FLT1 D7 Human
Description
Molecular Structure and Production
FLT1 D7 Human is a soluble, glycosylated protein comprising the first seven extracellular immunoglobulin-like domains (Met1-Thr751) of FLT1 fused to the Fc region of human IgG1 . Key structural features include:
This construct retains VEGF-binding capacity while lacking transmembrane and intracellular tyrosine kinase domains, making it a decoy receptor .
Ligand Binding and Antagonism
-
High-Affinity VEGF Trap: Binds VEGF-A, VEGF-B, and placental growth factor (PlGF) with sub-nanomolar affinity, inhibiting downstream VEGFR-2 signaling .
-
Mechanism: Competes with membrane-bound VEGFR-1/VEGFR-2 for ligand binding, reducing angiogenic and inflammatory responses .
Angiogenesis Studies
FLT1 D7 Human is widely used to modulate VEGF signaling in experimental models:
-
Muscular Dystrophy: Systemic administration in mdx mice (a Duchenne muscular dystrophy model) improved muscle perfusion and reduced fibrosis by increasing capillary density .
-
Cancer Research: Suppresses tumor angiogenesis by sequestering VEGF, as demonstrated in xenograft models .
SARS-CoV-2 Spike Protein Interaction
A 2022 study identified FLT1 D7 as a novel binding partner for the SARS-CoV-2 spike receptor-binding domain (RBD), suggesting a potential role in COVID-19-related vascular pathology .
Comparative Analysis of FLT1 Constructs
Product Specs
Product Science Overview
Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Flt-1, is a high-affinity tyrosine kinase receptor that plays a crucial role in angiogenesis and vasculogenesis. It binds to several ligands, including VEGF-A, VEGF-B, and placental growth factor (PlGF) . The recombinant form of VEGFR-1 D1-7 (Human) is a truncated version that includes the first seven immunoglobulin-like domains of the extracellular region, which are essential for ligand binding.
VEGFR-1 is composed of an extracellular domain with seven immunoglobulin-like loops, a single transmembrane helix, and an intracellular tyrosine kinase domain. The D1-7 fragment specifically refers to the extracellular portion, which is responsible for binding VEGF ligands. This binding initiates a cascade of downstream signaling pathways that regulate endothelial cell proliferation, migration, and survival .
VEGFR-1 is primarily involved in the regulation of angiogenesis, the process by which new blood vessels form from pre-existing vessels. This receptor modulates the activity of VEGF-A, a potent angiogenic factor, by acting as a decoy receptor that sequesters VEGF-A, thereby preventing it from binding to VEGFR-2, which has a higher signaling activity . This regulatory mechanism is crucial for maintaining the balance between angiogenesis and vascular stability.
The expression of VEGFR-1 is upregulated in various pathological conditions, including cancer, where it contributes to tumor angiogenesis and metastasis. Inhibiting VEGFR-1 signaling has been explored as a therapeutic strategy to suppress tumor growth and progression . Additionally, VEGFR-1 is implicated in inflammatory diseases, where it mediates the recruitment of monocytes and macrophages to sites of inflammation .
The recombinant form of VEGFR-1 D1-7 is produced using recombinant DNA technology, which involves the insertion of the VEGFR-1 gene into an expression vector, followed by the expression of the protein in a suitable host system, such as insect cells . This recombinant protein is used in various research applications, including the study of VEGF signaling pathways, the development of anti-angiogenic therapies, and the screening of potential drug candidates.
