FLT1 D4 Human

Vascular Endothelial Growth Factor Receptor-1 D4 Human Recombinant
Cat. No.
BT21022
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(a)Analysis by RP-HPLC.
(b)Analysis 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

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.

Product Specs

Introduction
Endothelial cells rely on three distinct vascular endothelial growth factor (VEGF) receptors, all of which belong to the receptor tyrosine kinases (RTKs) family. These receptors are identified as VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their presence is primarily observed in endothelial cells, although VEGFR-1 is also found in monocytes, dendritic cells, and trophoblast cells. The discovery of the flt-1 gene dates back to 1990. Structurally, the receptor consists of seven immunoglobulin-like domains in its extracellular region, a single transmembrane region, and an intracellular split tyrosine kinase domain. When compared to VEGFR-2, the Flt-1 receptor exhibits a stronger affinity for VEGF but demonstrates weaker signaling activity. As a result, VEGFR-1 does not induce endothelial cell proliferation but instead transmits signals that govern differentiation. Notably, in 1996, a soluble variant of VEGFR-1 (sVEGFR-1) was identified in HUVE supernatants. This variant arises from alternative splicing of the flt-1 mRNA. The precise biological functions of sVEGFR-1 remain to be fully elucidated; however, it appears to act as an endogenous regulator of angiogenesis, exhibiting a binding affinity for VEGF that is comparable to that of the full-length receptor.
Description
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.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
FLT1 D1-4 was lyophilized from a sterile solution at a concentration of 1 mg/ml, without the addition of any other substances.
Solubility
To reconstitute the lyophilized FLT1 D4, it is recommended to dissolve it in sterile water at a concentration of at least 100 µg/ml. This solution can then be further diluted into other aqueous solutions as required.
Stability
Lyophilized FLT-1 demonstrates stability at room temperature for a duration of 3 weeks. However, for optimal storage, it should be kept desiccated at a temperature below -18°C. Upon reconstitution, FLT1 should be stored at 4°C for a period of 2-7 days. For extended storage, it is advisable to store it below -18°C. To ensure long-term stability during storage, it is recommended to add a carrier protein such as 0.1% HSA or BSA. Avoid repeated freeze-thaw cycles.
Purity
Purity levels exceed 90.0% as determined through the following methods: (a) Analysis by RP-HPLC and (b) Analysis by SDS-PAGE.
Biological Activity
The biological activity of FLT1D1-4 is assessed based on its ability to inhibit the binding of iodinated VEGF to both solid surfaces and cell surfaces. This activity has been confirmed through Far-Western and cross-linking experiments using iodinated VEGF.
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.

Product Science Overview

Introduction

Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Fms-like tyrosine kinase-1 (FLT-1), is a receptor tyrosine kinase that plays a crucial role in angiogenesis, the process of forming new blood vessels from pre-existing ones. This receptor is part of the VEGF family, which includes several proteins such as VEGF-A, VEGF-B, VEGF-C, VEGF-D, and placental growth factor (PlGF). VEGFR-1 is primarily involved in the regulation of vascular development and permeability.

Structure and Function

VEGFR-1 consists of an extracellular domain, a transmembrane domain, and an intracellular tyrosine kinase domain. The extracellular domain is responsible for binding to its ligands, VEGF-A, VEGF-B, and PlGF. The binding of these ligands to VEGFR-1 triggers a cascade of intracellular signaling pathways that regulate various cellular processes, including cell migration, survival, and proliferation.

VEGFR-1 is known for its high affinity for VEGF-A, which is a key mediator of angiogenesis. Interestingly, VEGFR-1 can act as a “decoy” receptor by sequestering VEGF-A and preventing it from binding to VEGFR-2, another receptor that mediates angiogenic signaling. This decoy function helps to fine-tune the angiogenic response and maintain vascular homeostasis .

Recombinant VEGFR-1 D4

Recombinant VEGFR-1 D4 refers to a specific domain of the VEGFR-1 protein that has been produced using recombinant DNA technology. This domain includes the extracellular region of the receptor, which is crucial for ligand binding. The recombinant form is often used in research to study the interactions between VEGFR-1 and its ligands, as well as to develop therapeutic agents that target angiogenesis-related diseases.

The production of recombinant VEGFR-1 D4 typically involves cloning the gene encoding the extracellular domain into an expression vector, which is then introduced into a host cell line such as HEK293 cells. The host cells express the recombinant protein, which can be purified using techniques like affinity chromatography .

Applications in Research and Medicine

Recombinant VEGFR-1 D4 is widely used in various research applications, including:

  1. Binding Studies: Investigating the interactions between VEGFR-1 and its ligands, such as VEGF-A and PlGF.
  2. Inhibitor Screening: Identifying and characterizing potential inhibitors of VEGFR-1 signaling, which could be used as therapeutic agents for diseases like cancer and age-related macular degeneration.
  3. Functional Assays: Assessing the biological activity of VEGFR-1 in processes like cell migration, proliferation, and angiogenesis.
Therapeutic Implications

VEGFR-1 is a promising target for anti-angiogenic therapies, which aim to inhibit the formation of new blood vessels in diseases characterized by excessive angiogenesis, such as cancer and diabetic retinopathy. By blocking VEGFR-1 signaling, it is possible to reduce tumor growth and metastasis, as well as to alleviate symptoms of other angiogenesis-related conditions .

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