Product List

FLT1 D3 Human

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.

Shipped with Ice Packs
Cat. No.
BT20864
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FLT1 D3 Human, His

Vascular Endothelial Growth Factor Receptor-1 D3 Human Recombinant, His Tag

FLT1 D1-3 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 298 amino acids fragment (31-328) and having a molecular mass of 38.16kDa. The 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.
Shipped with Ice Packs
Cat. No.
BT20949
Source
Insect Cells.
Appearance
Sterile Filtered clear solution.

FLT1 D4 Human

Vascular Endothelial Growth Factor Receptor-1 D4 Human Recombinant

Soluble FLT1 D1-4 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 457 amino acids and having a molecular mass of 55 kDa. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF.
The VEGFR1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21022
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FLT1 D5 Human

Vascular Endothelial Growth Factor Receptor-1 D5 Human Recombinant

Soluble FLT1 D1-5 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 562 amino acids and having a molecular mass of 70 kDa. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for binding of VEGF.
The FLT1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21186
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FLT1 D7 Human

Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant

Soluble FLT1 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric, glycosylated, polypeptide containing 751 amino acids and having a molecular mass of 130 kDa. The soluble receptor protein contains only the first 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. The FLT1 fc/Chimera is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21255
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FLT1 D7 Mouse

Vascular Endothelial Growth Factor Receptor-1 D1-7 Mouse Recombinant

Soluble FLT1 Mouse Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric , polypeptide containing 965 amino acids. The monomers have a molecular mass of 130 kDa. The soluble receptor protein contains all 7 extracellular domains (Tyr23-Asn757), which contain all the information necessary for high affinity ligand binding.
Shipped with Ice Packs
Cat. No.
BT21321
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FLT1 Human

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.

Shipped with Ice Packs
Cat. No.
BT21403
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FLT1 Human, HEK Active

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.

Shipped with Ice Packs
Cat. No.
BT21489
Source
HEK293
Appearance

Filtered clear solution.

FLT1 Human, His

Vascular Endothelial Growth Factor receptor-1 Human Recombinant, His Tag

FLT1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 298 amino acids fragment (31-328) corresponding to the IgG like domains 1-3 from the mature soluble FLT1 protein, having a total molecular mass of 43kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The FLT1 His is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21588
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

FLT4 Fc Human

Vascular Endothelial Growth Factor Receptor-3 Fc Chimera Human Recombinant

Soluble FLT4 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a monomeric, glycosylated, polypeptide containing 774 amino acids and having a molecular mass of 260 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.
The FLT4 Fc Chimera is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21672
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Introduction

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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