modulates a substantial number of human genes, with particular relevance to collagen I/III synthesis, MMP-2/TIMP-1 balance, decorin synthesis, and SOD3 antioxidant expression in cultured fibroblasts [14].
In primary work, GHK-Cu at 0.01–100 nM applied to human adult dermal fibroblasts increased elastin and collagen production, and modulated MMP1/MMP2/TIMP1 in concentration-dependent fashion [15]. Maquart et al. (1988, FEBS Lett) provided the foundational demonstration that the GHK-Cu complex stimulates collagen synthesis in fibroblast cultures [16]. A 2024 review by Park et al. summarizes tripeptide roles in wound healing and skin regeneration [17].
Canonical mechanism diagram
Selected preclinical evidence
- Pickart L, Margolina A. Regenerative and protective actions of GHK-Cu in light of new gene data. Int J Mol Sci 19(7):1987 (2018). [14]PMCID PMC6073405 →
- Pickart L, Vasquez-Soltero JM, Margolina A. The human tripeptide GHK-Cu in oxidative stress and aging. Biomed Res Int 2015:648108. [15]PMID 22666519 →
- Maquart FX, et al. Stimulation of collagen synthesis in fibroblast cultures by GHK-Cu²⁺. FEBS Lett 238(2):343-346 (1988). [16]PMID 42585928 →
- Park J, et al. Tripeptides in wound healing and skin regeneration: a comprehensive review. Int J Med Sci 22:4175 (2024). [17]DOI 10.7150/ijms.4175 →
- Pickart L, Margolina A. GHK peptide as a natural modulator of multiple cellular pathways in skin regeneration. Biomed Res Int 2015:648108. [18]PMCID PMC4508379 →
Sermorelin
Synthetic 29-amino-acid fragment corresponding to the biologically active N-terminal sequence of growth-hormone-releasing hormone (GHRH 1–29). Widely used as a research tool for studying pituitary somatotrope physiology.
- Sequence: 29-aa fragment of native human GHRH(1–44)
- Receptor: GHRH-R (class-B GPCR), pituitary somatotrope
- Domain: growth-axis preclinical research, pituitary physiology
Mechanism of action
Sermorelin engages the GHRH receptor — a class-B G-protein-coupled receptor expressed predominantly on pituitary somatotroph cells. Receptor binding activates the canonical class-B cascade Gαs → adenylate cyclase → cAMP → PKA, with phosphorylation of CREB and transcription of growth-hormone messenger RNA [19,20].
Walker (1991, Drugs Aging) characterized sermorelin's preferential pituitary engagement; subsequent work established its use as a pituitary-axis research tool. Because sermorelin engages the natural GHRH receptor in a pulsatile fashion, preclinical literature contrasts its profile with continuous-receptor agonists in receptor-desensitization studies [20].
Selected preclinical evidence
- Walker RF. Sermorelin: a better approach to growth-hormone research. Drugs Aging (1991). [19]PMID 18046908 →
- Walker RF. Sermorelin: a better approach to management of adult-onset growth-hormone insufficiency? Clin Interv Aging 1(4):307-308 (2006). [20]PMCID PMC2699646 →
- Prakash A, Goa KL. Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth-hormone deficiency. BioDrugs (1999). [21]PMID 18031173 →
Tesamorelin
Trans-3-hexenoyl-modified GHRH(1-44) analog with extended plasma half-life vs native GHRH; engages the same GHRH-R / Gαs / cAMP / PKA pathway at the pituitary somatotrope.
- Modification: N-terminal trans-3-hexenoyl group conferring resistance to DPP-4 cleavage
- Receptor: GHRH-R (class-B GPCR)
- Domain: pituitary GH-axis research, visceral-adipose preclinical models
Mechanism of action
Tesamorelin engages GHRH-R with the same canonical Gαs / cAMP / PKA cascade as native GHRH. The N-terminal lipid modification confers resistance to dipeptidyl peptidase-4 (DPP-4) cleavage, extending half-life relative to unmodified GHRH analogs [22,23]. Falutz et al. (2007, NEJM) reported visceral-adipose effects in clinical research; Stanley et al. (2012, JCEM) demonstrated that responders showed correlated metabolic-profile changes (triglycerides, adiponectin, glucose homeostasis) [22,23].
