FLT1 (Protein | Antibody | cDNA Clone | ELISA Kit)

All FLT1 reagents are produced in house and quality controlled, including 9 FLT1 Antibody, 52 FLT1 Gene, 4 FLT1 Lysate, 4 FLT1 Protein, 3 FLT1 qPCR. All FLT1 reagents are ready to use.

FLT1 Protein (4)

FLT1 Antibody (9)

FLT1 cDNA Clone (52)

NM_001159920.1
NM_002019.2
NM_010228.3
NM_019306.1

FLT1 Lysate (4)

FLT1 Background

Vascular endothelial growth factor receptor 1, also known as VEGFR-1, Fms-like tyrosine kinase 1, Tyrosine-protein kinase FRT, Tyrosine-protein kinase receptor FLT, Vascular permeability factor receptor and FLT1, is a single-pass type I membrane protein and secreted protein which belongs to theprotein kinase superfamily, Tyr protein kinase family and CSF-1/PDGF receptor subfamily. VEGFR-1 / FLT1 contains sevenIg-like C2-type (immunoglobulin-like) domains and oneprotein kinase domain. VEGFR-1 / FLT1 is expressed mostly in normal lung, but also in placenta, liver, kidney, heart and brain tissues. It is specifically expressed in most of the vascular endothelial cells, and also expressed in peripheral blood monocytes. VEGFR-1 / FLT1 is not expressed in tumor cell lines. VEGFR-1 / FLT1 is an essential receptor tyrosine kinase that regulates mammalian vascular development and embryogenesis. EGF-induced angiogenesis requires inverse regulation of VEGFR-1 and VEGFR-2 in tumor-associated endothelial cells. VEGFR-1 / FLT1 is a receptor for VEGF, VEGFB and PGF. It has a tyrosine-protein kinase activity. The VEGF-kinase ligand/receptor signaling system plays a key role in vascular development and regulation of vascular permeability.

FLT1 References

  • Shibuya M., et al.,(1990), Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family. Oncogene 5:519-524.
  • Kendall R.L., et al., (1993), Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor.Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709.
  • Herley M.T., et al.,(1999), Characterization of the VEGF binding site on the Flt-1 receptor.Biochem. Biophys. Res. Commun. 262:731-738.