HAV P2C

Hepatitis A Virus P2C Recombinant
Cat. No.
BT8287
Source
Synonyms
Appearance
Purity
Protein is >90% 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 38.5 kDa protein contains the P2C immunodominant regions, amino acids 1121-1234.

Product Specs

Introduction
Hepatitis A virus (HAV) possesses numerous antigenic domains within its polyprotein structure. Research utilizing 237 overlapping synthetic peptides revealed 42 distinct antigenic domains. Of these, 19 were located within the structural proteins and 22 within the nonstructural proteins, with one domain spanning the VP1 and P2A protein junction. Five domains exhibited significant immunodominance due to their broad and strong immunoreactivity. One domain resides within the VP2 protein (amino acids 57-90). A second domain (amino acids 767-842) encompasses the C-terminal region of VP1 and the complete P2A protein. The third domain (amino acids 1403-1456) includes the C-terminal portion of the P2C protein and the N-terminal half of P3A. The fourth domain (amino acids 1500-1519) spans nearly the entire P3B protein, and the fifth domain (amino acids 1719-1764) comprises the C-terminal region of P3C and the N-terminal region of P3D. Notably, four of these highly immunoreactive domains originate from smaller HAV proteins or encompass cleavage sites between HAV proteins.
Description
This recombinant protein, derived from E. coli, has a molecular weight of 38.5 kDa and contains the immunodominant regions of the HAV P2C protein, specifically amino acids 1121-1234.
Purity
Greater than 90% purity as determined by 10% SDS-PAGE and Coomassie blue staining.
Formulation
Supplied in a solution of 10mM CBB (Coomassie Brilliant Blue), pH 9.6, 0.1% SDS (sodium dodecyl sulfate), and 50% glycerol.
Stability

For optimal stability, HAV P2C protein should be stored at -18°C. While it can remain stable at 4°C for up to one week, long-term storage at this temperature is not recommended.
Repeated freezing and thawing of the protein should be avoided.

Applications
HAV P2C antigen is well-suited for use in ELISA and Western blotting procedures. It is a highly effective antigen for the detection of HAV with minimal cross-reactivity.
Purification Method
HAV P2C protein was purified by proprietary chromatographic technique.
Specificity
Immunoreactive with sera HAV-infected individuals.

Product Science Overview

Introduction

Hepatitis A virus (HAV) is a significant pathogen causing communicable liver disease worldwide. It belongs to the family Picornaviridae and is the sole member of the Hepatovirus genus . HAV infection is generally mild, but in some cases, particularly in older adults, it can lead to severe liver disease, including fulminant hepatitis .

Hepatitis A Virus Structure and Genome

HAV is a non-enveloped virus with an icosahedral capsid approximately 27 nm in diameter . The virus has a single-stranded RNA genome of about 7.5 kb, which encodes a single polyprotein that is processed into structural and nonstructural proteins . The nonstructural proteins are essential for viral replication and include the 2C protein, which is the focus of this article.

The 2C Protein

The 2C protein of HAV is a nonstructural protein that plays a crucial role in viral replication . It shares 24-27% sequence identity with 2C proteins of other picornaviruses, and key motifs are conserved . The 2C protein has been shown to possess ATPase activity but lacks helicase activity . Additionally, it exhibits an ATPase-independent ribonuclease activity with a preference for polyuridylic single-stranded RNAs .

Recombinant HAV 2C Protein

Recombinant HAV 2C protein has been studied to understand its biochemical and structural properties. The crystal structure of an HAV 2C fragment has been determined to a resolution of 2.2 Å, revealing an ATPase domain, a region equivalent to the enterovirus 2C zinc-finger (ZFER), and a C-terminal amphipathic helix (PBD) . The PBD of HAV 2C occupies a hydrophobic pocket in the adjacent 2C, and this interaction is vital for 2C functions .

Biological Functions and Mechanisms

The ribonuclease activity of HAV 2C is essential for virus replication. Mutations in acidic residues that are crucial for this activity abrogate virus replication . The ribonuclease activity is shared by other picornavirus 2Cs, providing novel insights into the mechanisms of virus replication .

Applications and Future Directions

Recombinant HAV genomes containing foreign protein-coding sequences inserted at the 2A/2B junction are novel and potentially useful protein expression vectors . These recombinant genomes can tolerate insertions and have been used to study the functions of various viral proteins . Understanding the biochemical and structural properties of HAV 2C can aid in the development of effective anti-HAV drugs and improve disease control measures .

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