Out of stock
Klow 80mg (Blend)
Glow
€99.00
In StockSize
1
For in-vitro laboratory research use only. Not intended for human consumption, veterinary, diagnostic, or clinical use.
Same-day dispatch
Order before 12:00 CET
≥99% HPLC Purity
Third-party batch verified
COA on Request
Batch lab report on request
Secure shipping
Professional packaging
Secure Payments
SEPA
Order before 12:00 for same-day shipping
Order now, ships today
OrderedToday
ShippedToday
Delivered1 Jul–3 Jul
Product Specifications
Format
Lyophilized powder
Strength
70 mg
Purity
99%
Testing
Third-party HPLC/MS
CAS
N/A
Intended use
Research only
Description
Glow is a research blend combining three extensively studied research peptides: Thymosin Beta-4 (TB4), BPC 157, and GHK-Cu. Each component has been independently investigated in laboratory research models related to cytoskeletal dynamics, extracellular matrix research, angiogenesis pathway research, and cellular signaling research.
By integrating these compounds into a single research formulation, Glow is designed for multi-pathway research approaches where overlapping or complementary mechanisms can be explored within one experimental framework.
Research Focus Areas
Cytoskeletal and Cellular Signaling Research
• TB4:actin polymerization and cytoskeletal dynamics research, cell migration research models
• BPC 157:angiogenesis pathway research, fibroblast research models, endothelial signaling research
• GHK-Cu:extracellular matrix research, copper-binding tripeptide research, antioxidant gene expression research
Extracellular Matrix and Connective Tissue Research
•Collagen synthesis pathway research
•Tissue remodeling research models
•Cellular recovery signaling research
Inflammatory and Oxidative Signaling Research
All three components are studied in research models involving inflammatory signaling pathways, oxidative balance research, and tissue resilience mechanisms (Pickart and Margolina, 2018, International Journal of Molecular Sciences).
The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.
This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.
TB4
TB-500 peptide is a synthetic full-length analog of thymosin beta-4, a 43-residue actin-binding research peptide abundantly expressed across many mammalian cell types. As a synthetic reference compound, TB-500 is supplied for use in actin-binding research, cytoskeletal dynamics research models, and cellular-process research in controlled laboratory settings.
TB-500 peptide is investigated for its interaction with monomeric G-actin, a core component of the cytoskeletal dynamics research system. In laboratory research studies, the parent thymosin beta-4 sequence has been characterized as a 1:1 actin-sequestering peptide that engages G-actin and modulates the equilibrium between monomeric and filamentous actin in cellular research models (Huff et al., 2001, International Journal of Biochemistry and Cell Biology). This actin-binding profile makes TB-500 a widely used reference compound in laboratory research studies of cytoskeletal dynamics research and cellular-process research signalling.
Beyond actin-binding research, TB-500 peptide has also been investigated in laboratory research studies examining endothelial cellular-process research models, inflammatory-pathway research, and structure-activity research comparing the full-length thymosin beta-4 sequence with discrete active-site fragments such as the heptapeptide LKKTETQ ([Sosne et al., 2010, Annals of the New York Academy of Sciences](https://pubmed.ncbi.nlm.nih.gov/20179146/)). These investigations have positioned TB-500 as an experimental research compound of interest in studies of cytoskeletal dynamics research and cellular-pathway research models. See also: BPC-157, TB500 Fragment (17-23), KPV
BPC 157
BPC-157 is a synthetic 15-residue gastric-pentadecapeptide research compound derived from a protein originally identified in gastric extracts. Composed of the sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, this gastric-extract-derived research peptide is supplied as a defined investigational laboratory peptide for use in cellular-process research, nitric oxide signalling research, and gastric-tissue research models in controlled laboratory settings.
BPC-157 has been investigated in laboratory research studies for its interaction with vascular endothelial signalling pathways and the nitric oxide system. Mechanistic research models have characterized engagement with vascular endothelial growth factor receptor-2 (VEGFR2) signalling and the Akt-eNOS axis, supporting investigations into nitric oxide signalling research and endothelial cellular-process research (Hsieh et al., 2017, Journal of Molecular Medicine; Hsieh et al., 2020, Scientific Reports).
Beyond endothelial pathway research, BPC-157 has also been investigated in laboratory research studies examining gastric-tissue research models, inflammatory-pathway research, and cellular-process research signalling. These investigations have positioned BPC-157 as an experimental research compound of interest in studies of pentadecapeptide pharmacology and integrated cellular-pathway signalling.
