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Research peptide blend GLOW, lyophilized reference standard for in vitro laboratory research.
Price (/ pack)
$362.68
Total
5 total vials
$362.68
✓ Total Savings: You save $90.67 (20% total savings vs regular price)
Quantity
In Stock · 5 Units Available
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- Third-party HPLC tested. Every lot ships with a batch-linked certificate of analysis naming the laboratory, the method and the measured result. Browse certificates
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Certificate of Analysis & Specifications
HPLC Purity
98.98% HPLC
Mean of 3 constituents
Assay Content
Per constituent
Listed below
Testing Lab
KMD Analytical
Lot Number
KRSGLO-70-260827-01
Tested Sep 25, 2026
Constituent Results
| Compound | Identity | Purity (area %) | Assay (mg/vial) |
|---|---|---|---|
| GHK-Cu· 50 mg | Conforms | 98.77 | 52.15 |
| TB-500· 10 mg | Conforms | 98.21 | 11.17 |
| BPC-157· 10 mg | Conforms | 99.96 | 9.93 |
Purity and content are reported per constituent; the figure above is their mean.
Storage
36°F to 46°F
Retest Date
Sep 25, 2028
Released COA Library
Published Certificates of Analysis for GLOW. All released analytical records are preserved here. Pending and in-testing lots are reachable only through the QR printed on the vial.
Related research materials
Research Data
Chemical & Structural Identifiers
- Formulation
- Multi-peptide co-lyophilized laboratory reference complex (Ternary research standard comprising Copper Tripeptide-1, Pentadecapeptide BPC-157, and Thymosin β4 active fragment TB-500).
- Salt / Counter-Ion
- Supplied as a co-lyophilized composite standard in stoichiometric proportion as stable acetate (CH3COO-) and cupric chelate salts.
Constituent Peptides
GHK-Cu
H-Gly-His-Lys-OH·Cu2+ · CAS: 49557-75-7 · Formula: C14H22CuN6O4 · MW: 401.91 g/mol
BPC-157
H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH · CAS: 137525-51-0 · Formula: C62H98N16O22 · MW: 1419.55 g/mol
TB-500 Fragment
Ac-Leu-Lys-Lys-Thr-Glu-Thr-Gln-OH (Ac-LKKTETQ) · CAS: 77591-33-4 / 885340-08-9 · Formula: C38H68N10O14 · MW: 889.01 g/mol
Analytical & COA Specifications
- Analytical Purity (RP-HPLC)
- Individual peptide purities ≥ 98.0% via baseline-resolved multi-peak gradient elution under UV detection at λ = 214 nm and 254 nm.
- GHK-Cu identity
- Conforms to reference by retention time and UV spectrum.
- BPC-157 identity
- Conforms to reference by retention time and UV spectrum.
- TB-500 identity
- Conforms to reference by retention time and UV spectrum.
- Physical Characterization
- Distinctive light blue to cyan lyophilized cake/powder (imparted by the coordination geometry of the cupric chelate).
Handling & Stability
Storage. Store dry composite solid desiccated at -20°C to -80°C, sealed under an inert gas matrix and protected from light.
Solubility. Soluble in sterile laboratory-grade deionized water (≥ 15 mg/mL) and sterile Phosphate-Buffered Saline (PBS, pH 7.4, ≥ 10 mg/mL) for in vitro assay application.
- Handling & Buffer Selection: Maintain assay solutions at neutral pH (pH 6.8--7.4). *Do not* introduce strong metal chelators (e.g., EDTA, EGTA) or reducing agents (e.g., DTT, β-mercaptoethanol) into stock buffers, as they disrupt the copper-binding matrix or cleave the peptide assemblies. Aliquot into single-use fractions to eliminate freeze-thaw degradation cycles.
Mechanism & Literature
Biochemical Research Classification: Multi-pathway peptide complex formulated to model concurrent extracellular matrix (ECM) regulation, cytoskeletal restructuring, and focal adhesion dynamics in cell culture systems.
Cellular Pathways Investigated: Documented in in vitro fibroblasts, keratinocytes, and endothelial cell lines to assess multi-target cellular signaling:
References (3)
- Pickart, L., et al. (2018). GHK peptide as a natural modulator of multiple cellular pathways in gene expression profiling. Biomolecules, 8(4), 166.
- Chang, C. H., et al. (2011). Pentadecapeptide BPC 157 enhances FAK and paxillin phosphorylation in in-vitro cell migration assays. Biochemical and Biophysical Research Communications, 404(4), 1015–1020.
- Philp, D., et al. (2003). Thymosin beta 4 and its active peptide fragment promote dermal cell migration and matrix deposition in vitro. Journal of Cell Science, 116(15), 3229–3236.
Technical Laboratory FAQs
What constituent molecules form the GLOW peptide laboratory reference standard?
The GLOW standard is a defined multi-peptide complex consisting of Copper Tripeptide-1 (GHK-Cu), Pentadecapeptide BPC-157, and the active actin-binding fragment of Thymosin β4 (TB-500).
How are individual peptide components verified in a co-lyophilized GLOW sample?
Analytical verification is conducted using high-resolution reverse-phase HPLC (RP-HPLC), resolving three distinct retention peaks and confirming the identity of GHK-Cu, TB-500, and BPC-157 by retention time and UV spectral comparison against the reference standard.
Why must EDTA and chelating reagents be omitted during GLOW blend reconstitution?
EDTA possesses a higher binding affinity for divalent copper than the GHK tripeptide backbone, leading to transchelation that strips Cu2+ from the peptide and alters the stability profile of the complex during in vitro assays.
For Research Use Only. Not for human or animal administration. Not intended to diagnose, treat, cure, or prevent any disease. Sold for laboratory research purposes only.