抗人 BID 抗体对
01AB00737
BH3 interacting domain death agonist (BID) is a pro-apoptotic member of the Bcl-2 protein family, characterized by containing only the BH3 domain, which is essential for its interaction with other Bcl-2 family proteins and its pro-death activity. BID acts as a sentinel for protease-mediated death signals and serves as a crucial link between the death receptor and mitochondrial pathways of apoptosis, particularly by promoting mitochondrial outer membrane permeabilization through direct activation of Bax or Bak, leading to the release of cytochrome c and other apoptogenic factors. BID is activated by proteolytic cleavage, most notably by caspases, resulting in truncated BID (tBID) that translocates to mitochondria to amplify apoptotic signaling. In terms of disease relevance, BID is upregulated by the tumor suppressor p53 and plays a significant role in p53-mediated apoptosis, implicating it in cancer biology and the cellular response to stress and DNA damage.
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技术参数
- 靶点基因名
- BID
- 蛋白别名
- BH3 interacting domain death agonist; BID
- UniProt
- P55957
- 物种
- Human
产品详情
- 靶点名称
- BID
- 蛋白名称
- BH3 interacting domain death agonist
- 蛋白别名
- BH3-interacting domain death agonist; p22 BID; BID) [Cleaved into: BH3-interacting domain death agonist p15; p15 BID; BH3-interacting domain death agonist p13; p13 BID; BH3-interacting domain death agonist p11; p11 BID]
- 靶点基因名
- BID
- UniProt
- P55957
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
BH3 interacting domain death agonist (BID) is a pro-apoptotic member of the Bcl-2 protein family, characterized by containing only the BH3 domain, which is essential for its interaction with other Bcl-2 family proteins and its pro-death activity. BID acts as a sentinel for protease-mediated death signals and serves as a crucial link between the death receptor and mitochondrial pathways of apoptosis, particularly by promoting mitochondrial outer membrane permeabilization through direct activation of Bax or Bak, leading to the release of cytochrome c and other apoptogenic factors. BID is activated by proteolytic cleavage, most notably by caspases, resulting in truncated BID (tBID) that translocates to mitochondria to amplify apoptotic signaling. In terms of disease relevance, BID is upregulated by the tumor suppressor p53 and plays a significant role in p53-mediated apoptosis, implicating it in cancer biology and the cellular response to stress and DNA damage.