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Human VEGFR-1/Flt-1 (D5), soluble
Human VEGFR-1/Flt-1 (D5), soluble
- 中文名称：
- Human VEGFR-1/Flt-1 (D5), soluble
- 英文名称：
- Human VEGFR-1/Flt-1 (D5), 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：
- AAA79174
- 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 degree C to -70 degree C. Reconstituted sVEGFR-1(D5) should be stored in working aliquots at -70 degree C.
- 货期：
- 6-8周
- 纯度：
- > 90% 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 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. 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), 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 splited 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 occuring 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.
