CUTC Human
Description
Biological Functions
CUTC facilitates copper homeostasis through:
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Efflux Regulation: Transports cuprous ions (Cu⁺) to prevent intracellular toxicity .
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Chaperone Activity: Transfers copper to export channels like CopB via labile binding sites .
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Microbiome Interactions: Murine studies link cecal CutC activity to trimethylamine oxide (TMAO) production, a cardiovascular risk factor .
Copper Binding and Trafficking
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Binding Assay: CUTC expressed in E. coli with 1 mM CuSO₄ showed 0.8 Cu atoms per protein monomer, confirming its role in Cu⁺ sequestration .
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Conserved Residues: Cys52, His145, and His222 form the Cu-binding site, distinct from bacterial homologs lacking Cys31 .
Recombinant Production
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Expression System: Purified via nickel chromatography with >90% purity .
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Stability: Maintains activity in 20 mM Tris-HCl (pH 8.0) with 5 mM DTT and 10% glycerol .
Disease Associations
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Inflammation: Diarrhea-induced murine models showed elevated cecal CutC activity correlating with increased TMAO, IL-6, and TNF-α levels .
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Microbiome Dysbiosis: Reduced microbial diversity (Alistipes, Bacteroides) coincided with CutC upregulation .
Clinical and Therapeutic Implications
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Cardiovascular Risk: TMAO derived from bacterial CutC activity is implicated in atherosclerosis , though human CUTC’s direct role remains unclear.
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Copper Metabolism Disorders: Dysregulation may contribute to Wilson’s disease or Menkes disease pathways, warranting further study .
Research Gaps and Future Directions
Product Specs
Product Science Overview
Copper is a vital micronutrient required for the proper metabolic functioning of most prokaryotic and eukaryotic organisms. It plays a pivotal role in the physiology of aerobic organisms, participating in processes such as electron transport, iron metabolism, and the functioning of antioxidant enzymes. However, copper’s reactivity can lead to the generation of free radicals, making its regulation within cells critical to avoid toxicity .
The cutC protein is a cytoplasmic and nuclear protein that can bind one Cu1+ ion per subunit. It is involved in the efflux trafficking of cuprous ions, helping to maintain the balance of copper within cells. The human cutC protein shares significant sequence identity with its counterparts in other species, including 89% with the mouse and 44% with the E. coli CutC proteins .
Recombinant human cutC protein is typically expressed in E. coli and purified using conventional chromatography techniques. The recombinant protein often includes an N-terminal His-tag to facilitate purification. The protein is usually lyophilized from a sterile PBS solution containing glycerol and other protectants to ensure stability during storage .
The cutC protein is primarily used for research purposes, particularly in studies related to copper metabolism and homeostasis. Understanding the function and regulation of cutC can provide insights into various diseases and conditions associated with copper imbalance, such as Wilson’s disease and Menkes disease .
