抗人 CFL1 抗体对
01AB03371
Cofilin 1 (CFL1) is a fundamental regulator of actin cytoskeleton dynamics belonging to the ADF/cofilin superfamily. It functions by binding F-actin in a pH-dependent manner, leading to the severing and depolymerization of filaments. This activity is essential for promoting actin turnover and providing the monomer pool required for repolymerization during cell motility, adhesion, and migration. CFL1 activity is tightly regulated by LIMK1, which inactivates the protein via phosphorylation at Ser3. It also interacts with partners such as Arp2/3 and CAP1 to facilitate lamellipodia formation and mitotic spindle organization. Clinically, mutations or dysregulation of CFL1 are associated with developmental disorders, including Smith-Lemli-Opitz Syndrome and Baraitser-Winter Syndrome. Additionally, its role in promoting vasculogenic mimicry and cell invasion makes it a significant factor in breast cancer progression and neuronal migration defects.
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技术参数
- 靶点基因名
- CFL1
- 基因别名
- CFL
- 蛋白别名
- cofilin 1; CFL1
- UniProt
- P23528
- 物种
- Human
产品详情
- 靶点名称
- CFL1
- 蛋白名称
- cofilin 1
- 蛋白别名
- Cofilin-1; 18 kDa phosphoprotein; p18; Cofilin; non-muscle isoform
- 靶点基因名
- CFL1
- 基因别名
- CFL
- UniProt
- P23528
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Cofilin 1 (CFL1) is a fundamental regulator of actin cytoskeleton dynamics belonging to the ADF/cofilin superfamily. It functions by binding F-actin in a pH-dependent manner, leading to the severing and depolymerization of filaments. This activity is essential for promoting actin turnover and providing the monomer pool required for repolymerization during cell motility, adhesion, and migration. CFL1 activity is tightly regulated by LIMK1, which inactivates the protein via phosphorylation at Ser3. It also interacts with partners such as Arp2/3 and CAP1 to facilitate lamellipodia formation and mitotic spindle organization. Clinically, mutations or dysregulation of CFL1 are associated with developmental disorders, including Smith-Lemli-Opitz Syndrome and Baraitser-Winter Syndrome. Additionally, its role in promoting vasculogenic mimicry and cell invasion makes it a significant factor in breast cancer progression and neuronal migration defects.