For a deeper review of the published literature, see our [BPC-157 research guide](/blog/bpc-157-research-guide). See also: TB-500 10 mg, KPV, GHK-Cu
GHK-Cu
GHK-Cu is a naturally occurring copper-binding tripeptide composed of glycine, histidine, and lysine. It is classified as a bioactive tripeptide-copper complex widely studied for its role in tissue remodeling and cellular signaling research.
In biological systems, GHK binds copper ions to form the bioactive GHK-Cu complex, which functions as a signaling molecule involved in maintaining tissue integrity. The peptide influences extracellular matrix remodeling by stimulating collagen synthesis and modulating matrix metalloproteinase activity. It also engages TGF-beta signaling pathways and supports endothelial-related cellular responses. At the genomic level, GHK-Cu has been shown to influence gene expression patterns associated with aging and cellular renewal.
Research interest in GHK-Cu focuses on its ability to influence extracellular matrix remodeling, stimulate collagen synthesis, modulate inflammatory signaling, and support [cellular renewal processes](/product/pinealon-20-mg). Investigations have documented its capacity to reset gene expression patterns associated with aging, activating protective and cellular-pathway genes ([Pickart & Margolina, 2018, International Journal of Molecular Sciences](https://pubmed.ncbi.nlm.nih.gov/29986520/)). Due to its broad biological activity, GHK-Cu is frequently investigated in cellular-pathway biology, skin physiology, and age-related tissue degeneration models. It remains a foundational compound in connective tissue and aging research. See also: Epitalon, Snap-8, MOTS-c
Scientific Background
Glow combines 3 research compounds: TB4, BPC 157, GHK-Cu. Scientific background for each component is documented below.
TB4
Thymosin beta-4 is a 43-amino-acid acidic peptide first isolated from thymic tissue and subsequently identified as one of the most abundant intracellular actin-sequestering peptides in mammalian cell types. It functions as a 1:1 G-actin-binding research peptide and contributes to the maintenance of a pool of monomeric actin available for rapid cytoskeletal reorganization in cellular research models.
TB-500 is supplied as a synthetic full-length analog of the thymosin beta-4 sequence, allowing laboratory research studies to use a defined reference compound for actin-binding research and cytoskeletal dynamics research. The sequence retains the central LKKTET actin-binding motif (residues 17-22), which has been mapped through mutational and structural research as the principal contact region with G-actin in research models.
This positioning at the intersection of cytoskeletal dynamics research, cellular-process research, and structure-activity research has made TB-500 an experimental research compound of considerable interest in laboratory research studies of actin-binding pharmacology, endothelial cellular-process research, and comparative thymosin beta-4 fragment research.
BPC 157
BPC-157 is classified as a synthetic gastric-pentadecapeptide research compound. The sequence was originally derived from a larger protein identified in gastric extracts, and the 15-residue synthetic version has become a widely used reference compound in cellular-pathway research and nitric oxide signalling research.
Laboratory research studies have characterized BPC-157 as a stable research peptide in acidic conditions, a property that distinguishes it from many other bioactive research peptides. This stability profile has made it a useful tool in laboratory research studies of gastric-tissue research, where peptide integrity under acidic conditions is an important methodological consideration.
Mechanistic research has investigated BPC-157 engagement with vascular endothelial pathways, including VEGFR2 signalling research and the Akt-eNOS axis. Additional research models have examined interaction with the broader nitric oxide system, Src-Cav-1-eNOS signalling, and inflammatory-pathway research. This positioning at the intersection of nitric oxide signalling research, endothelial cellular-process research, and gastric-tissue research has made BPC-157 a research peptide of considerable interest in laboratory research studies of pentadecapeptide pharmacology and integrated cellular-pathway signalling.
GHK-Cu
GHK was first identified in human plasma and later recognized for its strong affinity for copper ions. The GHK-Cu complex naturally occurs in tissues and fluids, where it participates in signaling pathways related to cellular-response research. Levels of GHK decline with age, which has led to scientific interest in its role in age-related loss of tissue cellular-pathway capacity.
Experimental studies have demonstrated that GHK-Cu can influence the expression of a wide range of genes involved in cell growth, antioxidant defense, inflammatory signaling control, and extracellular matrix organization. These properties have positioned GHK-Cu as an important research compound in studies of cellular-process signaling, skin aging, and connective tissue biology.
