For Research Use Only — Not for Human or Veterinary Use

GHK-Cu is the copper(II) complex of the tripeptide glycyl-L-histidyl-L-lysine (GHK). GHK was first isolated from human plasma, binds copper(II) with high affinity, and is widely used in laboratory models of extracellular-matrix (ECM) remodelling, fibroblast biology and gene-expression profiling. This guide covers the compound’s identity, the mechanisms reported in the literature, and the documentation to review before using a lot.

Research use only. GHK-Cu supplied by OligoPoly Laboratories is a laboratory research material. It is not a drug, supplement or cosmetic and is not for human or veterinary use.

Compound identity

Name GHK-Cu; copper(II) complex of glycyl-L-histidyl-L-lysine
CAS number (GHK-Cu) 89030-95-5
Registered formula (complex) C14H23CuN6O4+ · 402.92 g/mol (PubChem CID 71587328)
Peptide ligand (GHK) CAS 49557-75-7 · C14H24N6O4 · 340.38 g/mol (PubChem CID 73587)

Registered formulas for copper complexes differ in how charge and counter-ions are shown. Use the certificate of analysis for the specific lot as the reference for the material in hand.

Origin and chemistry

GHK is a naturally occurring tripeptide. Its copper(II) affinity is similar to that of the copper-transport site on albumin, and it readily forms the GHK-Cu complex [1]. A GHK sequence also occurs within the α2(I) chain of type I collagen, which led to the proposal that the tripeptide can be released by proteases at sites of tissue injury [2].

Mechanisms reported in the literature

Extracellular-matrix synthesis

In human fibroblast cultures, GHK-Cu stimulated collagen synthesis at very low concentrations, independent of changes in cell number [2]. Reviews of the literature describe effects on the synthesis of collagen, elastin, metalloproteinases and anti-proteases in cell and animal models [1].

Remodelling and anti-oxidative signalling

Laboratory studies summarised by Pickart report chemoattraction of repair cells, modulation of inflammatory mediators and increased antioxidant-enzyme activity in experimental models [1].

Gene-expression profiling

Analyses of gene-expression data associate GHK with up- and down-regulation of a large number of human genes, which has made it a subject of connectivity-map-style research [3].

These findings come from in-vitro and animal research. They describe what researchers investigate with GHK-Cu, not an effect of this research material.

Typical laboratory research questions

Analytical identity and purity

For GHK-Cu, a certificate should report purity by HPLC and identity by mass spectrometry. Because the material is a metal complex, copper content and the free-peptide fraction are also relevant quality attributes. Read the certificate alongside HPLC vs LC-MS in peptide testing and how to read a COA.

Documentation for OligoPoly GHK-Cu

A certificate is published for GHK-Cu 50 mg, batch SGX-OL-2026-0811-K99. The GHK-Cu 50 mg research peptide page lists the catalog record and related materials.

Frequently asked questions

What is the difference between GHK and GHK-Cu?

GHK is the free tripeptide. GHK-Cu is its copper(II) complex. They have different CAS numbers and formulas; both are listed above.

Why does the registered formula carry a charge?

Database entries for metal–peptide complexes often represent a specific ionic form. The lot certificate is the reference for the supplied material.

Is GHK-Cu for cosmetic or personal use?

Not this material. OligoPoly GHK-Cu is sold for laboratory research use only.

References

  1. Pickart L. The human tri-peptide GHK and tissue remodeling. J Biomater Sci Polym Ed. 2008;19(8):969-988. doi:10.1163/156856208784909435
  2. Maquart FX, et al. Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS Lett. 1988;238(2):343-346. doi:10.1016/0014-5793(88)80509-x
  3. Pickart L, Vasquez-Soltero JM, Margolina A. The human tripeptide GHK-Cu in prevention of oxidative stress and degenerative conditions of aging: implications for cognitive health. Oxid Med Cell Longev. 2012;2012:324832. doi:10.1155/2012/324832
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