Selected literature
- Falutz J, et al. Metabolic effects of a growth-hormone-releasing factor in patients with HIV. N Engl J Med 357:2359-2370 (2007). [22]DOI 10.1056/NEJMoa072375 →
- Stanley TL, et al. Reduction in visceral adiposity is associated with an improved metabolic profile in HIV-infected patients receiving tesamorelin. JCEM 97(3):989-998 (2012). [23]PMCID PMC3348954 →
- Stanley TL, Grinspoon SK. Effects of growth hormone-releasing hormone on visceral fat, metabolic, and cardiovascular indices in human studies. Growth Horm IGF Res (2015). [24]PMID 25555516 →
KLOW Blend
Combination research blend of KPV, GHK-Cu, BPC-157, and TB-500 used by investigators studying convergent tissue-remodeling and inflammation pathways. Each constituent has independent preclinical literature; the blend exists for protocol-level convenience in cell-culture and rodent models where multi-pathway engagement is the experimental aim.
- KPV — α-MSH C-terminal tripeptide (Lys-Pro-Val). Reported anti-inflammatory effects in colitis and dermatologic preclinical models, often described as MC1R-independent [29].
- GHK-Cu — see §GHK-Cu (copper transport, MMP modulation, ECM remodeling).
- BPC-157 — see §BPC-157 (VEGFR2 / eNOS, angiogenesis, tissue protection).
- TB-500 — see §TB-500 (actin sequestration, cell migration, ILK / Akt).
Researchers should reference each constituent's primary literature individually; this product does not have its own combined-product randomized publications. Lot composition and per-constituent concentration are reported on the COA.
Selected KPV literature
GLOW Blend
Combination research blend of GHK-Cu, BPC-157, and TB-500 used in dermal-research and ECM-remodeling preclinical contexts. As with KLOW, each constituent is documented independently; researchers should consult primary literature per constituent.
The three constituents collectively engage copper-dependent ECM remodeling (GHK-Cu — collagen I/III, MMP-2/TIMP-1, decorin), angiogenesis and vasomotor signaling (BPC-157 — VEGFR2 / Akt / eNOS), and cell-migration cytoskeletal dynamics (TB-500 — G-actin sequestration, ILK / Akt). The three pathways converge in dermal-fibroblast and integumentary preclinical models.
No combined-product randomized literature exists for the blend; refer to each constituent section for primary citations.
CJC-1295 (long-acting GHRH analog)
Synthetic growth-hormone-releasing-hormone analog studied in preclinical and early clinical pharmacology for prolonged stimulation of the somatotrope GHRH receptor.
- Class: GHRH(1-29) analog
- Receptor: GHRH-R (class-B GPCR) on pituitary somatotropes
Mechanism of action
Binds the pituitary GHRH receptor and activates Gαs → cAMP → PKA signaling driving GH transcription and pulsatile release. Teichman et al. (2006) reported prolonged stimulation of GH and IGF-I secretion; Ionescu & Frohman (2006) characterized the pulsatile GH response in early clinical pharmacology.
Selected literature
- Teichman SL, et al. Prolonged stimulation of GH and IGF-I secretion by CJC-1295. J Clin Endocrinol Metab 91(3):799-805 (2006).PMID 16352683 →
- Ionescu M, Frohman LA. Pulsatile secretion of GH persists during continuous stimulation by CJC-1295. J Clin Endocrinol Metab 91(12):4792-4797 (2006).PMID 17018654 →
Ipamorelin (selective growth-hormone secretagogue)
Pentapeptide ghrelin/growth-hormone-secretagogue-receptor agonist, characterized in preclinical work as a selective GH secretagogue with minimal effect on other pituitary hormones.