Structure
Glow is supplied as a homogeneous lyophilized mixture. Structural details for each compound:
TB4
TB-500 Structure
Peptide Class:Synthetic full-length thymosin beta-4 research peptide
Residue Count:43 amino acids
Central Actin-Binding Motif:LKKTET (residues 17-22)
Molecular Formula:C₂₁₂H₃₅₀N₅₆O₇₈S
Molecular Weight:~4960 g/mol
CAS Number:885340-08-9
Alternative Designations:Thymosin beta-4 synthetic analog, Tβ4 research peptide
BPC 157
BPC-157 Structure
Peptide Class:Synthetic gastric-pentadecapeptide research compound
Residue Count:15 amino acids
Amino Acid Sequence:Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val
Sequence (single-letter):GEPPPGKPADDAGLV
Molecular Formula:C₆₂H₉₈N₁₆O₂₂
Molecular Weight:~1419 g/mol
CAS Number:137525-51-0
PubChem CID:9941957
Alternative Designations:Body Protection Compound-157, Bepecin
GHK-Cu
Peptide Class:Copper-binding tripeptide
Amino Acid Sequence:Gly-His-Lys (GHK)
Molecular Formula:C₁₄H₂₃CuN₆O₄⁺
Molecular Weight:~402.9 g/mol
CAS Number:89030-95-5
Mechanism of Action
Each compound in Glow engages distinct biochemical targets. Mechanism of action per compound:
TB4
1. Actin-Binding and Cytoskeletal Dynamics Research
TB-500 engages monomeric G-actin in a 1:1 stoichiometry through its central LKKTET actin-binding motif. In laboratory research studies, this interaction sequesters G-actin and modulates the equilibrium between monomeric and filamentous actin populations, supporting investigations into cytoskeletal dynamics research and cellular-process research models.
2. Cellular-Process Signalling Research
TB-500 has been investigated in cellular research models for its interaction with endothelial and epithelial cell migration pathways. Research models indicate that the full-length thymosin beta-4 sequence engages cellular-process signalling research relevant to cellular-pathway research and structure-activity research with discrete actin-binding fragments such as LKKTETQ.
3. Inflammatory-Pathway Research
Laboratory research studies have examined how TB-500 modulates inflammatory-pathway research markers in cellular and animal research models. These investigations are relevant to cytokine-signalling research and comparative research on thymosin beta-4 active-site fragments.
4. Structure-Activity Research
By supplying the full-length 43-residue sequence, TB-500 enables comparative research alongside discrete fragments such as the heptapeptide LKKTETQ (residues 17-23). This supports structure-activity research investigating how isolated actin-binding domains compare to the parent peptide in actin-binding research and cellular-process research models.
Research Applications
•Actin-binding research and cytoskeletal dynamics research models
•Cellular-process research and endothelial cellular-process signalling
•Inflammatory-pathway research and cytokine-signalling research
•Structure-activity research comparing full-length thymosin beta-4 with active-site fragments
•Comparative peptide research with TB500 Fragment (17-23) and other Tβ4-derived research peptides
•Cardiovascular cellular research models and angiogenic-pathway research
Conclusion
TB-500 is a synthetic full-length thymosin beta-4 research peptide that engages monomeric G-actin through its central LKKTET motif and supports laboratory research studies of cytoskeletal dynamics research, cellular-process research, and inflammatory-pathway research. Its defined sequence and 1:1 actin-binding profile make it a valuable reference compound for laboratory research studies of actin-binding pharmacology and comparative research with thymosin beta-4 active-site fragments.
BPC 157
1. VEGFR2 Signalling Research
BPC-157 has been investigated in laboratory research studies for engagement with vascular endothelial growth factor receptor-2 (VEGFR2) signalling. Mechanistic research models indicate that BPC-157 modulates VEGFR2 expression and internalization, supporting investigations into endothelial cellular-process research and vascular-pathway research (Hsieh et al., 2017, Journal of Molecular Medicine).
2. Akt-eNOS Axis and Nitric Oxide Signalling Research
Laboratory research studies have characterized BPC-157 engagement with the Akt-endothelial nitric oxide synthase (eNOS) axis. This signalling research is associated with nitric oxide production in endothelial research models and has been investigated as a downstream consequence of VEGFR2 modulation in cellular-pathway research.
3. Src-Cav-1-eNOS Pathway Research
Research models have also characterized BPC-157 engagement with the Src-Caveolin-1-eNOS pathway. Mechanistic research indicates that BPC-157 enhances phosphorylation of Src, Cav-1 and eNOS and reduces Cav-1-eNOS binding in vascular research models, supporting investigations into nitric oxide signalling research independent of canonical VEGFR2 input (Hsieh et al., 2020, Scientific Reports).
4. Gastric-Tissue Research Models
Laboratory research studies have investigated BPC-157 stability in acidic conditions and its engagement with gastric-tissue research models. These investigations support research on pentadecapeptide pharmacology and cellular-pathway research relevant to gastric-tissue research.
