FLT4 Human

Vascular Endothelial Growth Factor Receptor-3 Human Recombinant

Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21777
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGFR2 Fc Human

Vascular Endothelial Growth Factor Receptor-2 Fc Chimera Human Recombinant

Soluble VEGFR2 Fc Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a disulfide-linked homodimeric, glycosylated, polypeptide containing 968 amino acids and having a molecular mass of 145 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.
The sKDR Fc Chimera is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21829
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGFR2 Human

Vascular Endothelial Growth Factor Receptor-2 Human Recombinant

Soluble VEGFR-2 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide having a molecular mass of 116 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.
The sKDR is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21886
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGFR2 Human, His

Vascular Endothelial Growth Factor receptor-2 Human Recombinant, His Tag

VEGFR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 987 amino acids (20-764a.a) and having a molecular mass of 110.5kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa). VEGFR2 is fused to a 239 amino acids hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21961
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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.

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