Products

Hepatitis E virus cDNA and Antigen

Cat#

Product Name

Swiss Prot#

Size

Price (US$)

Order

PN0557

Recombinant Protein-Hepatitis E virus Capsid protein (a.a.19 to 400)

Q80IR7

100 µg

1195

Order

PN0558

Recombinant Protein-Hepatitis E virus X domain (a.a.22 to 158)

Q81867

100 µg

1195

Order

PN0559

Recombinant Protein-Hepatitis E virus Structural protein 2 (a.a.50 to 344)

Q9WJZ5

100 µg

1195

Order

PN0560

Recombinant Protein-Hepatitis E virus genotype 1 Capsid protein (a.a.21 to 420)

P29326

100 µg

1195

Order

PN0561

Recombinant Protein-Hepatitis E virus genotype 1 Protein ORF3 (pORF3) (a.a.17 to 114)

O90299

100 µg

1195

Order

PN0562

Recombinant Protein-Hepatitis E virus genotype 3 Capsid protein (a.a.24 to 660)

Q9YLQ9

100 µg

1195

Order

RPN0557

cDNA-Hepatitis E virus Capsid protein (a.a.19 to 400)

Q80IR7

2 µg

1905

Order

RPN0558

cDNA-Hepatitis E virus X domain (a.a.22 to 158)

Q81867

2 µg

800

Order

RPN0559

cDNA-Hepatitis E virus Structural protein 2 (a.a.50 to 344)

Q9WJZ5

2 µg

1470

Order

RPN0560

cDNA-Hepatitis E virus genotype 1 Capsid protein (a.a.21 to 420)

P29326

2 µg

1995

Order

RPN0561

cDNA-Hepatitis E virus genotype 1 Protein ORF3 (pORF3) (a.a.17 to 114)

O90299

2 µg

800

Order

RPN0562

cDNA-Hepatitis E virus genotype 3 Capsid protein (a.a.24 to 660)

Q9YLQ9

2 µg

3180

Order

Hepatitis E virus cDNA and recombinant antigen

  • Codon-optimized cDNA is cloned into E. coli expression vector with 6x His-tag at N-terminus and ready-to-use for recombinant protein production.
  • Recombinant protein applications: Western Blot may be used for other applications determined by the user.
  • Protein Purity: >90%, as determined by SDS-PAGE under reducing conditions.
  • Protein Activity: N/A
  • Protein Tag:  Contains A 6x histidine tag at N-terminus.
  • Protein Formulation: Liquid
  • Source: Produced from E. coli

Hepatitis E virus (HEV) is a non-enveloped, single-stranded RNA virus that causes acute hepatitis (liver inflammation) in humans. It is primarily spread through contaminated water or food and is most common in developing countries with poor sanitation conditions. Symptoms of HEV infection include fatigue, abdominal pain, jaundice (yellowing of the skin and eyes), and dark urine. In most cases, HEV infection resolves on its own, but severe cases can lead to liver failure and death, particularly in pregnant women and individuals with weakened immune systems. There is currently no specific antiviral treatment for HEV, and management is focused on relieving symptoms and providing supportive care. Vaccines against HEV are available in some countries, but their use is limited, and their efficacy is still being evaluated.

Hepatitis E virus antigen is a protein found on the surface of the virus that can be used to detect the presence of HEV in a sample, such as blood or stool. Antigens can trigger an immune response, leading to the production of antibodies, which can be used as a marker of HEV infection. The use of HEV antigens in diagnostic tests, such as ELISA (enzyme-linked immunosorbent assay) and rapid immunochromatography tests, is important for detecting and monitoring HEV infection, particularly in outbreaks and in populations at high risk for HEV exposure. The development of recombinant HEV antigens, which are produced in a laboratory using recombinant DNA technology, has improved the sensitivity and specificity of diagnostic tests for HEV.

The genome of Hepatitis E virus (HEV) is a single-stranded RNA molecule that is approximately 7.2 kilobases in length. The HEV genome is positive-sense, meaning that it can be directly translated into protein without the need for reverse transcription. The HEV genome encodes three open reading frames (ORFs), which contain the genetic information for the structural proteins that make up the virus particle and the non-structural proteins that are involved in virus replication and evasion of host immune responses. The genetic diversity of HEV is thought to contribute to its ability to cause outbreaks in different regions and populations around the world. The study of the HEV genome has also led to a better understanding of the molecular mechanisms of HEV replication and pathogenesis, which is important for the development of effective diagnostics, vaccines, and antiviral therapies for HEV infection. HEV encodes for several proteins, including the Capsid protein, X domain, Structural protein 2, and Protein ORF3 (pORF3).


The Capsid protein is the major structural protein of HEV, and it forms the viral capsid that protects the viral RNA. The Capsid protein is also involved in viral entry into host cells.

The X domain is a conserved domain found in HEV and several other RNA viruses. It plays a critical role in viral replication, and it is required for the formation of the replication complex.

Structural protein 2 is involved in virus assembly and release. It interacts with the Capsid protein and is necessary for the production of infectious virions.

Protein ORF3 (pORF3) is a multifunctional protein that modulates host cell signaling pathways and is involved in viral pathogenesis. It is thought to be involved in the inhibition of interferon signaling, which helps the virus evade the host immune response. pORF3 also interacts with the viral capsid protein and is involved in virion assembly.

HEV infection is a significant global health concern, particularly in developing countries with poor sanitation and hygiene. Understanding the roles of these HEV proteins is critical for the development of effective treatments and vaccines against HEV infection. Currently, there is no specific treatment for HEV infection, and the available vaccines are not widely available in many parts of the world.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E.coli expression Vector), which are ready for production of the recombinant proteins.

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