FLT1 D3 Human

Vascular Endothelial Growth Factor Receptor-1 D3 Human Recombinant
Cat. No.
BT20864
Source
Insect Cells.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

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.

Product Specs

Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, which belong to the receptor tyrosine kinase (RTK) family. These receptors are VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is mostly limited to endothelial cells, except for VEGFR-1, which is also found on monocytes, dendritic cells, and trophoblast cells. The flt-1 gene was first identified in 1990. The receptor has seven immunoglobulin-like extracellular domains, a single transmembrane region, and an intracellular split tyrosine kinase domain. In comparison to VEGFR-2, the Flt-1 receptor exhibits a stronger affinity for VEGF but weaker signaling activity. As a result, VEGFR-1 does not stimulate endothelial cell proliferation but rather transmits differentiation signals. Interestingly, a soluble variant of VEGFR-1 (sVEGFR-1) was discovered in HUVE supernatants in 1996, produced by alternative splicing of the flt-1 mRNA. While the exact functions of sVEGFR-1 are unclear, it appears to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Description
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.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
FLT1 D1-3 was lyophilized from a sterile solution at a concentration of 1 mg/mL in 1xPBS.
Solubility
It is recommended to reconstitute the lyophilized FLT1 D3 in sterile water to a concentration of at least 100 µg/mL. This solution can be further diluted into other aqueous solutions.
Stability
Lyophilized FLT-1 remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. After reconstitution, store FLT1 at 4°C for 2-7 days. For long-term storage, keep it below -18°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The activity of FLT1D1-3 was assessed by its ability to inhibit VEGF-165-induced proliferation of HUVE cells.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Source
Insect Cells.
Amino Acid Sequence

SKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSI TKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYI FISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDT LIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQT NTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRA SVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSV HIYDKAFITVKHRKQQVLETVAGKRSY.

Product Science Overview

Introduction

Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Fms-like tyrosine kinase 1 (FLT1), is a receptor tyrosine kinase that plays a crucial role in the regulation of angiogenesis, the process by which new blood vessels form from pre-existing vessels. This receptor is part of the VEGFR family, which includes VEGFR-1, VEGFR-2, and VEGFR-3, each with distinct roles in vascular development and function .

Structure and Function

VEGFR-1 is characterized by its seven immunoglobulin (Ig)-like domains, a single transmembrane domain, and an intracellular tyrosine kinase domain. The receptor binds to various ligands, including VEGFA, VEGFB, and placental growth factor (PlGF), mediating a range of biological processes such as endothelial cell proliferation, migration, and survival .

Historical Background

The discovery of VEGFR-1 dates back to the early 1990s when it was identified as a functional receptor for VEGFA. Subsequent research revealed its high affinity for VEGFA, suggesting its role as a decoy receptor that modulates VEGFA signaling by sequestering the ligand and preventing its interaction with VEGFR-2 . This regulatory mechanism is essential for maintaining the balance of angiogenic signals in various physiological and pathological conditions.

Recombinant VEGFR-1 D3

The recombinant form of VEGFR-1 D3 (Human) is a truncated version of the receptor, encompassing specific extracellular domains responsible for ligand binding. This recombinant protein is produced using advanced expression systems, such as HEK293 cells, to ensure high purity and functionality . The recombinant VEGFR-1 D3 is widely used in research to study its interactions with VEGF ligands and to develop therapeutic strategies targeting angiogenesis-related diseases.

Applications in Research and Medicine

VEGFR-1 D3 (Human Recombinant) is a valuable tool in both basic and applied research. It is used in binding studies to investigate the interactions between VEGFR-1 and its ligands, providing insights into the molecular mechanisms underlying angiogenesis . Additionally, this recombinant protein is employed in the development of anti-angiogenic therapies for conditions such as cancer and age-related macular degeneration, where pathological angiogenesis plays a critical role .

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