FLT1 D3 Human, His
Description
Formulation and Stability
Two primary formulations are documented:
Functional Properties and Mechanism
FLT1 D3 competes with full-length VEGFR-1/2 for VEGF binding, acting as a dominant-negative receptor.
Research Applications
FLT1 D3 is utilized in diverse contexts:
Table 1: Disease Models and Outcomes
Key Research Findings
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Alternative Splicing: sFLT1 isoforms generated by intronic polyadenylation regulate VEGF bioavailability, with implications in preeclampsia .
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Muscle Regeneration: VEGFA-FLT1-AKT1 signaling promotes muscle stem cell survival, suggesting therapeutic potential in dystrophy .
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Viral Interactions: FLT1 D3 binds SARS-CoV-2 spike RBD, raising questions about its role in viral tropism .
Product Specs
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 angiogenesis and vasculogenesis. It is part of the VEGF receptor family, which includes VEGFR-1, VEGFR-2, and VEGFR-3. These receptors are activated by binding to their respective ligands, the Vascular Endothelial Growth Factors (VEGFs), which are key regulators of blood vessel formation.
VEGFR-1 consists of an extracellular domain, a single transmembrane helix, and an intracellular tyrosine kinase domain. The extracellular domain is composed of seven immunoglobulin-like (Ig-like) domains, with the third domain (D3) being critical for ligand binding. The D3 domain of VEGFR-1 is responsible for high-affinity binding to VEGF-A, VEGF-B, and placental growth factor (PlGF).
VEGFR-1 acts primarily as a decoy receptor, sequestering VEGF ligands and preventing them from binding to VEGFR-2, which is the main mediator of angiogenic signaling. By modulating the availability of VEGF ligands, VEGFR-1 regulates angiogenesis and vascular permeability.
Recombinant VEGFR-1 D3 (Human, His Tag) is a truncated form of the receptor that includes the third Ig-like domain fused to a polyhistidine (His) tag. The His tag facilitates purification and detection of the recombinant protein using nickel affinity chromatography and anti-His antibodies, respectively.
The recombinant VEGFR-1 D3 is typically expressed in bacterial or mammalian expression systems. In bacterial systems, the gene encoding the D3 domain is cloned into an expression vector and transformed into Escherichia coli (E. coli) cells. The cells are then induced to produce the recombinant protein, which is subsequently purified using nickel affinity chromatography. In mammalian systems, the gene is transfected into Chinese hamster ovary (CHO) cells or other suitable cell lines, and the recombinant protein is secreted into the culture medium for purification.
Recombinant VEGFR-1 D3 is used in various research applications, including:
- Binding Studies: Investigating the interaction between VEGFR-1 and its ligands.
- Inhibition Assays: Evaluating the efficacy of potential inhibitors targeting VEGFR-1.
- Structural Studies: Analyzing the structure of the VEGFR-1 D3 domain to understand its binding mechanism.
- Therapeutic Development: Developing anti-angiogenic therapies for diseases such as cancer, where VEGF signaling plays a critical role in tumor growth and metastasis.
