GHK-Cu 100mg

Description

A high-purity copper-binding tripeptide studied for its role in tissue remodeling, collagen synthesis, and cellular repair mechanisms in research models.

GHK-Cu (Glycyl-L-histidyl-L-lysine copper) is a naturally occurring copper complex first identified in human plasma. As a tripeptide with a high affinity for copper, it belongs to a group of emergency signal peptides which are released during tissue injury. In laboratory settings, GHK-Cu is extensively studied for its ability to modulate various biological pathways, particularly those involving extracellular matrix remodeling and cellular regeneration. Scientific interest in GHK-Cu focuses on its unique interaction with copper ions, which serve as essential cofactors for numerous enzymes, including superoxide dismutase. Research indicates that this complex may influence the expression of a significant number of human genes, shifting them toward a state associated with repair and antioxidant activity. Its structural stability and molecular weight make it a primary subject for research involving dermatological models and tissue engineering studies.

Product Overview

GHK-Cu, or Copper Tripeptide-1, is a small fragment of the protein collagen that is naturally found in the body. It is widely utilised in biochemical research to investigate the mechanisms of wound healing, collagen synthesis, and anti-inflammatory responses. This product is supplied as a highly purified lyophilised powder, ensuring maximum stability for analytical and in vitro research environments.

Specifications

Appearance: Lyophilised Blue Powder Quantity: 100mg Molecular Formula: C14H22CuN6O4 Purity: ≥99% (HPLC Verified) Storage: Store in a cool, dry place, away from direct light. For long-term stability, storage at -20°C is recommended.

Research Applications

Current research into GHK-Cu explores its potential impact on fibroblast activation and its role in increasing the production of glycosaminoglycans. It is frequently employed in studies regarding DNA repair, the modulation of matrix metalloproteinases (MMPs), and the promotion of vascular endothelial growth factor (VEGF) expression. Note that all findings are based on laboratory research models.

Research Use Notice

For laboratory research use only. Not for human or veterinary use.