Research Applications
•Nitric oxide signalling research and Akt-eNOS axis research
•VEGFR2 signalling research and endothelial cellular-process research models
•Src-Cav-1-eNOS pathway research and vasomotor-tone research
•Gastric-tissue research models and pentadecapeptide stability research
•Inflammatory-pathway research and cytokine-signalling research
•Comparative research with TB-500 and other cellular-process research peptides
Conclusion
BPC-157 is a synthetic 15-residue gastric-pentadecapeptide research compound that engages VEGFR2 signalling, the Akt-eNOS axis, and the Src-Cav-1-eNOS pathway in research models. Its combination of acidic-condition stability and characterized engagement with nitric oxide signalling research makes it a valuable investigational laboratory peptide for laboratory research studies in cellular-pathway research, endothelial cellular-process research, and gastric-tissue research models.
GHK-Cu
1. Copper Transport and Delivery
GHK binds copper ions and facilitates their safe transport and delivery to cells, supporting copper-dependent enzymatic processes essential for cellular-process research and antioxidant defense.
2. Extracellular Matrix Regulation
GHK-Cu has been shown to stimulate collagen, elastin, and proteoglycan synthesis while simultaneously regulating matrix metalloproteinases, contributing to balanced tissue remodeling.
3. Modulation of Inflammatory Signaling
Research indicates that GHK-Cu may help regulate inflammatory pathways by reducing pro-inflammatory cytokine activity and supporting inflammatory-pathway gene expression profiles.
4. Gene Expression and Cellular Renewal
GHK-Cu influences the expression of genes associated with cell survival, differentiation, and cellular signaling research, supporting cellular turnover and tissue maintenance.
Research Applications
•Cellular-process research and cellular signaling studies in experimental models
•Skin and aging research focused on collagen production and oxidative balance
•Cellular-pathway biology including stem cell activity and differentiation studies
•Inflammatory signaling and tissue-remodeling models examining matrix-related genes
•Connective tissue biology and age-related tissue degeneration investigations
•Copper-dependent enzymatic and antioxidant defense pathway research
Conclusion
GHK-Cu is a copper-binding tripeptide investigated for its role in cellular-process research, extracellular matrix regulation, and gene expression associated with cellular-response signaling. By supporting copper-dependent biological processes, modulating inflammatory signaling, and promoting structural protein synthesis, GHK-Cu represents a foundational research compound in cellular-pathway biology and aging-related tissue studies.
References
Published references for each compound in Glow, listed by component:
TB4
•Huff T. et al. (2001). beta-Thymosins, small acidic peptides with multiple functions. International Journal of Biochemistry and Cell Biology.
•Sosne G. et al. (2010). Biological activities of thymosin beta4 defined by active sites in short peptide sequences. Annals of the New York Academy of Sciences.
•Mannherz H.G. & Hannappel E. (2009). The beta-thymosins: intracellular and extracellular activities of a versatile actin-binding peptide family. Cell Motility and the Cytoskeleton.
•Safer D. et al. (1991). Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable. Journal of Biological Chemistry.
•Domanski M. et al. (2004). Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. Journal of Biological Chemistry.
•Xue B. & Robinson R.C. (2013). Guardians of the actin monomer. European Journal of Cell Biology.
BPC 157
•Hsieh M.J. et al. (2017). Pro-angiogenic BPC157 is associated with VEGFR2 activation and up-regulation. Journal of Molecular Medicine.
•Hsieh M.J. et al. (2020). Modulatory effects of BPC 157 on vasomotor tone and the activation of Src-Caveolin-1-endothelial nitric oxide synthase pathway. Scientific Reports.
•Sikiric P. et al. (2014). Stable gastric pentadecapeptide BPC 157-NO-system relation. Current Pharmaceutical Design.
•Sikiric P. et al. (2018). Stable gastric pentadecapeptide BPC 157: vascular recruitment and gastrointestinal-tract research. Current Pharmaceutical Design.
•Vukojevic J. et al. (2021). Pentadecapeptide BPC 157 and the central nervous system. Frontiers in Pharmacology (research-model review).
•Jozwiak M. et al. (2025). Multifunctionality and possible research applications of the BPC 157 peptide, literature and patent review. Pharmaceuticals.
GHK-Cu
•Pickart L. et al. (2003). The human tri-peptide GHK and tissue remodeling. Journal of Biomaterials Science.
•Maquart F.X. et al. (1993). Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex GHK-Cu. FEBS Letters.
•Hong Y. et al. (2008). Gene expression profiling of GHK-Cu in human cells. Biogerontology.
•Pickart L., Margolina A. (2018). Cellular-response signaling and protective actions of the GHK-Cu peptide. Biomolecules.
•Pickart L., Margolina A. (2018). Regenerative and protective actions of the GHK-Cu peptide in the light of the new gene data. International Journal of Molecular Sciences.
€ 99.00