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抗人 MDGA1 抗体对
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抗人 MDGA1 抗体对

01AB00899

MAM domain containing glycosylphosphatidylinositol anchor 1 (MDGA1) is a 135–140 kDa glycoprotein in the IgCAM superfamily, predominantly expressed in the developing nervous system and anchored to the cell surface via a GPI anchor. The mature human MDGA1 protein consists of 914 amino acids and features six Ig-like domains, a fibronectin type III domain, a MAM domain, and a GPI anchor, with high sequence conservation across mammals. Functionally, MDGA1 mediates neuronal migration, neurite outgrowth, and cell-cell adhesion, playing a crucial role in early CNS development. It regulates synaptic formation by sterically blocking neurexin access to neuroligins, thereby modulating neuroligin-neurexin trans-synaptic bridges and suppressing synaptic inhibition, particularly at GABAergic synapses. Disease relevance includes its negative regulation of amyloid precursor protein (APP)-mediated synaptic inhibition, implicating MDGA1 in the modulation of inhibitory synaptic transmission and potentially in neurodevelopmental or neurodegenerative disorders.

Human
规格起售价
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技术参数

靶点基因名
MDGA1
基因别名
MAMDC3
蛋白别名
MAM domain containing glycosylphosphatidylinositol anchor 1; MDGA1
UniProt
Q8NFP4
物种
Human

产品详情

靶点名称
MDGA1
蛋白名称
MAM domain containing glycosylphosphatidylinositol anchor 1
蛋白别名
MAM domain-containing glycosylphosphatidylinositol anchor protein 1; GPI and MAM protein; GPIM; Glycosylphosphatidylinositol-MAM; MAM domain-containing protein 3
靶点基因名
MDGA1
基因别名
MAMDC3
UniProt
Q8NFP4
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

MAM domain containing glycosylphosphatidylinositol anchor 1 (MDGA1) is a 135–140 kDa glycoprotein in the IgCAM superfamily, predominantly expressed in the developing nervous system and anchored to the cell surface via a GPI anchor. The mature human MDGA1 protein consists of 914 amino acids and features six Ig-like domains, a fibronectin type III domain, a MAM domain, and a GPI anchor, with high sequence conservation across mammals. Functionally, MDGA1 mediates neuronal migration, neurite outgrowth, and cell-cell adhesion, playing a crucial role in early CNS development. It regulates synaptic formation by sterically blocking neurexin access to neuroligins, thereby modulating neuroligin-neurexin trans-synaptic bridges and suppressing synaptic inhibition, particularly at GABAergic synapses. Disease relevance includes its negative regulation of amyloid precursor protein (APP)-mediated synaptic inhibition, implicating MDGA1 in the modulation of inhibitory synaptic transmission and potentially in neurodevelopmental or neurodegenerative disorders.