人 beta Dystroglycan 抗体对
01AB00486
Dystroglycan 1 (DAG1) is a protein encoded by the DAG1 gene on chromosome 3 in humans. It is a central component of the dystrophin-glycoprotein complex, which links the extracellular matrix to the cytoskeleton, providing structural integrity in muscle tissues. The protein is initially synthesized as a 97 kDa precursor that undergoes post-translational processing to yield two non-covalently associated subunits: alpha-dystroglycan, an extracellular protein that binds to alpha-laminin (merosin), and beta-dystroglycan, a transmembrane protein that binds to dystrophin and intracellular actin cables. Dystroglycan plays crucial roles in muscle function and is also expressed in non-muscle tissues, including the brain and neural retina. Abnormal dystroglycan expression and/or O-mannosylation have been implicated in the pathogenesis of cancer.
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技术参数
- 靶点基因名
- DAG1
- 蛋白别名
- dystroglycan 1; beta Dystroglycan
- UniProt
- Q14118
- 物种
- Human
产品详情
- 靶点名称
- beta Dystroglycan
- 蛋白名称
- dystroglycan 1
- 蛋白别名
- Dystroglycan 1; Dystroglycan; Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan; Alpha-DG; Beta-dystroglycan; Beta-DG]
- 靶点基因名
- DAG1
- UniProt
- Q14118
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Dystroglycan 1 (DAG1) is a protein encoded by the DAG1 gene on chromosome 3 in humans. It is a central component of the dystrophin-glycoprotein complex, which links the extracellular matrix to the cytoskeleton, providing structural integrity in muscle tissues. The protein is initially synthesized as a 97 kDa precursor that undergoes post-translational processing to yield two non-covalently associated subunits: alpha-dystroglycan, an extracellular protein that binds to alpha-laminin (merosin), and beta-dystroglycan, a transmembrane protein that binds to dystrophin and intracellular actin cables. Dystroglycan plays crucial roles in muscle function and is also expressed in non-muscle tissues, including the brain and neural retina. Abnormal dystroglycan expression and/or O-mannosylation have been implicated in the pathogenesis of cancer.