- Class: growth-hormone secretagogue (GHS-R1a / ghrelin receptor agonist)
- Selectivity: reported GH release without significant ACTH/cortisol or prolactin elevation
Mechanism of action
Acts on the GHS-R1a (ghrelin) receptor, signaling via Gαq → PLC → IP3 / Ca²⁺ in somatotropes to stimulate GH release. Raun et al. (1998) first described ipamorelin as a selective GH secretagogue; Andersen et al. (2001) quantified its selectivity for GH release versus other pituitary hormones in preclinical models.
Selected literature
- Raun K, et al. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol 139(5):552-561 (1998).PMID 9849822 →
- Andersen NB, et al. Selectivity of ipamorelin for GH release in vivo. Growth Horm IGF Res (2001).PMID 11168566 →
MOTS-c (mitochondrial-derived peptide)
16-amino-acid mitochondrial-derived peptide encoded within the 12S rRNA region of the mitochondrial genome, studied in preclinical metabolic and exercise-physiology research.
- Origin: mitochondrial 12S rRNA open reading frame
- Reported pathway: AMPK activation; folate–AICAR–purine-metabolism axis
Mechanism of action
Preclinical literature reports MOTS-c modulates the AMPK energy-sensing pathway and the folate–methionine / AICAR purine-biosynthesis axis, with translocation to the nucleus under metabolic stress to regulate adaptive gene expression. Lee et al. (2015) reported its discovery and metabolic regulation; Reynolds et al. (2021) characterized it as an exercise-induced mitochondrial-encoded regulator.
Selected literature
- Lee C, et al. The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis. Cell Metab 21(3):443-454 (2015).PMID 25738459 →
- Reynolds JC, et al. MOTS-c is an exercise-induced mitochondrial-encoded regulator. Nat Commun 12:470 (2021).PMID 33623019 →
Epithalon (telomerase-research tetrapeptide)
Synthetic tetrapeptide (Ala-Glu-Asp-Gly) derived from the pineal peptide epithalamin, studied in preclinical models for effects on telomerase activity, chromatin, and aging biology.
- Sequence: Ala-Glu-Asp-Gly (AEDG)
- Reported activity: telomerase induction; chromatin decondensation at specific loci
Mechanism of action
Preclinical work reports Epithalon (Epitalon) can induce telomerase activity and decondense chromatin at specific genomic loci, with reported effects on lifespan and tumor incidence in rodent models. Khavinson et al. (2002) reported chromatin activation; Anisimov et al. (2003) reported an inhibitory effect on carcinogenesis in a rodent model. Evidence is preclinical and RUO.
Selected literature
- Khavinson VKh, et al. Peptide Epitalon activates chromatin at the old age. Neuro Endocrinol Lett 23(4):301-305 (2002).PMID 12198650 →
- Anisimov VN, et al. Inhibitory effect of the peptide Epitalon on colon carcinogenesis. Cancer Lett 198(2):201-207 (2003).PMID 12049808 →
Full citations.
- Sikiric P, et al. Novel cytoprotective mediator BPC 157. Curr Pharm Des 24(18):1990-2001 (2018). PMID 29879879.
- Hsieh MJ, et al. Modulatory effects of BPC 157 on vasomotor tone & Src-Cav-1-eNOS pathway. Sci Rep 10:17078 (2020). DOI 10.1038/s41598-020-74022-y.
- Sikiric P, et al. BPC 157 Robert's stomach cytoprotection. Curr Pharm Des 26(25):2855-2866 (2020). PMCID PMC7096228.
- Sikiric P, et al. BPC 157 and the central nervous system. Neural Regen Res 17(3):482-487 (2022). PMCID PMC8504390.
- Chang CH, et al. BPC 157 promotes tendon-fibroblast outgrowth. J Appl Physiol (2011). PMID 21030672.
