VEGF Human

Vascular Endothelial Growth Factor Human Recombinant
Cat. No.
BT7088
Source
Escherichia Coli.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec'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.
Shipped with Ice Packs
In Stock

Description

Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.
The VEGF is purified by proprietary chromatographic techniques.

Product Specs

Introduction

Vascular endothelial growth factor (VEGF) is a key signaling molecule that plays a crucial role in the formation of new blood vessels. While its effects have been extensively studied on vascular endothelial cells, VEGF also influences various other cell types, including monocytes, macrophages, neurons, cancer cells, and kidney epithelial cells. VEGF contributes to increased vascular permeability, stimulates the formation of new blood vessels (vasculogenesis) and the production of endothelial cells, encourages cell migration, and hinders programmed cell death (apoptosis). In laboratory settings, VEGF has been observed to promote both the division and movement of endothelial cells. Additionally, VEGF acts as a vasodilator, widening blood vessels, and enhances the permeability of small blood vessels. It was initially known as vascular permeability factor. VEGF is present in healthy cartilage; however, only cartilage affected by osteoarthritis expresses the VEGF receptors NP1, VEGFR1, and VEGFR2. Notably, the concentration of VEGF in the culture medium of chondrocytes derived from osteoarthritic cartilage was found to be over three times higher compared to the medium from normal chondrocytes.

Description
Recombinant Human Vascular Endothelial Growth Factor, produced in E. coli, is a non-glycosylated polypeptide chain consisting of two identical chains. Each chain contains 165 amino acids, resulting in a total molecular mass of 38.2 kDa. The purification of VEGF is achieved through specialized chromatographic methods.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The VEGF protein was freeze-dried from a concentrated solution (1mg/ml) without any additional substances.
Solubility
To reconstitute the lyophilized VEGF, it is recommended to dissolve it in sterile 18M-cm H2O at a concentration of at least 100 µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized VEGF remains stable at room temperature for up to 3 weeks; however, for long-term storage, it should be kept desiccated at a temperature below -18°C. Once reconstituted, VEGF should be stored at 4°C for 2-7 days. For extended storage periods, it is advisable to store it below -18°C. To ensure optimal stability during long-term storage, it is recommended to add a carrier protein such as 0.1% HSA or BSA. It is important to avoid repeated freeze-thaw cycles.
Purity
The purity of VEGF is greater than 95.0% as determined by two methods: (a) Analysis by RP-HPLC and (b) Analysis by SDS-PAGE.
Biological Activity
The biological activity of VEGF is assessed by measuring its ability to stimulate the growth of human umbilical vein endothelial cells (HUVEC) in a dose-dependent manner. Using a concentration range of 3.7-5.6 ng/ml, the specific activity is determined to be 178,570-270,270 IU/mg.
Protein Content
The quantification of VEGF protein content is performed using two independent methods: 1. UV spectroscopy at 280 nm, employing an absorbance value of 0.2875 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is derived from the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, utilizing a calibrated VEGF solution as a reference standard.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Source
Escherichia Coli.
Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR

Product Science Overview

Introduction

Vascular Endothelial Growth Factor (VEGF) is a critical signaling protein involved in the formation of blood vessels, a process known as angiogenesis. It plays a pivotal role in both physiological and pathological conditions, including embryonic development, wound healing, and tumor growth . Human recombinant VEGF is a bioengineered form of this protein, produced using recombinant DNA technology to study its functions and therapeutic potential.

Structure and Isoforms

VEGF is a heparin-binding glycoprotein that typically exists as a homodimer. The human VEGF gene undergoes alternative splicing to produce several isoforms, including VEGF121, VEGF145, VEGF165, VEGF189, and VEGF206 . Among these, VEGF165 is the most studied and widely used in research and therapeutic applications .

Biological Functions

VEGF primarily acts on endothelial cells, promoting their proliferation, migration, and new blood vessel formation. It binds to specific receptors on the surface of these cells, namely VEGFR-1 and VEGFR-2, triggering a cascade of signaling pathways essential for angiogenesis . VEGF also increases vascular permeability, which is crucial in both normal and pathological conditions.

Production of Human Recombinant VEGF

The production of human recombinant VEGF involves cloning the VEGF gene into an expression vector, which is then introduced into a host cell, commonly Escherichia coli (E. coli). The host cells are cultured, and the recombinant protein is expressed, extracted, and purified using techniques such as nickel affinity chromatography . This process ensures a high yield of biologically active VEGF, which can be used for various research and therapeutic purposes.

Therapeutic Applications

Recombinant VEGF has shown promise in treating conditions that require enhanced angiogenesis, such as ischemic heart disease and peripheral artery disease . It is also being explored in cancer therapy, where inhibiting VEGF can reduce tumor vascularization and growth . However, the therapeutic use of VEGF must be carefully controlled due to its potent effects on blood vessel formation and permeability.

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