抗人 WAS 抗体对
01AB00984
The Wiskott-Aldrich Syndrome Protein (WASP) is a key actin nucleation-promoting factor that regulates the dynamics of the actin cytoskeleton through activation of the Arp2/3 complex. WASP facilitates the formation of branched actin filaments, crucial for cellular processes such as endocytosis, cell migration, and immune synapse formation. Its activity is tightly regulated by interactions with Rho-family GTPases and its conserved WH2-Central-Acidic (WCA) domain, which binds actin monomers and the Arp2/3 complex. WASP’s efficiency in actin nucleation varies among family members due to differences in their acidic C-terminal residues, influencing the architecture of actin networks they produce. Mutations in the WAS gene disrupt normal WASP function, leading to diseases like Wiskott-Aldrich Syndrome (WAS), an X-linked disorder characterized by immune deficiencies, thrombocytopenia, and eczema. These mutations often result in unregulated actin polymerization, impairing hematopoietic cell functions and increasing susceptibility to infections.
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技术参数
- 靶点基因名
- WAS
- 基因别名
- IMD2
- 蛋白别名
- WASP actin nucleation promoting factor; WAS
- UniProt
- P42768
- 物种
- Human
产品详情
- 靶点名称
- WAS
- 蛋白名称
- WASP actin nucleation promoting factor
- 蛋白别名
- Actin nucleation-promoting factor WAS; Wiskott-Aldrich syndrome protein; WASp
- 靶点基因名
- WAS
- 基因别名
- IMD2
- UniProt
- P42768
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
The Wiskott-Aldrich Syndrome Protein (WASP) is a key actin nucleation-promoting factor that regulates the dynamics of the actin cytoskeleton through activation of the Arp2/3 complex. WASP facilitates the formation of branched actin filaments, crucial for cellular processes such as endocytosis, cell migration, and immune synapse formation. Its activity is tightly regulated by interactions with Rho-family GTPases and its conserved WH2-Central-Acidic (WCA) domain, which binds actin monomers and the Arp2/3 complex. WASP’s efficiency in actin nucleation varies among family members due to differences in their acidic C-terminal residues, influencing the architecture of actin networks they produce. Mutations in the WAS gene disrupt normal WASP function, leading to diseases like Wiskott-Aldrich Syndrome (WAS), an X-linked disorder characterized by immune deficiencies, thrombocytopenia, and eczema. These mutations often result in unregulated actin polymerization, impairing hematopoietic cell functions and increasing susceptibility to infections.