Vascular Endothelial Growth Factor Receptor-1 D3 Human Recombinant
FLT1 D1-3 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 327 amino acids and having a molecular mass of 45 kDa.
The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF.
The FLT1 is purified by proprietary chromatographic techniques.
Vascular Endothelial Growth Factor Receptor-1 D3 Human Recombinant, His Tag
Vascular Endothelial Growth Factor Receptor-1 D4 Human Recombinant
Vascular Endothelial Growth Factor Receptor-1 D5 Human Recombinant
Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant
Vascular Endothelial Growth Factor Receptor-1 D1-7 Mouse Recombinant
Vascular Endothelial Growth Factor Receptor-1 Human Recombinant
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.
Vascular Endothelial Growth Factor receptor-1 Human Recombinant, HEK Active
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.
Vascular Endothelial Growth Factor receptor-1 Human Recombinant, His Tag
Vascular Endothelial Growth Factor Receptor-3 Fc Chimera Human Recombinant
Vascular Endothelial Growth Factor (VEGF) receptors (VEGFRs) are a family of receptor tyrosine kinases that play a crucial role in angiogenesis and vasculogenesis. There are three main subtypes of VEGFRs: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4) . These receptors can be membrane-bound or soluble, depending on alternative splicing .
Key Biological Properties: VEGFRs have an extracellular portion with seven immunoglobulin-like domains, a single transmembrane region, and an intracellular portion containing a split tyrosine-kinase domain .
Expression Patterns and Tissue Distribution: VEGFR-1 and VEGFR-2 are primarily expressed in vascular endothelial cells, while VEGFR-3 is mainly found in lymphatic endothelial cells . VEGFR-1 acts as a decoy receptor, modulating VEGFR-2 signaling, whereas VEGFR-2 mediates most of the known cellular responses to VEGF . VEGFR-3 is involved in lymphangiogenesis, responding to VEGF-C and VEGF-D .
Primary Biological Functions: VEGFRs are essential for endothelial cell proliferation, migration, and survival . They play a pivotal role in angiogenesis, the formation of new blood vessels from pre-existing ones, and vasculogenesis, the formation of the circulatory system during embryogenesis .
Role in Immune Responses and Pathogen Recognition: VEGFRs are involved in immune responses by regulating the migration and function of immune cells, such as monocytes and macrophages .
Mechanisms with Other Molecules and Cells: VEGFRs interact with various molecules, including neuropilins (NRP-1/2) and heparan sulfate proteoglycans (HSPGs), forming multiprotein complexes . Upon binding to VEGF ligands, VEGFRs dimerize and undergo transphosphorylation, activating downstream signaling cascades .
Binding Partners and Downstream Signaling Cascades: VEGFR-2 is the primary signaling receptor, mediating endothelial cell responses through pathways such as the MAPK/ERK, PI3K/AKT, and PLCγ pathways .
Transcriptional Regulation: VEGFR expression is regulated by various transcription factors, including ETS family members . Hypoxia and inflammatory conditions can upregulate VEGFR expression .
Post-Translational Modifications: VEGFR activity is modulated by phosphorylation, ubiquitination, and proteolytic cleavage .
Biomedical Research: VEGFRs are extensively studied in cancer research due to their role in tumor angiogenesis .
Diagnostic Tools: VEGFR levels can serve as biomarkers for various diseases, including cancer and ocular diseases .
Therapeutic Strategies: Anti-VEGF therapies, such as bevacizumab, target VEGFR signaling to inhibit pathological angiogenesis in diseases like cancer and age-related macular degeneration .
Development: VEGFRs are critical for embryonic development, particularly in forming the vascular system .
Aging and Disease: Dysregulation of VEGFR signaling is associated with various diseases, including cancer, diabetic retinopathy, and rheumatoid arthritis .
VEGFRs are indispensable for vascular health and disease, making them a focal point in biomedical research and therapeutic development.