FLT1 D3 Human

Vascular Endothelial Growth Factor Receptor-1 D3 Human Recombinant

Recombinant Human FLT1 D1-3, produced in baculovirus, is a monomeric, glycosylated polypeptide with 327 amino acids and a molecular mass of 45 kDa. This soluble receptor protein only encompasses the first three extracellular domains, which are sufficient for VEGF binding. FLT1 is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20864
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.

FLT1 D3 Human, His

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

Recombinant Human FLT1 D1-3, produced in baculovirus, is a monomeric, glycosylated polypeptide encompassing amino acids 31-328. This fragment, with a molecular weight of 38.16 kDa, consists of the first three extracellular domains of the FLT1 receptor, which are sufficient for VEGF binding. The purification of FLT1 is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20949
Source
Insect Cells.
Appearance
A clear solution that has undergone sterile filtration.

FLT1 D4 Human

Vascular Endothelial Growth Factor Receptor-1 D4 Human Recombinant

Produced in baculovirus, Recombinant Human Soluble FLT1 D1-4 is a monomeric, glycosylated polypeptide. It comprises 457 amino acids and possesses a molecular mass of 55 kDa. This soluble receptor protein encompasses only the initial four extracellular domains, which are sufficient for VEGF binding. The purification of VEGFR1 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21022
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.

FLT1 D5 Human

Vascular Endothelial Growth Factor Receptor-1 D5 Human Recombinant

Produced in baculovirus, Recombinant Human Soluble FLT1 D1-5 is a monomeric, glycosylated polypeptide. This 562-amino acid protein weighs approximately 70 kDa and comprises the first five extracellular domains of FLT1, sufficient for VEGF binding. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21186
Source
Insect Cells.
Appearance
White, lyophilized (freeze-dried) powder, sterile-filtered.

FLT1 D7 Human

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

Recombinant human soluble FLT1, fused with the Fc region of human IgG1, is produced in a baculovirus expression system. This disulfide-linked homodimeric glycoprotein consists of 751 amino acids, boasting a molecular weight of 130 kDa. The soluble receptor encompasses only the first seven extracellular domains (Met1-Thr751), which are sufficient for high-affinity ligand binding. The purification process of FLT1 Fc/Chimera involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21255
Source
Insect Cells.
Appearance
White, lyophilized powder, sterile-filtered.

FLT1 D7 Mouse

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

This product consists of the extracellular domain of mouse VEGFR-1 (soluble FLT1), fused to the Fc region of human IgG1. It is produced in baculovirus as a disulfide-linked homodimer. Each monomer has a molecular weight of 130 kDa, comprising amino acids Tyr23-Asn757, encompassing all seven extracellular domains responsible for high-affinity VEGF binding.
Shipped with Ice Packs
Cat. No.
BT21321
Source
Insect Cells.
Appearance
White powder, sterile-filtered and lyophilized.

FLT1 Human

Vascular Endothelial Growth Factor Receptor-1 Human Recombinant

Recombinant human soluble FLT1, produced in a baculovirus expression system, is a monomeric, glycosylated polypeptide. It consists of 687 amino acids and has a molecular weight of 96 kDa. This soluble receptor protein encompasses the first six extracellular domains, which are sufficient for VEGF binding. FLT1 is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21403
Source
Insect Cells.
Appearance
White lyophilized (freeze-dried) powder, sterile-filtered.

FLT1 Human, HEK Active

Vascular Endothelial Growth Factor receptor-1 Human Recombinant, HEK Active

Recombinant human FLT1 is a glycosylated polypeptide chain consisting of 535 amino acids (residues 27-328a.a) with a molecular weight of 60.3kDa (calculated). It is fused to a 233 amino acid hIgG-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21489
Source
HEK293
Appearance
Clear, filtered solution.

FLT1 Human, His

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

Recombinant FLT1 Human, His-tagged protein, expressed in E. coli, consists of amino acids 31-328, representing the IgG-like domains 1-3 of the mature soluble FLT1 protein. This non-glycosylated polypeptide chain, with a molecular weight of 43kDa, includes a 4.5kDa N-terminal hexahistidine tag and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21588
Source
Escherichia Coli.
Appearance
Clear and sterile solution.

FLT4 Fc Human

Vascular Endothelial Growth Factor Receptor-3 Fc Chimera Human Recombinant

Soluble FLT4 Human Recombinant, fused with the Fc region of human IgG1 and produced in a baculovirus expression system, is a monomeric, glycosylated polypeptide. This protein comprises 774 amino acids and has a molecular weight of 260 kDa. The soluble receptor encompasses only the first seven extracellular domains, which are sufficient for ligand binding. Purification of the FLT4 Fc Chimera is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21672
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.
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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