Products

Duck enteritis virus cDNA and Antigen

Cat#

Product Name

Swiss Prot#

Size

Price (US$)

Order

PN0315

Recombinant Protein-Duck enteritis virus Glycoprotein C (a.a.23 to 431)

A6YRK4

100 µg

1195

Order

PN0316

Recombinant Protein-Duck enteritis virus Glycoprotein H (a.a.100 to 450)

Q5D4R9

100 µg

1195

Order

RPN0315

cDNA-Duck enteritis virus Glycoprotein C (a.a.23 to 431)

A6YRK4

2 µg

2040

Order

RPN0316

cDNA-Duck enteritis virus Glycoprotein H (a.a.100 to 450)

Q5D4R9

2 µg

1750

Order

Duck enteritis 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

Duck Enteritis Virus (DEV) is a highly infectious herpesvirus that affects domestic and wild ducks, geese, and other birds. The virus can cause a severe and often fatal disease known as duck viral enteritis, which is characterized by a wide range of clinical signs, including depression, anorexia, diarrhea, and respiratory distress.

The genome of the Duck Enteritis Virus (DEV) has a linear double-stranded DNA structure. The DEV genome consists of approximately 162 kilobase pairs (kbp) and contains both unique and repetitive regions. The unique regions contain most of the genes responsible for viral replication, while the repetitive regions are involved in genome stability and packaging. The DEV genome has a high degree of similarity with other herpesviruses, and its structure is organized into a unique long region, a unique short region, and terminal repeat regions. Understanding the structure of the DEV genome is crucial for developing effective diagnostic tests, treatments, and vaccines against the virus.

The duck enteritis virus glycoprotein antigen refers to the specific portion of the glycoprotein that elicits an immune response and is recognized by the host’s immune system. The glycoprotein antigen is often a target for the development of diagnostic tests and vaccines, as it can stimulate the production of antibodies that help protect against future infection. The detection of antibodies to the duck enteritis virus glycoprotein antigen can be used to diagnose a past or current infection. Understanding the glycoprotein antigen of the duck enteritis virus can provide important information for the development of treatments and vaccines for this virus.

Duck enteritis virus (DEV), also known as duck plague virus, is a herpesvirus that infects ducks and other waterfowl. The genome of DEV encodes several viral proteins, including:

Glycoprotein C: This is a viral envelope glycoprotein that is involved in viral attachment and entry into host cells. It interacts with host cell surface receptors to facilitate viral entry.

Glycoprotein H: This is another viral envelope glycoprotein that is involved in viral entry into host cells. It interacts with glycoprotein L to mediate the fusion of the viral envelope with the host cell membrane.

Understanding the functions and interactions of these glycoproteins is crucial for the development of effective therapies and vaccines against DEV. Several strategies have been proposed for the prevention and control of the disease, including the development of recombinant vaccines, antiviral drugs, and improved biosecurity measures. Continued research into the structure and function of gC and gH will be essential for the development of effective control measures against DEV and other related herpesviruses.

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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