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抗人 UFM1 抗体对
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抗人 UFM1 抗体对

01AB01403

Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like protein that plays a crucial role in various cellular processes through a post-translational modification known as UFMylation. This process involves the covalent attachment of UFM1 to lysine residues on target proteins, similar to ubiquitination. UFM1 is essential for maintaining cellular homeostasis, particularly in the endoplasmic reticulum (ER), where it regulates ER-associated degradation, ribosome quality control, and responses to stress. Mutations in genes associated with the UFM1 system, such as UFM1 itself, UBA5, and UFC1, have been linked to severe human diseases, including hereditary developmental epileptic encephalopathy and Schohat-type osteochondrodysplasia. These conditions underscore the importance of UFM1 in developmental processes and highlight its potential as a therapeutic target in diseases related to protein misfolding and stress responses in cells.

Human
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技术参数

靶点基因名
UFM1
基因别名
C13orf20
蛋白别名
ubiquitin fold modifier 1; UFM1
UniProt
P61960
物种
Human

产品详情

靶点名称
UFM1
蛋白名称
ubiquitin fold modifier 1
蛋白别名
Ubiquitin-fold modifier 1
靶点基因名
UFM1
基因别名
C13orf20
UniProt
P61960
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like protein that plays a crucial role in various cellular processes through a post-translational modification known as UFMylation. This process involves the covalent attachment of UFM1 to lysine residues on target proteins, similar to ubiquitination. UFM1 is essential for maintaining cellular homeostasis, particularly in the endoplasmic reticulum (ER), where it regulates ER-associated degradation, ribosome quality control, and responses to stress. Mutations in genes associated with the UFM1 system, such as UFM1 itself, UBA5, and UFC1, have been linked to severe human diseases, including hereditary developmental epileptic encephalopathy and Schohat-type osteochondrodysplasia. These conditions underscore the importance of UFM1 in developmental processes and highlight its potential as a therapeutic target in diseases related to protein misfolding and stress responses in cells.