FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Filtered clear solution.
Greater than 90.0% as determined by SDS-PAGE.
FLT1 Human Recombinant is a single, glycosylated polypeptide chain containing 535 amino acids (27-328a.a) and having a molecular mass of 60.3kDa (calculated). FLT1 is fused to a 233 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.
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 .