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Alphapep

RESEARCH USE ONLY. All Alphapep compounds are for in-vitro laboratory research. Not for human or veterinary use, diagnosis, or consumption.

Copper Peptides

Copper-binding tripeptide reference material

GHK-Cu supplied as lyophilized reference material for in-vitro work. Laboratory research use only.

Compounds
2
GHK-Cu lot
99.74%
Certificates
2
Method
LCMS-UV

2 compounds in this line

Scope

What the molecule is

GHK is a tripeptide of glycine, L-histidine and L-lysine. In the copper form supplied here it is complexed with copper(II), and that coordination is what gives the powder its characteristic purple colour: a visible property of the complex rather than an additive. It is supplied as a characterised reference standard for in-vitro coordination and cell-culture work, and for no other purpose.

GHK-Cu
Copper-Binding Tripeptide
Formula
C14H23CuN6O4
Mass
402.9 Da
Supplied as
100mg
Glow
Proprietary Multi-Peptide Research Blend
Composition of the blend
GHK-Cu88.78%
BPC-1576.95%
TB-500 (TB-4)4.27%

Composition of the blend, not an overall purity figure.

Fig. 1 — What is supplied in this line, by composition.
Documentation

Analytical specification

The lot is assayed by an independent laboratory by LCMS-UV, reporting purity as UV peak-area percentage and confirming identity by mass. Appearance is recorded on the certificate as well, which for this compound is a meaningful check: the purple colour is a direct consequence of the copper complex being intact.

01
Lot synthesised
02
Independent lab · LCMS-UV
03
Certificate per lot
Purity
99.74%
Identity
Mass match
Classification

A coordination grouping, not a sequence family

This line is defined by coordination chemistry rather than by sequence homology, and it is not a recognised structural family. InterPro, Pfam and UniProt classify proteins by sequence relationship; a copper complex of a tripeptide has no homology to record, and the tripeptide is far shorter than any domain model describes.

InterProNo homology
PfamNo homology
UniProtNo homology

Checked against the peptide, not against the complex. These resources index sequence, and a coordination geometry is not a sequence feature.

Fig. 3 — Classified by coordination, which these databases do not index.
Structure

What the members share comes from the metal

A copper(II) centre held in a nitrogen-donor environment produces a broad d-d absorption band in the visible region near 600 to 640 nm, which is why materials of this type are coloured while metal-free peptides are not. That band is also a rapid check that the metal is bound rather than present as a free salt alongside uncomplexed peptide, and the natural copper isotope pattern, 63Cu to 65Cu at roughly 69 to 31, gives the mass spectrum a confirmatory signature that a copper-free impurity cannot reproduce.

Compounds
2
Assay method
LCMS-UV
Laboratory
ACS Peptide Testing Labs
Certificate date
2026-07-28
Appearance
Purple powder
Fig. 4 — The line as the catalogue records it.
Measurement

The variability is the boundary

Where the coordinating histidine sits in the chain determines the donor arrangement, so two peptides binding the same metal need not present the same geometry. Stoichiometry varies as well: the same ligand and metal are catalogued both as one-to-one and as two-to-one complexes, which are compositionally different species of different mass, and catalogue entries in this area are not consistent about which they mean.

Reported as
99.74%

Percentage of total UV peak area attributable to the target compound.

Confirmed by
Mass match

Measured mass of the principal peak against the calculated mass for the sequence.

Tied to
AAHW061

Each certificate is issued against a specific accession, not against the compound.

Fig. 5 — What the measurement rests on.

Certificates of analysis

All certificates