Products

Gorilla hepatitis B virus cDNA and Antigen

Cat#

Product Name

Swiss Prot#

Size

Price (US$)

Order

PN0477

Recombinant Protein-Gorilla hepatitis B virus Capsid protein HBcAg(a.a.29 to 183)

P0C6I9

100 µg

1195

Order

PN0478

Recombinant Protein-Gorilla hepatitis B virus External core antigen-HBeAg (a.a.20 to 183)

Q9WJE9

100 µg

1195

Order

PN0479

Recombinant Protein-Gorilla hepatitis B virus large envelope protein (a.a.2 to 170)

Q9WKC4

100 µg

1195

Order

RPN0477

cDNA-Gorilla hepatitis B virus Capsid protein HBcAg(a.a.29 to 183)

P0C6I9

2 µg

770

Order

RPN0478

cDNA-Gorilla hepatitis B virus External core antigen-HBeAg (a.a.20 to 183)

Q9WJE9

2 µg

978

Order

RPN0479

cDNA-Gorilla hepatitis B virus large envelope protein (a.a.2 to 170)

Q9WKC4

2 µg

840

Order

Gorilla hepatitis B 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

Gorilla hepatitis B virus (GHBV) is a type of hepatitis B virus that infects gorillas. It is like the hepatitis B virus that affects humans, but it is not known to be transmissible to humans. GHBV can cause liver disease in infected gorillas, leading to symptoms such as fatigue, jaundice, and abdominal pain. There is no specific treatment for GHBV infection in gorillas, but efforts to conserve and protect gorilla populations can help reduce the spread of the virus in the wild.

Gorilla hepatitis B virus (GHBV) antigen refers to a substance (protein) present on the surface of GHBV that triggers an immune response. Antigens are recognized by the body’s immune system and help it identify pathogens, such as GHBV. In the context of GHBV, the antigen can be used as a tool for developing diagnostic tests to detect GHBV infection in gorillas. Additionally, the antigen may be used for vaccine development to help protect gorillas from GHBV infection.

Gorilla hepatitis B virus (GHBV) is a member of the Hepadnaviridae family, which includes the human hepatitis B virus (HBV) and other related viruses.

The GHBV virion is composed of a partially double-stranded DNA genome enclosed in an icosahedral capsid, which is itself surrounded by an envelope. Several viral proteins are involved in the assembly and function of the GHBV virion, including:

Capsid protein HBcAg – The HBcAg protein forms the viral capsid and is involved in the packaging and protection of the viral genome.

HBeAg – The HBeAg protein is derived from the precore/core region of the viral genome and is secreted into the bloodstream. It is thought to play a role in regulating the immune response to the virus and may facilitate viral replication.

Large envelope protein – The large envelope protein is involved in the assembly and release of the virion, as well as viral entry into host cells.

The capsid protein HBcAg is a major target of the host immune system and can elicit a strong antibody response in infected individuals. The HBeAg protein is also an important target for the host immune response and is used as a marker of viral replication in clinical settings.

Chronic infection with GHBV, as with HBV, can lead to the development of liver disease, including cirrhosis and liver cancer. Antiviral therapies, including nucleoside analogs and interferon, are effective in suppressing viral replication and reducing the risk of liver disease in infected individuals. Vaccines for HBV are also effective in preventing infection with GHBV, as the two viruses share a high degree of genetic similarity.

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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