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Human VEGFR-1/Flt-1 (native), soluble
Human VEGFR-1/Flt-1 (native), soluble
- 中文名称:
- Human VEGFR-1/Flt-1 (native), soluble
- 英文名称:
- Human VEGFR-1/Flt-1 (native), soluble
- 品牌:
- AAA Biotech
- 品牌介绍:
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具,核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号:
- AAA79126
- 规格:
- 0.005 mg|2x0.005 mg|3x0.005 mg|5x0.005 mg|4x0.005 mg
- 保存建议:
- Lyophilized samples are stable for greater than six months at –20°C to –70°C. Reconstituted sVEGFR-1 should be stored in working aliquots at -70°C.
- 货期:
- 6-8周
- 纯度:
- > 95% by SDS-PAGE & silver stain
- 产品形式:
- Lyophilized
- 免责声明:
- *本产品仅供科研实验使用,不得用于临床诊断。*
- 说明书:
Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.