TBEV gE C-end

Tick-Borne Encephalitis Virus gE C-end Recombinant
Cat. No.
BT7099
Source
Escherichia Coli.
Synonyms
Appearance
Purity
Encephalitis protein is >95% pure as determined by 10% PAGE (coomassie staining).
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

The E.coli derived recombinant protein contains the Tick-borne Encephalitis Virus C-end regions of glycoprotein E, 296-414 amino acids.

Product Specs

Introduction
Tick-borne encephalitis (TBE) is caused by the tick-borne encephalitis virus (TBEV), a member of the Flaviviridae family. A closely related virus found in Far Eastern Eurasia is the Russian spring-summer encephalitis virus (RSSEV). The Flaviviridae family includes other tick-borne viruses closely related to TBEV and RSSEV, such as the Omsk hemorrhagic fever virus and Kyasanur Forest virus. Louping ill virus is also a member of this family.
Description
This recombinant protein is derived from E. coli and contains the C-terminal region of the Tick-borne Encephalitis Virus glycoprotein E, specifically amino acids 296-414.
Purity
The purity of the Encephalitis protein is greater than 95%, as determined by 10% PAGE (Coomassie staining).
Formulation
The protein is supplied in a solution of 20mM MES (pH 6.5), 8M urea, 200mM NaCl, and 0.05% Tween-20.
Stability
While the Encephalitis protein remains stable at 4°C for up to 1 week, it is recommended to store it below -18°C. Avoid repeated freeze-thaw cycles.
Applications
The Encephalitis antigen is suitable for use in ELISA and Western blots. It serves as an excellent antigen for the detection of Tick-borne encephalitis virus with minimal specificity issues.
Source
Escherichia Coli.
Purification Method
Encephalitis protein was purified by proprietary chromatographic technique.
Specificity
Immunoreactive with sera of encephalitis virus infected individuals.

Product Science Overview

Introduction

Tick-Borne Encephalitis Virus (TBEV) is a positive-sense, single-stranded RNA virus belonging to the family Flaviviridae and the genus Flavivirus . It is considered one of the most medically significant arthropod-borne viruses in Europe, causing a range of symptoms from subclinical to severe encephalitis . The virus is primarily transmitted through tick bites and, less commonly, through the consumption of unpasteurized dairy products from infected animals .

Structure and Function of the Envelope (E) Protein

The envelope (E) protein of TBEV plays a crucial role in the virus’s ability to infect host cells. It is located on the surface of the viral particle and is responsible for mediating the fusion of the viral membrane with the host cell membrane . The E protein is also the major target for neutralizing antibodies, making it a key component in vaccine development .

Recombinant gE C-end

The gE C-end refers to the C-terminal end of the E protein. Recombinant versions of this protein segment have been developed to study its role in the virus’s pathogenicity and to explore its potential in vaccine formulations . Recombinant proteins are produced by inserting the gene encoding the protein into a host cell, such as E. coli, which then expresses the protein. This allows for the production of large quantities of the protein for research and vaccine development .

Research and Applications

Research has shown that the E protein, including its C-terminal end, is a significant determinant of the virus’s ability to infect neurons and cause disease . For instance, specific amino acid substitutions in the E protein have been linked to increased neurovirulence and pathogenicity . These findings are crucial for understanding the mechanisms of TBEV infection and for developing effective vaccines.

Recombinant versions of the E protein, including the gE C-end, have been used in various studies to evaluate their immunogenicity and protective efficacy . For example, recombinant domains of the E protein have been shown to induce immune responses and provide partial protection against TBEV infection in animal models . These studies highlight the potential of recombinant E protein segments in the development of subunit vaccines and diagnostic tools.

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