推荐产品
生物源
human
品質等級
重組細胞
expressed in baculovirus infected Sf21 cells
化驗
>90% (SDS-PAGE)
形狀
lyophilized powder
效力
≤35 ng/mL ED50
分子量
predicted mol wt ~100 kDa
包裝
pkg of 50 μg
儲存條件
avoid repeated freeze/thaw cycles
雜質
endotoxin, tested
UniProt登錄號
儲存溫度
−20°C
基因資訊
human ... FLT1(2321)
應用
VEGF Receptor-1 (Flt-1)/Fc chimera human may be used tostudy vasculogenesis and angiogenesis.
生化／生理作用
VEGF Receptor-1 (VEGF R1) also known as Flt-1 belongs to class III subfamily of RTKs and is a potent VEGF antagonist expressed mainly in endothelial cells. VEGF R1 binds to vascular endothelial growth factor B (VEGF-B) and regulates the activity of plasminogen activator in endothelial cells. It also assists endothelial cells in the proper spatial organization of lumen-containing vessels. Additionally, alternatively spliced VEGF R1 pre-mRNA helps in regulating the VEGF activity in angiogenesis. VEGF R1 also activates PLC gamma which in turn produces cellular signaling molecules diacylglycerol as well as inositol 1,4,5-trisphosphate and activates protein kinase C.
VEGF receptors, class III receptor tyrosine kinases, have seven Ig like extracellular motifs and a tyrosine kinase intracellular domain split by a kinase insert sequence. VEGFR 1 was originally called fms like tyrosine kinase 1 (flt 1), indicating its homology to receptors of PDGF, M CSF, and SCF. VEGFR 1 is one of the five receptor tyrosine kinases (KDR/Flk-1, Flt-4, tie-1 and tek/tie-2) whose expression is almost exclusively restricted to endothelial cells. These receptors are likely to play central roles in vasculogenesis and angiogenesis. Recombinant VEGF R1 binds VEGF with high affinity and is a potent VEGF inhibitor. VEGFR 1 and 2 are both expressed in an endothelial cell-specific manner and are detectable in virtually all tissues in adults and embryos. Hypoxia induces endothelial cell expression of VEGFR 1 but not VEGFR 2. Monocytes express VEGFR 1 and 2 and can migrate to the site of VEGF release, but this response appears to be VEGFR 1 mediated. VEGFR 2 is also expressed in pancreatic duct cells. VEGFR 2 is involved in commitment of endothelial-cell lineages and to cell proliferation, while VEGFR 1 seems to be responsible for guiding endothelial cells into the proper spatial organization into lumen-containing vessels. VEGFR 2 is a key marker for pluripotent HSCs. Neurophilins, a group of unrelated receptors for some VEGF family members may also act as coreceptors to facilitate VEGF binding to VEGFR 2. VEGFR 3 is a specific marker for lymphatic vessels. VEGFR 3 has also been detected on some high endothelial venules, in embryonic pre-lymphatic blood vessels, some tumor blood vessels, and certain hematopoietic and leukemia cells.
外觀
Lyophilized from a 0.2 μm filtered solution in 20 mM MOPS, 500 mM sodium chloride, 0.05% CHAPS, pH 7.0 containing 50 μg bovine serum albumin per 1 μg of cytokine
分析報告
The biological activity is measured by its ability to Inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells.
儲存類別代碼
13 - Non Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
Y He et al.
Molecular endocrinology (Baltimore, Md.), 13(4), 537-545 (1999-04-09)
Angiogenesis is essential for normal mammalian development and is controlled by the local balance of pro- and antiangiogenic factors. Here we describe a novel mouse cDNA sequence encoding sFLT-1 that is a potent antagonist to vascular endothelial growth factor (VEGF)
A Sawano et al.
Biochemical and biophysical research communications, 238(2), 487-491 (1997-09-23)
Flt-1, a tyrosine kinase receptor for vascular endothelial growth factor (VEGF), plays important roles in the angiogenesis required for embryogenesis and in monocyte/macrophage migration. However, the signal transduction of Flt-1 is poorly understood due to its very weak tyrosine kinase
B Olofsson et al.
Proceedings of the National Academy of Sciences of the United States of America, 95(20), 11709-11714 (1998-09-30)
The vascular endothelial growth factor (VEGF) family has recently expanded by the identification and cloning of three additional members, namely VEGF-B, VEGF-C, and VEGF-D. In this study we demonstrate that VEGF-B binds selectively to VEGF receptor-1/Flt-1. This binding can be
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