抗人 VEGF 受体 2 抗体对
01AB01187
Kinase insert domain receptor (KDR), also known as vascular endothelial growth factor receptor 2 (VEGFR-2) or CD309, is a type IV receptor tyrosine kinase encoded by the KDR gene in humans and plays a central role in mediating the effects of vascular endothelial growth factor (VEGF) on endothelial cells. Structurally, KDR is a transmembrane protein characterized by extracellular immunoglobulin-like domains, a single transmembrane region, and an intracellular tyrosine kinase domain; its extracellular domains are critical for ligand binding and receptor dimerization, while the intracellular kinase domain transduces signals that regulate angiogenesis, vascular permeability, and endothelial cell proliferation. KDR interacts with several proteins, including SHC1, SHC2, and Annexin A5, and its activity is tightly regulated by structural features within its immunoglobulin-like domains. Dysregulation or overexpression of KDR is implicated in various diseases, most notably cancer, where it contributes to tumor angiogenesis and progression, and specific KDR genetic variants have been associated with altered microvessel density in non-small cell lung cancer.
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技术参数
- 靶点基因名
- KDR
- 基因别名
- FLK1; VEGFR2
- 蛋白别名
- kinase insert domain receptor; VEGF Receptor 2
- UniProt
- P35968
- 物种
- Human
产品详情
- 靶点名称
- VEGF Receptor 2
- 蛋白名称
- kinase insert domain receptor
- 蛋白别名
- Vascular endothelial growth factor receptor 2; VEGFR-2; Fetal liver kinase 1; FLK-1; Kinase insert domain receptor; KDR; Protein-tyrosine kinase receptor flk-1; CD antigen CD309
- 靶点基因名
- KDR
- 基因别名
- FLK1; VEGFR2
- UniProt
- P35968
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Kinase insert domain receptor (KDR), also known as vascular endothelial growth factor receptor 2 (VEGFR-2) or CD309, is a type IV receptor tyrosine kinase encoded by the KDR gene in humans and plays a central role in mediating the effects of vascular endothelial growth factor (VEGF) on endothelial cells. Structurally, KDR is a transmembrane protein characterized by extracellular immunoglobulin-like domains, a single transmembrane region, and an intracellular tyrosine kinase domain; its extracellular domains are critical for ligand binding and receptor dimerization, while the intracellular kinase domain transduces signals that regulate angiogenesis, vascular permeability, and endothelial cell proliferation. KDR interacts with several proteins, including SHC1, SHC2, and Annexin A5, and its activity is tightly regulated by structural features within its immunoglobulin-like domains. Dysregulation or overexpression of KDR is implicated in various diseases, most notably cancer, where it contributes to tumor angiogenesis and progression, and specific KDR genetic variants have been associated with altered microvessel density in non-small cell lung cancer.