5-Amino-1MQ (10mg)

A naturally occurring, high-affinity tripeptide-copper complex characterized for research applications involving tissue remodeling, wound healing, bioenergetics, oxidative stress modulation, and genomic regulation.

Trust & Quality Verification

  • Research Use Only. Not for human or veterinary use.
  • 99% Purity Replacement Guarantee
  • Verifiable purity via HPLC & Mass Spectrometry
  • Supplied as lyophilized powder for stability during transport and storage
  • Certificate of Analysis (COA) available per lot
  • Safety Data Sheet (SDS) available

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SKU: V-5A1MQ-10MG Category:

99%+

Purity Standard

HPLC

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COA

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Description

GHK-Cu (Glycyl-L-histidyl-L-lysine copper complex) is a synthetic form of a naturally occurring human tripeptide that possesses a high binding affinity for copper (II) ions. It is widely utilized in research to investigate tissue remodeling and skin regeneration through the modulation of multiple cellular pathways.

Distinct from simple copper salts, the GHK-Cu complex functions as a delivery system and a modulator of gene expression. Research indicates it influences genes relevant to nervous system function and cognitive decline. In laboratory settings, it is frequently employed to study the stimulation of connective tissue accumulation, angiogenesis, and the regulation of oxidative stress in various tissue models.

Biochemical Characteristics

Chemically, GHK-Cu is defined by its ability to facilitate the uptake of copper into cells, which is essential for the function of numerous enzymes involved in collagen synthesis and antioxidant defense.

  • Sequence/Structure: Tripeptide (Gly-His-Lys) chelated with Copper (Cu2+).
  • Permeability: Studies utilize various carrier systems, such as liposomes, to enhance the permeation and retention of GHK-Cu in target tissues for cosmetic and therapeutic modeling.
  • Stability: The complex exhibits potent antioxidant properties and is capable of preventing metal-induced protein aggregation.
  • Specificity: GHK-Cu modulates a broad spectrum of human genes, capable of resetting gene expression patterns in cancer cell lines such as MCF7 and PC3.

Chemical Properties

Property Specification
Molecule Name GHK-Cu (Copper Peptide)
Synonyms Glycyl-L-histidyl-L-lysine-Cu2+; Copper Tripeptide-1
Sequence Gly-His-Lys·Cu
Molecular Formula C₁₄H₂₂CuN₆O₄ (Complex)
Molecular Weight ~401.91 g/mol (varies by salt/hydration)
Form Lyophilized Powder (Blue)
Purity ≥99% (Verified via HPLC)
Solubility Soluble in water
Documentation COA available per lot; SDS available

5-Amino-1MQ is strictly for laboratory research and is commonly employed in the following investigational areas:

NAD+ Salvage Pathway Characterization

Research indicates that NNMT activity drains the available pool of nicotinamide, a precursor for NAD+. 5-Amino-1MQ is utilized as a chemical probe to block this drain, allowing researchers to quantify the subsequent restoration of NAD+ levels and measure the activity of NAD+-dependent enzymes, such as PARPs and Sirtuins, in various cell lines.

Adipocyte Biology and Lipogenesis

In vitro studies utilizing differentiated adipocytes employ 5-Amino-1MQ to observe its impact on lipid accumulation and adipogenesis. Investigations focus on how NNMT inhibition alters the expression of transcription factors related to lipogenesis and fatty acid oxidation, providing data on cellular energy homeostasis and metabolic reprogramming.

Muscle Physiology and Bioenergetics

Experimental models involving myoblasts utilize this compound to study muscle satellite cell proliferation and fusion. Researchers quantify changes in mitochondrial respiration rates and oxidative phosphorylation efficiency to understand the role of the NNMT-NAD+ axis in cellular aging and tissue regeneration signaling.

Oncology and Cellular Proliferation

Elevated NNMT expression is observed in various cancer cell lines. 5-Amino-1MQ is used in oncology research to determine the effects of enzymatic inhibition on tumor cell metabolism, specifically looking at the “Warburg effect” and the methylation potential of the cell, which influences epigenetic progression.

Pathway / Mechanistic Context

The primary mechanism of action for 5-Amino-1MQ in research settings is the competitive inhibition of NNMT.

  • NNMT Activity: Under normal conditions, NNMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide (NAM), producing 1-methylnicotinamide (1-MNA). This process effectively removes NAM from the NAD+ salvage pathway.
  • Inhibition: By blocking NNMT, 5-Amino-1MQ prevents the methylation of nicotinamide.
  • Resulting Flux: This inhibition preserves the pool of nicotinamide, which can then be converted back into NAD+ via the salvage pathway enzymes (NAMPT). Simultaneously, it prevents the depletion of SAM, a critical universal methyl donor for epigenetic modification.

Preclinical Research Summary

Published preclinical literature documents investigations of 5-Amino-1MQ across multiple experimental models:

  • Adipose Tissue: Studies in diet-induced obesity mouse models have observed that NNMT inhibition via 5-Amino-1MQ may reduce lipogenesis and decrease adipocyte size without altering food intake.
  • Muscle Satellite Cells: Research indicates that elevated NAD+ levels resulting from NNMT inhibition may enhance the proliferation and fusion capacity of muscle satellite cells in aged tissue models.
  • Cellular Bioenergetics: Data from metabolic assays suggest that treatment with 5-Amino-1MQ can increase oxygen consumption rates (OCR) and ATP production in specific cell lines, indicative of enhanced mitochondrial function.

Form & Analytical Testing

This material is produced via robust chemical synthesis and supplied as a lyophilized (freeze-dried) powder.

  • Lyophilization: Removes water content under vacuum to maintain compound integrity and extend shelf-life.
  • Identity Verification: Each lot undergoes Mass Spectrometry (MS) to confirm molecular weight and identity.
  • Purity Verification: High-Performance Liquid Chromatography (HPLC) is performed to ensure the product meets the ≥99% purity standard required for reproducible research data.

Storage & Handling

Stable at room temperature for up to 90 days. For long-term storage, keep at -20C (-4F) or colder.

Once mixed with a solvent (e.g., bacteriostatic water), the solution must be stored at 4C (39F) and utilized within 30 days. Avoid repeated freeze-thaw cycles, as this degrades the peptide structure.

Referenced Citations

  • Stable at room temperature for up to 90 days. For long-term storage, keep at -20°C (-4°F) or colder.
  • Once mixed with a solvent (e.g., bacteriostatic water), the solution must be stored at 4 °C (39°F) and utilized within 30 days. Avoid repeated freeze-thaw cycles, as this degrades the peptide structure.

RESEARCH USE ONLY

This product is intended strictly for laboratory research use only. It is not for human or veterinary use. It is not intended for diagnosis, treatment, cure, or prevention of any disease. All purchases are subject to our Terms of Service and Purity Guarantee.

No COAs available for this product.

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RESEARCH USE ONLY

This product is intended strictly for laboratory research use only. It is not for human or veterinary use. It is not intended for diagnosis, treatment, cure, or prevention of any disease. All purchases are subject to our Terms of Service and Purity Guarantee.

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