人 α-2-巨球蛋白抗体对
01AB03472
Alpha-2-macroglobulin (A2M) is a ~720-kDa tetrameric plasma glycoprotein composed of four identical subunits, each containing 1451 amino acids, that functions as a broad-spectrum protease inhibitor in the innate immune system. The protein exhibits a distinctive hollow cylindrical structure with two identical functional halves and operates through a "trap mechanism" involving a flexible bait region that serves as an exceptionally good substrate for endopeptidases of all catalytic types. Upon protease cleavage of the bait region, A2M undergoes a conformational transition from an expanded to a compact state, trapping active proteases within its tetrameric cage while simultaneously exposing a reactive thioester bond that covalently links the captured protease, further stabilizing the enzyme-inhibitor complex. This dual mechanism—steric entrapment and covalent modification—allows A2M to selectively inhibit large substrate proteolysis while permitting small peptide digestion. A2M dysfunction is implicated in various pathological conditions including inflammation, infection, and immune disorders, where dysregulated protease activity contributes to tissue damage and disease progression.
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技术参数
- 靶点基因名
- A2M
- 基因别名
- CPAMD5
- 蛋白别名
- alpha-2-macroglobulin; Alpha-2-Macroglobulin
- UniProt
- P01023
- 物种
- Human
产品详情
- 靶点名称
- Alpha-2-Macroglobulin
- 蛋白名称
- alpha-2-macroglobulin
- 蛋白别名
- Alpha-2-macroglobulin; Alpha-2-M; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5
- 靶点基因名
- A2M
- 基因别名
- CPAMD5
- UniProt
- P01023
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Alpha-2-macroglobulin (A2M) is a ~720-kDa tetrameric plasma glycoprotein composed of four identical subunits, each containing 1451 amino acids, that functions as a broad-spectrum protease inhibitor in the innate immune system. The protein exhibits a distinctive hollow cylindrical structure with two identical functional halves and operates through a "trap mechanism" involving a flexible bait region that serves as an exceptionally good substrate for endopeptidases of all catalytic types. Upon protease cleavage of the bait region, A2M undergoes a conformational transition from an expanded to a compact state, trapping active proteases within its tetrameric cage while simultaneously exposing a reactive thioester bond that covalently links the captured protease, further stabilizing the enzyme-inhibitor complex. This dual mechanism—steric entrapment and covalent modification—allows A2M to selectively inhibit large substrate proteolysis while permitting small peptide digestion. A2M dysfunction is implicated in various pathological conditions including inflammation, infection, and immune disorders, where dysregulated protease activity contributes to tissue damage and disease progression.