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GHK-CU 100mg - Wholesale
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$60.00
Regular price
$120.00
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GHK-CU 100mg - Wholesale
Overview
GHK-Cu (glycyl-L-histidyl-L-lysine–copper) is a naturally occurring copper-peptide complex first isolated from human plasma albumin in 1973. It is found endogenously in plasma, saliva, and urine, with concentrations declining from approximately 200 ng/mL at age 20 to 80 ng/mL by age 60. This age-related decline is associated with reduced regenerative capacity. GHK-Cu is among the most extensively researched peptides in regenerative medicine and cosmeceutical science.
Mechanism of Action
GHK-Cu functions as both a signaling peptide and a copper-carrying complex. It stimulates collagen, elastin, and glycosaminoglycan synthesis in dermal fibroblasts, modulates matrix metalloproteinase (MMP) activity to support extracellular matrix remodeling, and promotes angiogenesis via vascular endothelial growth factor (VEGF) signaling. Gene expression studies indicate that GHK influences upward of 30% of human genes, including those related to tissue repair, anti-inflammatory responses, antioxidant defense, and nerve regeneration.
Research and Off-Label Applications
Wound healing and tissue repair, skin anti-aging and collagen stimulation, hair follicle health and scalp circulation, anti-inflammatory and antioxidant activity, and emerging investigation into lung fibrosis, gastrointestinal conditions, and neuroprotection.
Administration
Available as both a topical cosmeceutical ingredient (INCI name: Copper Tripeptide-1) and as a prescription injectable. Topical formulations typically show measurable results within 6–8 weeks. Injectable forms may demonstrate changes within 2–4 weeks.
Potential Adverse Effects
Topical use is generally well tolerated. Injectable use may cause mild injection site reactions. Serious adverse events are rare at cosmetic concentrations. Long-term systemic safety data remains under investigation.
Properties
1. Basic Information
2. Structural Properties Peptide Nature: Linear tripeptide; copper(II) coordination occurs via the histidine imidazole ring nitrogen, the N-terminal amine, and the deprotonated amide nitrogen, forming a square-planar chelate complex consistent with the ATCUN (amino terminal copper and nickel binding) motif
Secondary Structure: No defined secondary structure due to tripeptide length; copper coordination constrains the local conformation around the His residue; the lysine side chain ε-amine is available for electrostatic interactions with cell surface components
Hydrophobicity: Predominantly hydrophilic; glycine and lysine residues confer aqueous solubility; overall low hydrophobicity profile
Charge: Net positive charge at physiological pH; lysine ε-amine (pKa ~10.5) and N-terminal amine carry positive charges; copper(II) coordination partially neutralizes the His imidazole contribution
3. Solubility
4. Stability Thermal Stability: Thermally stable as a copper complex under standard storage conditions; free tripeptide without copper is more susceptible to degradation; the copper coordination complex provides additional conformational stabilization
Proteolytic Stability: Susceptible to aminopeptidase and other exopeptidase activity in biological matrices due to short chain length; tripeptide length limits extensive proteolytic processing; copper coordination may partially protect against aminopeptidase cleavage at the N-terminus
Storage: Store lyophilized at −20°C protected from light; aqueous solutions stable at 2–8°C for up to 30 days; avoid alkaline pH conditions which may promote copper hydroxide precipitation; protect from strong chelating agents (EDTA, EGTA) which will strip copper coordination
5. Chemical Reactivity Copper(II) coordination via ATCUN motif is reversible; copper can be displaced by stronger chelating agents or at extreme pH values; coordination stability is highest at pH 6–8
Copper(II)/copper(I) redox cycling enables superoxide dismutase-like activity in experimental systems; this redox activity is proposed as a contributor to antioxidant observations in the research literature
Histidine imidazole ring is susceptible to oxidation under prolonged exposure to hydrogen peroxide or strong oxidants; protect from oxidative environments
Lysine ε-amine is available for acylation or other chemical modification; relevant for cosmetic and pharmaceutical formulation chemistry
No disulfide bonds; oxidative stability profile is favorable relative to cysteine-containing peptides
6. Other Properties
- Name: GHK-Cu (Copper Tripeptide-1; glycyl-L-histidyl-L-lysine copper(II))
- Type: Naturally occurring copper-chelating tripeptide complex
- Length: 3 amino acids
- Sequence: Gly-His-Lys (copper(II) coordinated via histidine imidazole nitrogen and terminal amine)
- Molecular Weight: ~340.4 Da (free tripeptide); ~403.9 Da (copper(II) complex)
- Formula: C₁₄H₂₃N₆O₄Cu (copper complex form)
2. Structural Properties Peptide Nature: Linear tripeptide; copper(II) coordination occurs via the histidine imidazole ring nitrogen, the N-terminal amine, and the deprotonated amide nitrogen, forming a square-planar chelate complex consistent with the ATCUN (amino terminal copper and nickel binding) motif
Secondary Structure: No defined secondary structure due to tripeptide length; copper coordination constrains the local conformation around the His residue; the lysine side chain ε-amine is available for electrostatic interactions with cell surface components
Hydrophobicity: Predominantly hydrophilic; glycine and lysine residues confer aqueous solubility; overall low hydrophobicity profile
Charge: Net positive charge at physiological pH; lysine ε-amine (pKa ~10.5) and N-terminal amine carry positive charges; copper(II) coordination partially neutralizes the His imidazole contribution
3. Solubility
- Highly soluble in water and aqueous buffers across physiological pH range
- Solubility exceeds 10 mg/mL in sterile water under standard conditions
