GLOW Peptide Blend 70mg Research Material

Compound: Three-component peptide preparation (GLOW)
Component 1: Copper tripeptide-1, glycyl-L-histidyl-L-lysine copper(II) complex — CAS 49557-75-7 · C14H22CuN6O4 · 401.93 Da · 50mg
Component 2: BPC-157, pentadecapeptide — CAS 137525-51-0 · C62H98N16O22 · 1419.53 Da · 10mg
Component 3: TB-500, full-length thymosin beta-4 sequence (43 residues) — CAS 77591-33-4 · 4963.4 Da · 10mg
Purity: ≥99% by HPLC · per-lot COA
Physical form: Lyophilized powder
Amount: 70mg total per vial (50mg / 10mg / 10mg)
Storage: Unopened vial: store sealed, dry, and protected from light at controlled room temperature or refrigerated. After opening or reconstitution: keep refrigerated at 2–8 °C.

Current lot documentation

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Current third-party laboratory report — Laboratory report

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lot-specific analytical documentation.

GLOW is a three-component lyophilized preparation supplied in a single vial and resolved by component on the certificate of analysis. GHK-Cu is the copper(II) coordination complex of the tripeptide glycyl-L-histidyl-L-lysine; BPC-157 is a synthetic pentadecapeptide of sequence Gly-Glu-Pro-Pro-Pro- Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val; TB-500 is the full-length 43-residue thymosin beta-4 sequence, which carries the LKKTETQ actin-binding motif. The three components are chemically distinct and are characterised separately.

GHK-Cu has no named receptor; its defining molecular interaction is square-planar coordination of copper(II) by the glycyl amine, the deprotonated backbone amide and the histidine imidazole nitrogen, characterised in vitro by UV-visible absorbance, circular dichroism and EPR spectroscopy, with conditional stability constants determined by potentiometric titration. For TB-500, the characterised molecular partner is monomeric G-actin; complex formation is quantified in vitro by pyrene-actin polymerisation assays, DNase I inhibition assays and isothermal titration calorimetry. For BPC-157, no high-affinity receptor has been established in the peer-reviewed literature, and in-vitro characterisation is reported at the level of defined enzymatic and immunoblot endpoints in cultured cell lysates rather than at a defined binding site.

Reference standard for HPLC and LC-MS method development across all three components
Copper(II) coordination characterisation by UV-visible, circular dichroism and EPR spectroscopy
Actin polymerisation and DNase I inhibition assays in defined buffer systems
Gene- or protein-expression assays in cultured fibroblast or endothelial cell lines
Peptide stability and solubility characterisation under defined temperature and pH conditions
Component-resolved identity and content verification by orthogonal chromatographic methods

Primary literature on the coordination chemistry of glycyl-L-histidyl-L-lysine copper(II), the actin-binding chemistry of the full-length thymosin beta-4 sequence, and the synthesis and analytical characterisation of BPC-157 is indexed in PubMed and in peptide and bioinorganic chemistry journals. Search results and cited literature do not establish the performance of a commercial lot or a use recommendation.

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