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人 CZIB 抗体对
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人 CZIB 抗体对

01AB01948

CXXC motif containing zinc binding protein (CZIB) is a small, evolutionarily conserved intracellular protein characterized by two canonical Cys-X-X-Cys (CXXC) motifs. These motifs facilitate the tetrahedral coordination of a zinc ion via four cysteine thiolates, which is essential for the protein's structural integrity and function. CZIB specifically interacts with the heavy-metal-associated (HMA) domain of the copper chaperone for superoxide dismutase (CCS). This interaction requires intact CXXC motifs in both partners, suggesting that CZIB plays a specialized role in metal-mediated protein-protein interactions and intracellular metal handling. As a soluble protein lacking transmembrane domains, CZIB is primarily involved in zinc and protein binding within the cytosol. Its conserved nature across species underscores its importance in maintaining metal homeostasis and supporting the functional assembly of metal-dependent chaperone complexes.

Human
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技术参数

靶点基因名
CZIB
基因别名
C1orf123
蛋白别名
CXXC motif containing zinc binding protein; CZIB
UniProt
Q9NWV4
物种
Human

产品详情

靶点名称
CZIB
蛋白名称
CXXC motif containing zinc binding protein
蛋白别名
CXXC motif containing zinc binding protein; UPF0587 protein C1orf123
靶点基因名
CZIB
基因别名
C1orf123
UniProt
Q9NWV4
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

CXXC motif containing zinc binding protein (CZIB) is a small, evolutionarily conserved intracellular protein characterized by two canonical Cys-X-X-Cys (CXXC) motifs. These motifs facilitate the tetrahedral coordination of a zinc ion via four cysteine thiolates, which is essential for the protein's structural integrity and function. CZIB specifically interacts with the heavy-metal-associated (HMA) domain of the copper chaperone for superoxide dismutase (CCS). This interaction requires intact CXXC motifs in both partners, suggesting that CZIB plays a specialized role in metal-mediated protein-protein interactions and intracellular metal handling. As a soluble protein lacking transmembrane domains, CZIB is primarily involved in zinc and protein binding within the cytosol. Its conserved nature across species underscores its importance in maintaining metal homeostasis and supporting the functional assembly of metal-dependent chaperone complexes.