FLT1 Human
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.
The FLT1 is purified by proprietary chromatographic techniques.
Product Specs
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH
Product Science Overview
Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Fms-like tyrosine kinase-1 (Flt-1), is a receptor tyrosine kinase that plays a crucial role in the regulation of angiogenesis and vasculogenesis. It is primarily expressed on endothelial cells and is involved in various physiological and pathological processes, including tumor growth, wound healing, and cardiovascular diseases .
VEGFR-1 is a member of the VEGF receptor family, which includes VEGFR-2 and VEGFR-3. It is composed of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tyrosine kinase domain. VEGFR-1 can exist in both membrane-bound and soluble forms due to alternative splicing events .
The receptor is widely expressed in normal and pathological tissues, including endothelial cells lining blood vessels, stromal cells, and various human cancer cells. Immunohistochemical studies have shown frequent VEGFR-1 expression in multiple malignancies, such as breast, lung, prostate, pancreas, ovarian, and colon cancers .
VEGFR-1 interacts with several ligands, including Vascular Endothelial Growth Factor-A (VEGF-A), VEGF-B, and Placental Growth Factor (PlGF). While VEGF-A can bind to both VEGFR-1 and VEGFR-2, VEGFR-1 is the only known receptor for VEGF-B and PlGF . The binding of these ligands to VEGFR-1 triggers a cascade of downstream signaling pathways that regulate endothelial cell proliferation, migration, and survival.
VEGFR-1 plays a dual role in angiogenesis. It acts as a decoy receptor by sequestering VEGF-A, thereby preventing its interaction with VEGFR-2, which is a more potent mediator of angiogenic signaling. This decoy function helps to fine-tune the angiogenic response and prevent excessive blood vessel formation .
In addition to its role as a decoy receptor, VEGFR-1 also promotes angiogenesis by activating endothelial cells and supporting cell types, such as stromal and hematopoietic cells. This activation is crucial for the formation of new blood vessels during embryonic development, wound healing, and tumor growth .
Recombinant human VEGFR-1 (rhVEGFR-1) is a biotechnologically engineered form of the receptor that is used in research and therapeutic applications. It is typically produced in Chinese hamster ovary (CHO) cells and purified using protein-A affinity chromatography . The recombinant protein retains the ability to bind VEGF-A and PlGF with high affinity, making it a valuable tool for studying VEGF signaling and developing anti-angiogenic therapies.
The therapeutic potential of targeting VEGFR-1 has been explored in various preclinical and clinical studies. For instance, IMC-18F1, a fully human IgG1 antibody that binds to VEGFR-1, has shown promise in inhibiting cancer growth in multiple in vitro and human tumor xenograft models . Recombinant VEGFR-1 has also been demonstrated to inhibit angiogenesis in vivo, making it a potential candidate for anti-angiogenic therapies in cancer and other diseases characterized by abnormal blood vessel formation .
