FLT1 D5 Human

Vascular Endothelial Growth Factor Receptor-1 D5 Human Recombinant
Cat. No.
BT21186
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 D1-5 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.

Product Specs

Introduction
The vascular endothelial growth factor (VEGF) receptors are a family of receptor tyrosine kinases (RTKs) found primarily on endothelial cells. Among them, VEGFR-1 (Flt-1), identified in 1990, stands out. This receptor, with seven immunoglobulin-like extracellular domains, a single transmembrane region, and an intracellular split tyrosine kinase domain, exhibits a higher affinity for VEGF but weaker signaling activity compared to VEGFR-2. Consequently, instead of promoting endothelial cell proliferation, VEGFR-1 primarily regulates cell differentiation. Notably, a soluble variant, sVEGFR-1, generated by alternative splicing of the flt-1 mRNA, was discovered in 1996. Found in HUVE supernatants, sVEGFR-1's exact biological functions remain elusive, but it appears to be involved in angiogenesis regulation by binding VEGF with an affinity comparable to the full-length receptor.
Description
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.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile-filtered.
Formulation
The lyophilized FLT1 D1-5 is prepared from a sterile solution (1 mg/ml) without any additives.
Solubility
To reconstitute lyophilized FLT1 D5, sterile water is recommended, with a minimum concentration of 100 µg/ml. Further dilutions can be made using other aqueous solutions.
Stability
While lyophilized FLT-1 remains stable at room temperature for up to three weeks, it should be stored desiccated below -18°C. After reconstitution, FLT1 should be stored at 4°C for 2-7 days. For extended storage, freeze at -18°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 90.0%, as determined by: (a) RP-HPLC analysis, and (b) SDS-PAGE analysis.
Biological Activity
FLT1 D5 activity is determined by its capacity to inhibit iodinated VEGF binding to solid surfaces and cell surfaces. Typically, the ED50 for this effect is 10 ng/ml, which translates to a specific activity of 100,000 IU/mg. In a 13-day CAM assay, sVEGFR-1 can inhibit VEGF-stimulated capillary sprouting at a concentration of 30 pM.
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 Flt-1, is a receptor tyrosine kinase that plays a crucial role in angiogenesis and vasculogenesis. It is one of the receptors for Vascular Endothelial Growth Factor (VEGF), which is a signal protein that stimulates the formation of blood vessels. The D5 domain of VEGFR-1 is particularly significant as it is involved in the binding of VEGF.

Structure and Function

VEGFR-1 is composed of several domains, including seven immunoglobulin-like domains in its extracellular region, a single transmembrane helix, and an intracellular tyrosine kinase domain. The D5 domain is one of these extracellular immunoglobulin-like domains and is critical for the receptor’s ability to bind VEGF.

VEGFR-1 acts as a decoy receptor, sequestering VEGF and preventing it from binding to VEGFR-2, which is more directly involved in promoting angiogenesis. This regulatory mechanism is essential for maintaining the balance of angiogenic signals in the body.

Recombinant VEGFR-1 D5

Recombinant human VEGFR-1 D5 is produced using recombinant DNA technology, which involves cloning the gene encoding the D5 domain into an expression vector, introducing this vector into a host cell (such as E. coli or CHO cells), and then purifying the expressed protein. This recombinant protein can be used in various research and therapeutic applications.

Applications
  1. Research: Recombinant VEGFR-1 D5 is widely used in research to study the mechanisms of angiogenesis and to develop anti-angiogenic therapies. It can be used in binding assays to investigate the interaction between VEGF and its receptors.
  2. Therapeutics: Due to its ability to bind VEGF, recombinant VEGFR-1 D5 has potential therapeutic applications in diseases characterized by excessive angiogenesis, such as cancer and age-related macular degeneration. By sequestering VEGF, it can inhibit the growth of new blood vessels that supply nutrients to tumors or diseased tissues.
Production and Purification

The production of recombinant VEGFR-1 D5 typically involves the following steps:

  1. Cloning: The gene encoding the D5 domain is cloned into an expression vector.
  2. Expression: The vector is introduced into a host cell line, such as E. coli or CHO cells, which then express the recombinant protein.
  3. Purification: The expressed protein is purified using techniques such as affinity chromatography. For example, a hexahistidine tag can be added to the protein to facilitate purification using nickel affinity chromatography.

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