HSV-2 VP13/14

Herpes Simplex Virus-2 VP13/14 Recombinant
Cat. No.
BT19059
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered clear solution.
Purity
Protein is >90% pure 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

The E.Coli derived HSV-2 VP13/14 recombinant protein, 1-280 amino acids, is fused to a Six histidine tag at C-terminus and has a MW of 31kDa (pI 6.77). 

Product Specs

Introduction
Herpes simplex virus (HSV) enters host cells through a multi-step process involving interactions between viral glycoproteins and cell surface receptors. The virus's outer envelope, studded with these glycoproteins, binds to specific receptors on the host cell surface. This binding triggers a fusion event between the viral envelope and the cell membrane, creating a pore. This pore serves as an entry point for the viral contents to enter the host cell. HSV entry mirrors the entry mechanisms observed in other viruses. Initially, complementary receptors on the virus and the host cell surface draw the two membranes close together. This proximity leads to an intermediate stage where the membranes begin to merge, forming a hemifusion state. Finally, a stable pore is established, facilitating the transfer of the viral envelope contents into the host cell.
Description
This product consists of the Herpes Simplex Virus type 2 (HSV-2) VP13/14 protein, specifically amino acids 1 to 280. It's recombinantly produced in E. coli and includes a C-terminal six-histidine tag for purification. The protein has a molecular weight of 31 kDa and an isoelectric point of 6.77.
Purity
SDS PAGE analysis confirms that the protein purity is greater than 90%.
Physical Appearance
The product is a clear solution that has been sterilized by filtration.
Formulation
The protein is supplied in a buffer of 10 mM Phosphate at pH 7.6 with 75 mM NaCl.
Stability
For short-term storage, HSV-2 VP13/14 remains stable at 4°C for up to 1 week. However, for long-term storage, it is recommended to store the protein below -18°C. Repeated freeze-thaw cycles should be avoided to maintain protein integrity.
Applications
This product is suitable for use in various research applications, including Enzyme-Linked Immunosorbent Assay (ELISA), Western Blot (WB), and Flow-Through experiments.
Source
Escherichia Coli.

Product Science Overview

Introduction

Herpes Simplex Virus-2 (HSV-2) is a member of the Herpesviridae family, primarily known for causing genital herpes. The virus has a complex structure, consisting of an envelope, tegument, capsid, and core. Among the various proteins encoded by HSV-2, the tegument proteins play a crucial role in the virus’s life cycle. One such tegument protein is VP13/14, encoded by the UL47 gene.

Structure and Function

VP13/14 is a major structural component of the virion tegument, the compartment located between the capsid and the virus envelope . The protein has apparent masses of 82 and 81 kDa, respectively, and is posttranslationally modified by phosphorylation, nucleotidylylation, and glycosylation . These modifications are believed to contribute to the protein’s functional diversity.

Nuclear Localization and Shuttling

VP13/14 is capable of nuclear shuttling, a property that is attributed to its nuclear localization signals (NLS) and nuclear export signals (NES) . The NLS of VP13/14 contains two runs of four arginine residues, similar to the arginine-rich NLS of retrovirus transactivator proteins like Tat, Rev, and Rex . Additionally, VP13/14 has three leucine-rich stretches in its C-terminal half, which resemble the NES of Rev and Rex . This nuclear shuttling capability is significant during virus entry and later stages of infection when large amounts of newly synthesized VP13/14 are present within the cell .

Immunological Significance

VP13/14 is also a major target antigen for T cells obtained from vitreous fluid samples of patients with HSV-induced acute retinal necrosis (ARN) . The protein contains specific epitopes recognized by CD4+ T cells, indicating its role in the local inflammatory response during HSV infection . This immunological significance makes VP13/14 a potential target for therapeutic interventions.

Recombinant VP13/14

Recombinant VP13/14 proteins are produced using various expression systems to study their structure, function, and immunogenicity. These recombinant proteins are valuable tools for understanding the molecular mechanisms of HSV-2 infection and developing potential vaccines and antiviral therapies.

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