抗人 LRP2BP 抗体对
01AB01209
LRP2 binding protein (LRP2BP) is a protein that likely functions as an adapter regulating the activity of LRP2 (also known as megalin), a large transmembrane receptor involved in endocytosis. LRP2 itself is a giant, single-pass transmembrane glycoprotein (~600 kDa) expressed mainly in absorptive epithelial cells, such as those in the kidney proximal tubule and thyroid. Structurally, LRP2 forms a homodimer with multiple domains including LDL receptor type A repeats, EGF-like domains, and β-propeller domains, enabling it to bind over 75 ligands. Its conformation changes in response to pH, facilitating ligand binding at the cell surface and ligand release in endosomes. LRP2BP is thought to modulate this receptor’s function, possibly influencing its ligand binding or trafficking. Dysfunction of LRP2 is linked to diseases such as proteinuria, kidney disorders, and brain-related pathologies, with some missense mutations impairing LRP2 homodimer assembly and function, thereby contributing to disease mechanisms. LRP2BP’s regulatory role suggests it may be involved in these pathological processes by affecting LRP2 activity.
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技术参数
- 靶点基因名
- LRP2BP
- 基因别名
- KIAA1325
- 蛋白别名
- LRP2 binding protein; LRP2BP
- UniProt
- Q9P2M1
- 物种
- Human
产品详情
- 靶点名称
- LRP2BP
- 蛋白名称
- LRP2 binding protein
- 蛋白别名
- LRP2-binding protein; Megalin-binding protein; MegBP
- 靶点基因名
- LRP2BP
- 基因别名
- KIAA1325
- UniProt
- Q9P2M1
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
LRP2 binding protein (LRP2BP) is a protein that likely functions as an adapter regulating the activity of LRP2 (also known as megalin), a large transmembrane receptor involved in endocytosis. LRP2 itself is a giant, single-pass transmembrane glycoprotein (~600 kDa) expressed mainly in absorptive epithelial cells, such as those in the kidney proximal tubule and thyroid. Structurally, LRP2 forms a homodimer with multiple domains including LDL receptor type A repeats, EGF-like domains, and β-propeller domains, enabling it to bind over 75 ligands. Its conformation changes in response to pH, facilitating ligand binding at the cell surface and ligand release in endosomes. LRP2BP is thought to modulate this receptor’s function, possibly influencing its ligand binding or trafficking. Dysfunction of LRP2 is linked to diseases such as proteinuria, kidney disorders, and brain-related pathologies, with some missense mutations impairing LRP2 homodimer assembly and function, thereby contributing to disease mechanisms. LRP2BP’s regulatory role suggests it may be involved in these pathological processes by affecting LRP2 activity.