Products

Theileria taurotragi cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0774

Recombinant protein-Theileria taurotragi Merozoite-piroplasm surface antigen (a.a.21 to 244)

O15935

100 µg

1195

Order

PL0775

Recombinant protein-Theileria taurotragi Sporozoite surface antigen STAG-1 (a.a.61 to 460)

Q964R2

100 µg

1195

Order

RPL0774

cDNA-Theileria taurotragi Merozoite-piroplasm surface antigen (a.a.21 to 244)

O15935

2 µg

1338

Order

RPL0775

cDNA-Theileria taurotragi Sporozoite surface antigen STAG-1 (a.a.61 to 460)

Q964R2

2 µg

2394

Order

Theileria taurotragi 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 taurotragi is a protozoan parasite that belongs to the phylum Apicomplexa and is the causative agent of benign theileriosis in cattle. This tick-borne disease is widespread in Africa and causes significant economic losses to the livestock industry.

Merozoite-piroplasm surface antigen (MPSP) and sporozoite surface antigen STAG-1 are two important molecules involved in T. taurotragi pathogenesis and vaccine development.

MPSP: A Key Component of T. taurotragi Infection
MPSP is a highly conserved protein that is expressed on the surface of T. taurotragi merozoites and piroplasms. It is involved in host cell invasion and immune evasion and is a potential vaccine candidate due to its immunogenicity and involvement in pathogenesis.

Recent studies have shown that MPSP plays a critical role in T. taurotragi pathogenesis by facilitating host cell invasion and modulating the host immune response. It also interacts with other parasite molecules to facilitate parasite survival and proliferation within the host.

STAG-1: A Promising Target for Vaccine Development
STAG-1 is a surface-exposed protein that is highly expressed on the surface of T. taurotragi sporozoites. It is an immunodominant antigen that elicits a strong immune response in infected animals.

STAG-1 is a promising target for vaccine development as it has been shown to confer protective immunity against T. taurotragi infection in animal models. It is involved in host cell invasion, and blocking its expression has been shown to reduce parasite burden significantly.

Understanding the Molecular Basis of T. taurotragi Pathogenesis
T. taurotragi pathogenesis is a complex process that involves multiple molecules and pathways. The parasite uses a variety of mechanisms to evade the host immune response, establish a persistent infection, and cause disease.

MPSP and STAG-1 are critical components of T. taurotragi pathogenesis and targeting these molecules could pave the way for the development of effective vaccines and control strategies.

Theileria taurotragi cDNA and recombinant antigens can be applied in the development of genetic and immunological diagnostic tools to detect and monitor the infection of Theileria taurotragi in livestock and wildlife. cDNA and recombinant antigens can be used to develop ELISA-based serological assays for the detection of Theileria taurotragi antibodies in the blood of infected animals. The development of such diagnostic tools could be useful in the management and control of the disease, as well as in the surveillance of at-risk animal populations. Moreover, these tools could be used to monitor the effectiveness of treatments and to identify potential sources of infection.

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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