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Recombinant Human Vascular Endothelial Growth Factor receptor-1 D1-3, His Tag
Recombinant Human Vascular Endothelial Growth Factor receptor-1 D1-3, His Tag
- 中文名称：
- Recombinant Human Vascular Endothelial Growth Factor receptor-1 D1-3, His Tag
- 英文名称：
- Recombinant Human Vascular Endothelial Growth Factor receptor-1 D1-3, His Tag
- 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：
- AAA38417
- 规格：
- 0.002 mg|0.01 mg|1 mg|2x1 mg|3x1 mg
- 保存建议：
- Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. Please avoid freeze thaw cycles.
- 货期：
- 6-8周
- 纯度：
- Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
- 产品形式：
- FLT1 His (0.96mg/ml) is supplied in 25mM Na-Acetate pH 4.8 and 50% glycerol.
Sterile Filtered clear solution.
- 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：
Description: FLT1 D1-3 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 298 amino acids fragment (31-328) and having a molecular mass of 38.16kDa. The receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.
Introduction: 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 HUVE 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.
