VEGF E (Orf Virus)

Vascular Endothelial Growth Factor-E Recombinant (Orf Virus)

Cat. No.

BT6861

Source

Escherichia Coli.

Synonyms

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Purity

Greater than 90.0% as determined 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.

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Description

A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa.

Product Specs

Introduction

A gene encoding a VEGF homologue, similar in sequence to VEGF-A, was recently discovered in the Orf virus (OV) genome (Lyttle et al., 1994). This viral homologue, termed VEGF-E, demonstrates significant amino acid sequence similarity to VEGF-A across different OV isolates and is considered a virulence factor potentially acquired from host genes. Notably, all eight cysteine residues crucial for the central cysteine knot motif, characteristic of the VEGF family, are conserved in VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of mammalian VEGF sequences reveals that VEGF-E, while distinct from previously identified VEGFs, shares the closest relationship with VEGF-A. Similar to VEGF-A, VEGF-E exhibits high-affinity binding to VEGF receptor-2 (KDR), leading to receptor autophosphorylation. However, unlike VEGF-A, VEGF-E does not bind to VEGF receptor-1 (Flt-1) or VEGF receptor-3 (FLT-4). These properties establish VEGF-E as a potent angiogenic factor with specific receptor binding characteristics.

Description

The DNA sequence encoding the mature form of ovVEGF-E, specifically isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020), was expressed in E. coli. This expression yielded a 132 amino acid fusion protein featuring an N-terminal His-tag and a thrombin cleavage site. The recombinant VEGF-E, initially produced as a monomer, underwent in vitro dimerization, resulting in a homodimer with an approximate mass of 35 kDa.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized to a powder form from a concentrated solution (1mg/ml) in phosphate-buffered saline (PBS).

Solubility

To reconstitute the lyophilized oVEGF-E Orf Virus, dissolve the powder in water or suitable buffer to a final concentration of at least 50 µg/ml. For long-term storage, adding 0.1% human or bovine serum albumin is recommended.

Stability

Lyophilized Vascular Endothelial Growth Factor-E Orf Virus remains stable at room temperature for up to 3 weeks; however, it is recommended to store the lyophilized product desiccated at a temperature below -18°C for extended periods. After reconstitution, VEGF E -OV should be stored at 4°C for 2-7 days. For long-term storage, freeze the reconstituted solution below -18°C. Avoid repeated freeze-thaw cycles.

Purity

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

Biological Activity

The biological activity of the protein is assessed through two methods: (1) its ability to induce the phosphorylation of VEGFR-2/KDR receptor in PAE/KDR cells and (2) its capacity to stimulate the proliferation of primary human umbilical vein endothelial cells (HUVECs). The effective concentration required to achieve 50% of the maximal response (ED₅₀) typically falls within the range of 1-5 ng/ml.

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH DSTKTWSEVF ENSGCKPRPM VFRVHDEHPE LTSQRFNPPC VTLMRCGGCC NDESLECVPT EEANVTMQLM GASVSGGNGM QHLSFVEHKK CDCKPPLTTT PPTTTRPPRR RR

Product Science Overview

Introduction

Vascular Endothelial Growth Factor-E (VEGF-E) is a unique member of the VEGF family, encoded by the Orf virus (OV), a parapoxvirus. VEGF-E is known for its potent angiogenic properties, which are crucial for the formation of new blood vessels. This article delves into the background, structure, and significance of VEGF-E, particularly in the context of its recombinant form.

Discovery and Structure

VEGF-E was first identified in the genome of the Orf virus, which infects sheep and goats, causing proliferative skin lesions. The gene encoding VEGF-E shows significant sequence similarity to VEGF-A, a well-known angiogenic factor in mammals. VEGF-E carries the characteristic cysteine knot motif present in all mammalian VEGFs, forming a distinct microheterogenic group within the VEGF family.

Mechanism of Action

VEGF-E functions by binding to VEGF receptor-2 (VEGFR-2 or KDR), but not to VEGF receptor-1 (VEGFR-1 or Flt-1). This selective binding triggers receptor autophosphorylation and a biphasic rise in intracellular calcium levels, leading to endothelial cell proliferation, chemotaxis, and angiogenesis. Unlike VEGF-A, VEGF-E does not bind to VEGFR-1, making it a potent and selective angiogenic factor.

Recombinant VEGF-E

Recombinant VEGF-E is produced by expressing the VEGF-E gene in mammalian cells or Escherichia coli. The recombinant protein is heat-stable and secreted as a dimer. It retains the angiogenic properties of the native protein, stimulating the release of tissue factor, endothelial cell proliferation, and vascular sprouting.

Role in Orf Virus Infection

During Orf virus infection, VEGF-E plays a critical role in the formation of proliferative skin lesions. The virus-encoded VEGF-E induces extensive capillary proliferation and dilation, contributing to the characteristic histological features of the infection. Disruption of the VEGF-E gene in recombinant Orf virus results in the loss of these angiogenic activities, highlighting its importance in the viral life cycle.

Applications and Significance

The unique properties of VEGF-E make it a valuable tool for studying angiogenesis and developing therapeutic strategies. Its selective binding to VEGFR-2 without affecting VEGFR-1 provides insights into receptor-specific signaling pathways. Additionally, recombinant VEGF-E has potential applications in promoting tissue regeneration and wound healing.

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VEGF E (Orf Virus)

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