Human VEGF R1 / Flt-1 Protein, His Tag

Proteins and Peptides

貨號 Cat. No.
VE1-H5220
規格 Size
1mg
品牌 Brand
ACROBiosystems
Species
Human
Conjugate
Unconjugated
Expression System
HEK293
Tag
His Tag

Description




Source : 


Human VEGF R1, His Tag (VE1-H5220) is expressed from human 293 cells (HEK293). It contains AA Ser 27 - Asn 756 (Accession # NP_002010.1).


 

Molecule : VEGF R1


 

Synonyms : FLT,VEGFR1,FLT1


 

Format : Powder


 

Category : Bio-Markers & CD Antigens


 

Accession : NP_002010.1


 

Storage : -20℃


 

Shipping condition : Powder,RT


 

Molecular Weight : 83.3 kDa


 

Characteristics :


This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 83.3 kDa. The protein migrates as 110-130 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.


 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.


 

Buffer : PBS, pH7.4


 

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.





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