Products

Theileria Hongan cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0772

Recombinant protein-Theileria Hongan buffalo 23 kDa piroplasm surface protein (a.a.38 to 223)

B2LUF8

100 µg

1195

Order

RPL0772

cDNA-Theileria Hongan buffalo 23 kDa piroplasm surface protein (a.a.38 to 223)

B2LUF8

2 µg

1110

Order

Theileria Hongan 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

Theileria Hongan is a tick-borne parasite that infects buffaloes and causes a disease known as tropical theileriosis. The disease is characterized by fever, anemia, and jaundice, and can be fatal if left untreated. Theileria Hongan is prevalent in Asia, particularly in China, India, and Southeast Asia, where it poses a significant threat to the livestock industry.

One of the key factors that contribute to the virulence of Theileria Hongan is its 23 kDa piroplasm surface protein (p23). This protein is located on the surface of the parasite’s merozoites, which are the invasive form of the parasite that infects the host’s red blood cells. The p23 protein is known to play a crucial role in the parasite’s survival and pathogenesis by facilitating its attachment and invasion of host cells.

The p23 protein is highly antigenic, meaning that it can trigger a strong immune response in the host. However, Theileria Hongan has developed several strategies to evade the host’s immune system, including antigenic variation, which allows the parasite to switch between different variants of the p23 protein to avoid recognition by the host’s immune system.

Recent studies have shown that the p23 protein is also involved in the regulation of the parasite’s cell cycle and differentiation. Theileria Hongan is known to have a complex life cycle, involving multiple stages of development within the tick vector and the host’s blood cells. The p23 protein has been shown to play a critical role in the differentiation of the parasite’s merozoites into the more invasive and virulent schizont stage.

Understanding the role of the p23 protein in Theileria Hongan’s pathogenesis and survival is crucial for the development of effective strategies for the prevention and control of tropical theileriosis. Researchers are currently exploring the potential of the p23 protein as a target for vaccine development, which could provide long-lasting protection against Theileria Hongan infection in buffaloes.

Theileria hongan cDNA and recombinant antigen can be used for the diagnosis of Theileria hongan infection in animals. cDNA can be used for the detection of Theileria hongan specific gene sequences in animals. The recombinant antigen can be used for the development of an ELISA-based diagnostic test for Theileria hongan infection. The antigen can also be used to develop an immunochromatographic test (ICT) for the detection of Theileria hongan antibody in animal serum. Both of these tests can be used to diagnose Theileria hongan infection in animals.

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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