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抗人 PADI4 抗体对
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抗人 PADI4 抗体对

01AB01542

Peptidyl arginine deiminase 4 (PADI4) is a calcium-dependent enzyme of 663 amino acids and approximately 74 kDa, encoded by the PADI4 gene on chromosome 1p36.13, and is primarily found in the cytoplasm and nucleus of granulocytes such as neutrophils and eosinophils. PADI4 catalyzes the post-translational conversion of arginine residues to citrulline (citrullination), a modification that regulates protein function, notably by deiminating histones H3 and H4, thereby influencing chromatin structure and gene expression. The enzyme functions as an oligomer, binding five calcium ions per subunit, and can undergo autodeimination, which modulates its protein-protein interactions. PADI4 is essential for the formation of neutrophil extracellular traps (NETs) through histone citrullination, playing a key role in innate immunity. Dysregulated PADI4 activity is implicated in the pathogenesis of autoimmune diseases, particularly rheumatoid arthritis, where it generates citrullinated proteins that trigger autoantibody production, and has also been linked to cancer and multiple sclerosis.

Human
规格起售价
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技术参数

靶点基因名
PADI4
基因别名
PAD4; PADI5; PDI5
蛋白别名
peptidyl arginine deiminase 4; PADI4
UniProt
Q9UM07
物种
Human

产品详情

靶点名称
PADI4
蛋白名称
peptidyl arginine deiminase 4
蛋白别名
Protein-arginine deiminase type-4; HL-60 PAD; Peptidylarginine deiminase IV; Protein-arginine deiminase type IV
靶点基因名
PADI4
基因别名
PAD4; PADI5; PDI5
UniProt
Q9UM07
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

Peptidyl arginine deiminase 4 (PADI4) is a calcium-dependent enzyme of 663 amino acids and approximately 74 kDa, encoded by the PADI4 gene on chromosome 1p36.13, and is primarily found in the cytoplasm and nucleus of granulocytes such as neutrophils and eosinophils. PADI4 catalyzes the post-translational conversion of arginine residues to citrulline (citrullination), a modification that regulates protein function, notably by deiminating histones H3 and H4, thereby influencing chromatin structure and gene expression. The enzyme functions as an oligomer, binding five calcium ions per subunit, and can undergo autodeimination, which modulates its protein-protein interactions. PADI4 is essential for the formation of neutrophil extracellular traps (NETs) through histone citrullination, playing a key role in innate immunity. Dysregulated PADI4 activity is implicated in the pathogenesis of autoimmune diseases, particularly rheumatoid arthritis, where it generates citrullinated proteins that trigger autoantibody production, and has also been linked to cancer and multiple sclerosis.