人 EPHB6 抗体对
01AB00806
EPH receptor B6 (EPHB6) is a member of the Eph receptor tyrosine kinase family, notable for its lack of intrinsic kinase activity despite retaining a typical receptor structure. The human EPHB6 protein consists of 1006 amino acids, featuring a 563-residue extracellular domain with serine- and cysteine-rich regions and two fibronectin type-III domains, a 21-residue transmembrane segment, and a 406-residue cytoplasmic domain that includes a non-catalytic kinase-like domain, proline-rich, SAM, and PDZ-binding motifs. EPHB6 forms stable heterodimers with other Eph receptors, such as EphB1, and participates in signal transduction through associations with enzymatically active partners. It binds ephrin-B ligands and is involved in regulating cell adhesion and migration, particularly during development and in the nervous system. Functionally, EPHB6 acts as a tumor suppressor, with its expression downregulated in various cancers, and has been shown to suppress cancer invasiveness and cell attachment through c-Cbl-dependent signaling pathways.
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技术参数
- 靶点基因名
- EPHB6
- 蛋白别名
- EPH receptor B6; EPHB6
- UniProt
- O15197
- 物种
- Human
产品详情
- 靶点名称
- EPHB6
- 蛋白名称
- EPH receptor B6
- 蛋白别名
- Ephrin type-B receptor 6; HEP; Tyrosine-protein kinase-defective receptor EPH-6
- 靶点基因名
- EPHB6
- UniProt
- O15197
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
EPH receptor B6 (EPHB6) is a member of the Eph receptor tyrosine kinase family, notable for its lack of intrinsic kinase activity despite retaining a typical receptor structure. The human EPHB6 protein consists of 1006 amino acids, featuring a 563-residue extracellular domain with serine- and cysteine-rich regions and two fibronectin type-III domains, a 21-residue transmembrane segment, and a 406-residue cytoplasmic domain that includes a non-catalytic kinase-like domain, proline-rich, SAM, and PDZ-binding motifs. EPHB6 forms stable heterodimers with other Eph receptors, such as EphB1, and participates in signal transduction through associations with enzymatically active partners. It binds ephrin-B ligands and is involved in regulating cell adhesion and migration, particularly during development and in the nervous system. Functionally, EPHB6 acts as a tumor suppressor, with its expression downregulated in various cancers, and has been shown to suppress cancer invasiveness and cell attachment through c-Cbl-dependent signaling pathways.