Products

Theileria mutans cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0762

Recombinant protein-Theileria mutans 32 kDa immunodominant piroplasm surface antigen (a.a.19 to 256)

P90657

100 µg

1195

Order

RPL0762

cDNA-Theileria mutans 32 kDa immunodominant piroplasm surface antigen (a.a.19 to 256)

P90657

2 µg

1422

Order

Theileria mutans 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 mutans is a species of protozoan parasite that causes bovine theileriosis, a tick-borne disease that affects cattle in many parts of the world. This disease is characterized by fever, anemia, weight loss, and sometimes death, leading to significant economic losses in the livestock industry.

One of the key proteins involved in the immune response to T. mutans is the 32 kDa immunodominant piroplasm surface antigen. This protein is expressed on the surface of the parasite and is recognized by the host’s immune system, leading to the production of antibodies that can help clear the infection.

Research has shown that the 32 kDa antigen is highly conserved across different strains of T. mutans, making it a promising target for diagnostic tests. A number of studies have investigated the use of this antigen in various diagnostic assays, including ELISA and Western blotting, with promising results.

In addition to its diagnostic potential, the 32 kDa antigen has also been studied for its immunogenicity, with some researchers exploring its use as a vaccine candidate. Several studies have shown that vaccination with the antigen can provide protection against T. mutans infection in experimental animal models, although further research is needed to evaluate its efficacy under field conditions.

Overall, the 32 kDa immunodominant piroplasm surface antigen of T. mutans is a promising target for both diagnostic and vaccine development purposes. As research in this area continues, it is hoped that new tools and strategies can be developed to help control the spread of bovine theileriosis and reduce its impact on the livestock industry.

Theileria mutans is a tick-borne protozoan parasite which is the causative agent of tropical theileriosis. The diagnosis of this infection is challenging due to its complex life cycle and the lack of specific diagnostic antigen targets. The application of cDNA and recombinant antigen in the diagnosis of Theileria mutans infection has been explored in recent years as a potential alternative to traditional methods of diagnosis. cDNA and recombinant antigen of Theileria mutans can be used to detect both the presence of the parasite in an animal as well as the presence of antibodies that may be present due to a previous infection. This method of diagnosis has the potential to be more accurate than traditional methods as it can detect both the presence of the parasite and the presence of antibodies, thus providing a more accurate diagnosis. Additionally, this method is cost-effective and can be used in a wide variety of settings.

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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