FLT1 Human, His
Description
The FLT1 His is purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Fms-like tyrosine kinase 1 (FLT1), is a high-affinity tyrosine kinase receptor for Vascular Endothelial Growth Factor (VEGF). VEGFR-1 plays a crucial role in the regulation of angiogenesis, the process by which new blood vessels form from pre-existing vessels. This receptor is involved in various physiological and pathological processes, including embryonic development, wound healing, and tumor growth.
VEGFR-1 is a transmembrane protein that consists of an extracellular ligand-binding domain, a single transmembrane helix, and an intracellular tyrosine kinase domain. The extracellular domain of VEGFR-1 binds to VEGF-A, VEGF-B, and Placental Growth Factor (PGF), mediating the activation of signaling pathways that promote endothelial cell proliferation, migration, and survival .
VEGFR-1 is considered a decoy receptor because it binds VEGF with high affinity but has a weaker tyrosine kinase activity compared to VEGFR-2. This binding limits the availability of VEGF for VEGFR-2, thereby modulating angiogenic signaling. VEGFR-1 also plays a role in macrophage migration through the activation of phospholipase C gamma (PLCγ) and phosphoinositide 3-kinase (PI3K) signaling pathways .
Recombinant human VEGFR-1 is produced using various expression systems, including mammalian cells and bacteria. The recombinant protein typically includes a His tag at the C-terminus to facilitate purification using nickel affinity chromatography. The His tag allows for efficient isolation of the protein from the expression system, ensuring high purity and yield.
The recombinant VEGFR-1 protein encompasses amino acids 27-756, corresponding to the extracellular domain of the receptor. This construct may also include additional tags, such as an Fc domain of human IgG1 or an Avi-tag™, to enhance stability and facilitate detection .
Recombinant VEGFR-1 is widely used in research to study angiogenesis and related signaling pathways. It serves as a valuable tool for investigating the mechanisms of VEGF-mediated endothelial cell functions and for screening potential therapeutic agents targeting VEGF signaling. Additionally, recombinant VEGFR-1 is utilized in various assays, including binding studies, cell migration assays, and in vivo angiogenesis models .
