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人 ZC2HC1C 抗体对
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人 ZC2HC1C 抗体对

01AB02048

Zinc finger C2HC-type containing 1C (ZC2HC1C) is a cysteine-rich protein belonging to the non-classical C2HC/C3H zinc-finger family. It utilizes coordinated zinc ions to stabilize its fold, which likely facilitates interactions with nucleic acids or other proteins. ZC2HC1C is evolutionarily conserved across vertebrates and is characterized by a disordered region and a polar compositional bias. Proteomic studies indicate that ZC2HC1C interacts with several ciliary and intraflagellar transport proteins, suggesting a functional role in the structure or signaling of the primary cilium. Although its precise biochemical mechanisms are still being defined, its association with the ciliary machinery points to an involvement in cellular sensing and developmental signaling. The conservation of its zinc-finger domains across species further underscores its potential importance in maintaining the integrity of ciliary-mediated processes.

Human
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技术参数

靶点基因名
ZC2HC1C
基因别名
C14orf140; FAM164C
蛋白别名
zinc finger C2HC-type containing 1C; ZC2HC1C
UniProt
Q53FD0
物种
Human

产品详情

靶点名称
ZC2HC1C
蛋白名称
zinc finger C2HC-type containing 1C
蛋白别名
Zinc finger C2HC domain-containing protein 1C
靶点基因名
ZC2HC1C
基因别名
C14orf140; FAM164C
UniProt
Q53FD0
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

Zinc finger C2HC-type containing 1C (ZC2HC1C) is a cysteine-rich protein belonging to the non-classical C2HC/C3H zinc-finger family. It utilizes coordinated zinc ions to stabilize its fold, which likely facilitates interactions with nucleic acids or other proteins. ZC2HC1C is evolutionarily conserved across vertebrates and is characterized by a disordered region and a polar compositional bias. Proteomic studies indicate that ZC2HC1C interacts with several ciliary and intraflagellar transport proteins, suggesting a functional role in the structure or signaling of the primary cilium. Although its precise biochemical mechanisms are still being defined, its association with the ciliary machinery points to an involvement in cellular sensing and developmental signaling. The conservation of its zinc-finger domains across species further underscores its potential importance in maintaining the integrity of ciliary-mediated processes.