Ligand antagonism: Soluble FLT1 (sFLT1) acts as a decoy receptor, sequestering VEGF-A and inhibiting its interaction with signaling receptors like KDR (VEGFR2) .
Regulation of angiogenesis: Overexpression of sFLT1 reduces endothelial cell proliferation and angiogenesis in vitro .
Inhibition of VEGF signaling: HEK293-derived FLT1 reduced VEGF-A-mediated phosphorylation of KDR in HUVECs by 60–80% (Fig. 2A–B in ).
Stability: Lyophilized FLT1 remains stable for >6 months at -70°C, with reconstituted activity maintained in PBS or cell culture media .
Thermodynamic activity: Retains ligand-binding capacity even at 4°C, confirming stability under non-endocytic conditions .
FLT1 Human, HEK Active is utilized in:
Angiogenesis assays: Inhibits VEGF-dependent proliferation of endothelial cells (EC50: 0.5–2 nM) .
Drug discovery: Screens for anti-angiogenic compounds targeting VEGF pathways .
Disease modeling: Used to study pathologies like cancer, diabetic retinopathy, and preeclampsia, where VEGF dysregulation is implicated .
Functional variability: Glycosylation patterns in HEK293 cells may differ slightly from native human endothelial cells, requiring validation in physiological models .
Clinical relevance: Longevity-associated FLT1 SNPs (e.g., rs3794396) suggest genetic modulation of VEGF pathways could influence age-related diseases .
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
SKLKDPELSL KGTQHIMQAG QTLHLQCRGE AAHKWSLPEM VSKESERLSI TKSACGRNGK QFCSTLTLNT AQANHTGFYS CKYLAVPTSK KKETESAIYI FISDTGRPFV EMYSEIPEII HMTEGRELVI PCRVTSPNIT VTLKKFPLDT LIPDGKRIIW DSRKGFIISN ATYKEIGLLT CEATVNGHLY KTNYLTHRQT NTIIDVQIST PRPVKLLRGH TLVLNCTATT PLNTRVQMTW SYPDEKNKRA SVRRRIDQSN SHANIFYSVL TIDKMQNKDK GLYTCRVRSG PSFKSVNTSV HILEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK.
Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Fms-like tyrosine kinase-1 (FLT1), is a member of the VEGF receptor family. It plays a crucial role in the regulation of angiogenesis, which is the formation of new blood vessels from pre-existing ones. This process is vital for both physiological and pathological conditions, including embryonic development, wound healing, and tumor growth .
VEGFR-1 is a receptor tyrosine kinase that is activated by binding to its ligands, which include VEGF-A, VEGF-B, and placental growth factor (PGF) . Upon ligand binding, VEGFR-1 undergoes dimerization and autophosphorylation, leading to the activation of downstream signaling pathways that regulate cell survival, migration, and proliferation .
VEGFR-1 acts as a decoy receptor, sequestering VEGF and preventing it from binding to VEGFR-2, which is the primary mediator of angiogenic signaling . This regulatory mechanism ensures a balance between angiogenesis and vascular stability. VEGFR-1 is also involved in the recruitment of monocytes and macrophages to sites of inflammation and tissue repair .
Recombinant human VEGFR-1 is produced using various expression systems, including HEK 293 cells, which are human embryonic kidney cells . The recombinant protein is used in research to study its role in angiogenesis and to develop therapeutic strategies for diseases characterized by abnormal blood vessel growth, such as cancer and age-related macular degeneration .
The study of VEGFR-1 has significant implications for understanding and treating various diseases. In cancer research, VEGFR-1 is targeted to inhibit tumor angiogenesis, thereby restricting tumor growth and metastasis . Additionally, VEGFR-1 is explored in therapies for ocular diseases, where abnormal blood vessel growth leads to vision loss .