Mouse VEGF R1 / Flt-1 Protein, Mouse IgG2a Fc Tag, low endotoxin

Source : 

Mouse VEGF R1, Mouse IgG2a Fc Tag, low endotoxin (VE1-M5256) is expressed from human 293 cells (HEK293). It contains AA Tyr 23 - Glu 759 (Accession # P35969-1).

 

Molecule : VEGF R1

 

Synonyms : FLT,VEGFR1,FLT1

 

Format : Powder

 

Category : Bio-Markers & CD Antigens

 

Accession : NP_034358.2

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 109.8 kDa

 

Characteristics :

This protein carries a mouse IgG2a Fc tag at the C-terminus. The protein has a calculated MW of 109.8 kDa. The protein migrates as 140 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

 

Endotoxin Level : Less than 0.1 EU per μg by the LAL method.

 

Buffer : 50 mM Tris, 100 mM Glycine, pH7.5

 

Description :

Vascular endothelial growth factor receptor 1 (VEGFR1) is also known as Fms-like tyrosine kinase 1 (FLT-1), Tyrosine-protein kinase receptor FLT, is a single-pass type I membrane protein and secreted protein which belongs to the protein kinase superfamily, Tyr protein kinase family and CSF-1/PDGF receptor subfamily. VEGFR1 is detected in normal lung, but also in placenta, liver, kidney, heart and brain tissues and specifically expressed in most of the vascular endothelial cells, and also expressed in peripheral blood monocytes. VEGFR1 acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. VEGFR1 may play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. VEGFR1 can promote endothelial cell proliferation, survival and angiogenesis in adulthood.

 

References :

(1) Shibuya M., et al., 1990, Oncogene 5:519-524.
(2) Kendall R.L., et al., 1993, Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709.
(3) Seetharam L., et al., 1995, Oncogene 10:135-147.
(4) Barleon B., et al., 1996, Blood 87:3336-3343.
(5) Grunewald F.S., et al., 2010, Biochim. Biophys. Acta 1804:567-580.
(6) Iyer S., et al., 2010, J. Biol. Chem. 285:23779-23789.