HBcAg (1-149)

Hepatitis B Virus Core (1-149 a.a) Recombinant
Cat. No.
BT9523
Source
Escherichia Coli.
Synonyms
Appearance
Sterile filtered colorless solution.
Purity

Greater than 90% 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.
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Description

HBcAg subtype adw2 produced in E.Coli, is a single, non-glycosylated, polypeptide chain containing 1-149 amino acids and having a molecular weight of approximately 20kDa. HBcAg adw2 1-149 protamine-like domain was truncated in order to enhance the differentiation of anti-HBe in ELISA test.
HBcAg is fused to a his tag and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Hepatitis B virus (HBV) is unusual in that it replicates its DNA genome via an RNA intermediate. This process, called reverse transcription, is a feature shared with retroviruses, such as HIV. Unlike retroviruses, the HBV genome does not integrate into the host cell's DNA. After binding to specific receptors on the hepatocyte surface, the virus enters the cell, and its core, containing the viral DNA, travels to the nucleus. The partially double-stranded DNA is then filled in to form a closed circular DNA molecule (cccDNA). The cccDNA serves as a template for the transcription of viral RNA, including pregenomic RNA (pgRNA). The pgRNA is packaged with viral polymerase into new viral core particles. Within these particles, reverse transcription of pgRNA occurs, generating new copies of the viral DNA. The new viral cores can either acquire an envelope and exit the cell to infect other hepatocytes or return to the nucleus, contributing to the persistence of HBV infection.
Description
The HBcAg subtype adw2, derived from E. coli, is a non-glycosylated polypeptide. This protein represents the truncated version of the HBcAg adw2 (amino acids 1-149) and has a molecular weight of approximately 20kDa. The truncation in the protamine-like domain of HBcAg adw2 1-149 is designed to enhance the differentiation of anti-HBe antibodies in ELISA. The protein is expressed with a His-tag for purification and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear and colorless solution that has been sterilized by filtration.
Formulation
The protein is supplied in a buffer consisting of phosphate-buffered saline (PBS) and 25mM potassium carbonate (K₂CO₃).
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. The addition of a carrier protein, such as HSA or BSA, at a concentration of 0.1% is advised for long-term storage. Repeated freeze-thaw cycles should be avoided to maintain product stability.
Purity
The purity of this protein is greater than 90% as determined by SDS-PAGE analysis.
Source
Escherichia Coli.
Amino Acid Sequence

MDIDPYKEFG ATVELLSFLP SDFFPSVRDL LDTASALYRE ALESPEHCSP HHTALRQAIL CWGELMTLAT WVGNNLEDPA SRDLVVNYVN TNVGLKIRQL LWFHISCLTF GRETVLEYLV SFGVWIRTPP AYRPPNAPIL

Product Science Overview

Introduction

The Hepatitis B Virus (HBV) is a significant global health concern, causing both acute and chronic liver infections. The core protein of HBV, also known as HBcAg (Hepatitis B core antigen), plays a crucial role in the virus’s life cycle. The recombinant form of the HBV core protein, specifically the 1-149 amino acid (a.a) segment, is widely studied for its structural and immunological properties.

Structure and Function

The full-length HBV core protein consists of 183 amino acids, but the 1-149 a.a segment is sufficient for capsid formation . This segment forms the assembly domain, which is essential for the creation of the viral capsid, a protective shell that encases the viral DNA. The remaining C-terminal region (150-183 a.a) is rich in arginine and is involved in nucleic acid binding .

Recombinant Expression

The recombinant HBV core protein (1-149 a.a) is typically expressed in Escherichia coli (E. coli) systems. This truncated version of the core protein can self-assemble into virus-like particles (VLPs) in vitro, making it a valuable tool for research and vaccine development . The ability to produce these particles recombinantly allows for large-scale production and purification, facilitating various studies on HBV structure and immunogenicity.

Immunological Significance

The HBV core antigen is highly immunogenic, meaning it can effectively stimulate an immune response. This property makes the recombinant HBV core protein (1-149 a.a) a potential candidate for vaccine development. It can be used to present foreign epitopes, enhancing the immunogenicity of other antigens when used as a vaccine platform .

Research Applications
  1. Structural Studies: The recombinant HBV core protein (1-149 a.a) is used to study the assembly and disassembly of the viral capsid. Understanding these processes is crucial for developing antiviral therapies that target capsid formation.
  2. Vaccine Development: Due to its immunogenic properties, the recombinant core protein is explored as a component of HBV vaccines and as a platform for presenting other viral antigens .
  3. Therapeutic Research: The core protein’s interactions with nucleic acids and its role in the viral life cycle make it a target for therapeutic interventions. Studies on phosphorylation and other post-translational modifications of the core protein provide insights into potential therapeutic targets .

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