- Sikiric P, et al. Stable gastric pentadecapeptide BPC 157 and wound healing. Front Pharmacol 12:627533 (2021). DOI 10.3389/fphar.2021.627533.
- Józwiak M, et al. Multifunctionality and possible medical application of BPC 157. Pharmaceuticals 18(2):185 (2025). DOI 10.3390/ph18020185.
- Sikiric P, et al. BPC 157 therapy: angiogenesis and NO comment. Pharmaceuticals (2025). PMCID PMC12567428.
- Goldstein AL, Hannappel E, Kleinman HK. Tβ4 actin-sequestering protein moonlights to repair injured tissues. Trends Mol Med 11(9):421-9 (2005). PMID 16099219.
- Goldstein AL, et al. Tβ4: multifunctional regenerative peptide. Ann NY Acad Sci 1270:1-9 (2012). PMID 23050815.
- Bock-Marquette I, et al. Tβ4 activates ILK and promotes cardiac repair. Nature 432:466-472 (2004). PMID 15565145.
- Malinda KM, et al. Tβ4 accelerates wound healing. J Invest Dermatol 113(3):364-368 (1999). PMID 10469335.
- Smart N, et al. Tβ4 induces adult epicardial progenitor mobilization. Nature (2007). PMID 17108969.
- Pickart L, Margolina A. Regenerative actions of GHK-Cu. Int J Mol Sci 19(7):1987 (2018). PMCID PMC6073405.
- Pickart L, et al. GHK-Cu in oxidative stress and aging. Biomed Res Int (2015). PMID 22666519.
- Maquart FX, et al. Stimulation of collagen synthesis by GHK-Cu. FEBS Lett (1988). PMID 42585928.
- Park J, et al. Tripeptides in wound healing — comprehensive review. Int J Med Sci (2024). medsci v22p4175.
- Pickart L, Margolina A. GHK as natural modulator in skin regeneration. Biomed Res Int (2015). PMCID PMC4508379.
- Walker RF. Sermorelin: a better approach to GH research. Drugs Aging (1991). PMID 18046908.
- Walker RF. Sermorelin: a better approach to adult-onset GH insufficiency? Clin Interv Aging 1(4):307-308 (2006). PMCID PMC2699646.
- Prakash A, Goa KL. Sermorelin review. BioDrugs (1999). PMID 18031173.
- Falutz J, et al. Tesamorelin in HIV. N Engl J Med 357:2359-2370 (2007). DOI 10.1056/NEJMoa072375.
- Stanley TL, et al. Visceral adiposity and tesamorelin response. JCEM 97(3):989-998 (2012). PMCID PMC3348954.
- Stanley TL, Grinspoon SK. GHRH effects on visceral fat & metabolism. Growth Horm IGF Res (2015). PMID 25555516.
- Coskun T, et al. LY3437943 triple GIP/GLP-1/glucagon agonist. Cell Metab 34(9):1234-1247 (2022). PMID 36354040.
- Urva S, et al. LY3437943 Phase 1b in T2D. Lancet (2022). DOI 10.1016/S0140-6736(22)02033-5.
- Triple agonism-based therapies for obesity. Curr Cardiovasc Risk Rep (2025). DOI 10.1007/s12170-025-00770-z.
- Mandrika I, et al. α-MSH and KPV inhibit cytokine-induced NF-κB activation. FEBS Lett (2001). PMID 9751529.
Research-use only.
All material on this page describes published preclinical and in-vitro research. Statements about mechanism, signaling, and pathway are summarized from cited primary sources and reviews. Nothing on this page constitutes medical, dietary, or therapeutic advice. Products are not foods, drugs, supplements, or cosmetics; they are not evaluated by the U.S. Food and Drug Administration; and they are not intended to diagnose, treat, cure, or prevent any disease. Products are intended for in-vitro and non-clinical research conducted by qualified researchers 21 or older.
Where claims are made, citations are provided. Researchers are encouraged to verify each claim against the cited source. Errors or omissions should be reported to [email protected] for correction.