VEGF Rat, Yeast

Vascular Endothelial Growth Factor Rat Recombinant, Yeast
Cat. No.
BT8548
Source

Saccharomyces cerevisiae

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 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.
Shipped with Ice Packs
In Stock

Description

Vascular Endothelial Growth Factor Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 25.7kDa each.
VEGF is purified by proprietary chromatographic techniques.

Product Specs

Introduction

Vascular endothelial growth factor (VEGF) is a crucial signaling protein for angiogenesis and vasculogenesis. While its effects are primarily observed in vascular endothelial cells, VEGF also influences other cell types, including monocytes/macrophages, neurons, cancer cells, and kidney epithelial cells. Its roles encompass enhancing vascular permeability, stimulating angiogenesis and vasculogenesis, promoting endothelial cell growth and migration, and inhibiting apoptosis. In vitro studies have demonstrated VEGF's ability to induce endothelial cell mitogenesis and migration. Additionally, VEGF acts as a vasodilator, augmenting microvascular permeability, and was initially termed 'vascular permeability factor.' Elevated VEGF levels are associated with POEMS syndrome, also known as Crow-Fukase syndrome. Furthermore, mutations in VEGF have been linked to both proliferative and nonproliferative diabetic retinopathy.

Description

Recombinant Rat Vascular Endothelial Growth Factor, produced in yeast, is a homodimeric protein linked by disulfide bonds. It comprises two polypeptide chains, each containing 165 amino acids, resulting in a molecular mass of approximately 25.7 kDa per chain. The purification process of VEGF involves proprietary chromatographic techniques.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The product is lyophilized from a 0.2 µm filtered solution concentrated in PBS at pH 7.4.

Solubility

For reconstitution, it is advised to dissolve the lyophilized Vascular Endothelial Growth Factor in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. Further dilutions can be prepared in other aqueous solutions.

Stability

Lyophilized VEGF remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. After reconstitution, Vascular Endothelial Growth Factor should be kept at 4°C for a period of 2-7 days. For extended storage, it should be kept below -18°C. It is crucial to avoid repeated freeze-thaw cycles.

Purity

The purity of the product is determined to be greater than 90.0% using SDS-PAGE analysis.

Biological Activity

The ED50 was determined using a cell proliferation assay with HUVEC (human umbilical vein endothelial cells) and was found to be in the range of 0.75-3.75 ng/ml.

Synonyms

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Source

Saccharomyces cerevisiae

Amino Acid Sequence

MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

Product Science Overview

Introduction

Vascular Endothelial Growth Factor (VEGF) is a critical signaling protein involved in both angiogenesis (the formation of new blood vessels from pre-existing ones) and vasculogenesis (the formation of entirely new blood vessels during embryonic development). VEGF plays a pivotal role in the growth and maintenance of the vascular system, making it a key focus in both physiological and pathological studies.

Historical Background

VEGF was first identified in the 1980s as a factor that increased vascular permeability and was initially termed Vascular Permeability Factor (VPF). Subsequent research revealed its broader role in endothelial cell mitogenesis and angiogenesis, leading to its renaming as VEGF .

Structure and Isoforms

VEGF is a glycosylated mitogen that specifically acts on endothelial cells. It exists in several isoforms, which are produced through alternative splicing of mRNA. These isoforms have different properties and roles in angiogenesis and vasculogenesis .

Rat Recombinant VEGF Produced in Yeast

The rat recombinant VEGF produced in yeast is a disulfide-linked homodimer consisting of two 165 amino acid polypeptide chains, with a molecular mass of approximately 25.7 kDa each. This recombinant protein is produced in the yeast Saccharomyces cerevisiae and is purified using proprietary chromatographic techniques .

Biological Activity

VEGF mediates several critical processes:

  • Increased Vascular Permeability: VEGF increases the permeability of blood vessels, allowing for the exchange of nutrients and waste products.
  • Angiogenesis and Vasculogenesis: VEGF induces the formation of new blood vessels and the growth of existing ones.
  • Endothelial Cell Growth: VEGF promotes the proliferation and migration of endothelial cells.
  • Inhibition of Apoptosis: VEGF helps in the survival of endothelial cells by inhibiting programmed cell death .
Clinical Significance

VEGF is implicated in various physiological and pathological conditions:

  • Physiological Angiogenesis: VEGF is essential for embryonic development, skeletal growth, and reproductive functions.
  • Pathological Angiogenesis: Elevated levels of VEGF are associated with diseases such as cancer, diabetic retinopathy, and age-related macular degeneration. Anti-VEGF therapies, such as monoclonal antibodies (e.g., bevacizumab), are used to treat these conditions by inhibiting abnormal blood vessel growth .
Applications in Research

Recombinant VEGF proteins, such as the rat VEGF produced in yeast, are widely used in laboratory research to study angiogenesis, endothelial cell behavior, and the development of anti-angiogenic therapies. These proteins are valuable tools for understanding the mechanisms underlying vascular growth and for developing new therapeutic strategies .

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