- Compatible with saline and common aqueous cosmetic and pharmaceutical vehicles
4. Stability Thermal Stability: Thermally stable as a copper complex under standard storage conditions; free tripeptide without copper is more susceptible to degradation; the copper coordination complex provides additional conformational stabilization
Proteolytic Stability: Susceptible to aminopeptidase and other exopeptidase activity in biological matrices due to short chain length; tripeptide length limits extensive proteolytic processing; copper coordination may partially protect against aminopeptidase cleavage at the N-terminus
Storage: Store lyophilized at −20°C protected from light; aqueous solutions stable at 2–8°C for up to 30 days; avoid alkaline pH conditions which may promote copper hydroxide precipitation; protect from strong chelating agents (EDTA, EGTA) which will strip copper coordination
5. Chemical Reactivity Copper(II) coordination via ATCUN motif is reversible; copper can be displaced by stronger chelating agents or at extreme pH values; coordination stability is highest at pH 6–8
Copper(II)/copper(I) redox cycling enables superoxide dismutase-like activity in experimental systems; this redox activity is proposed as a contributor to antioxidant observations in the research literature
Histidine imidazole ring is susceptible to oxidation under prolonged exposure to hydrogen peroxide or strong oxidants; protect from oxidative environments
Lysine ε-amine is available for acylation or other chemical modification; relevant for cosmetic and pharmaceutical formulation chemistry
No disulfide bonds; oxidative stability profile is favorable relative to cysteine-containing peptides
6. Other Properties
- ATCUN motif: The Gly-His-Lys sequence represents a canonical amino terminal copper and nickel (ATCUN) binding motif; copper coordination is highly selective and thermodynamically favorable at physiological pH
- Gene expression breadth: Preclinical transcriptomic studies have reported GHK-Cu-associated modulation of gene sets involved in tissue remodeling, inflammation, antioxidant defense, and DNA repair pathways in experimental models
- Endogenous occurrence: GHK is found in human plasma, saliva, and urine; plasma concentrations reported to decline from approximately 200 ng/mL in young adults to approximately 80 ng/mL with advancing age in observational studies
- INCI designation: Registered as Copper Tripeptide-1 under the International Nomenclature of Cosmetic Ingredients (INCI); widely used as an active ingredient in cosmeceutical formulations
Description
GHK-Cu is a naturally occurring copper-binding tripeptide and has been described in the scientific literature as a signaling peptide with reported activity across tissue remodeling, extracellular matrix regulation, and gene expression modulation pathways. Publications referencing GHK-Cu discuss it in the context of dermal fibroblast biology, collagen and elastin synthesis signaling, and matrix metalloproteinase (MMP) pathway pharmacology within experimental systems.
Reports involving GHK-Cu describe its proposed interactions with cellular signaling systems and associated downstream effects under defined experimental conditions. Observations of collagen synthesis markers, MMP activity modulation, VEGF-associated angiogenic signaling components, and gene expression patterns are limited to non-clinical research settings and are reported as descriptive findings within cellular and animal model studies.
All references to GHK-Cu are confined to mechanistic and observational research contexts and do not extend beyond laboratory-based investigation.
In the scientific literature, GHK-Cu has been referenced in non-clinical research involving fibroblast biology, gene expression profiling, wound healing models, and extracellular matrix studies. These publications describe experimental contexts in which molecular interactions, tissue remodeling markers, and pathway-associated signaling components were observed and recorded.
Reported research contexts include examination of:
- Collagen, elastin, and glycosaminoglycan synthesis signaling dynamics observed in dermal fibroblast models
- Matrix metalloproteinase (MMP) activity modulation and extracellular matrix remodeling markers in experimental settings
- VEGF-associated angiogenic signaling components evaluated under experimental conditions
- Gene expression profiling studies reporting GHK-Cu-associated transcriptional activity across tissue repair and antioxidant defense pathways
- Comparative copper-binding and signaling profiles relative to other copper-peptide complexes in experimental systems
All reported applications are confined to descriptive investigation within controlled laboratory research environments.
Mechanistic discussions in preclinical publications describe GHK-Cu as a tripeptide–copper complex in which the glycyl-L-histidyl-L-lysine backbone is described as functioning as both a signaling molecule and a copper-transport carrier. Endogenous concentrations of this complex are reported to decline with age, and this observation is discussed in the context of age-associated changes in tissue regenerative signaling within the cited literature. These descriptions are limited to molecular and biochemical observations within experimental systems and do not imply functional outcomes beyond the reported research context.
GHK-Cu is supplied as a research-grade peptide material. Identity and composition have been reported as characterized using analytical techniques commonly applied to peptide research materials, including chromatographic and mass spectrometric methods. Individual laboratories determine handling, storage, and analytical verification parameters in accordance with internal research protocols.
COA
Storage
All of our products are manufactured using the Lyophilization (Freeze Drying) process, which ensures that our products remain 100% stable for shipping for up to 3-4 months. Once the peptides are reconstituted (mixed with bacteriostatic water), they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
