Products

Theileria sergenti cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0769

Recombinant protein-Theileria sergenti TS-Ikeda type 23 kDa piroplasm surface protein (a.a.27 to 223)

Q9NDX7

100 µg

1195

Order

PL0770

Recombinant protein-Theileria sergenti Piroplasm major immunodominant protein (a.a.24 to 283)

Q27401

100 µg

1195

Order

RPL0769

cDNA-Theileria sergenti TS-Ikeda type 23 kDa piroplasm surface protein (a.a.27 to 223)

Q9NDX7

2 µg

1176

Order

RPL0770

cDNA-Theileria sergenti Piroplasm major immunodominant protein (a.a.24 to 283)

Q27401

2 µg

1554

Order

Theileria sergenti 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 sergenti is a protozoan parasite that belongs to the phylum Apicomplexa and is the causative agent of theileriosis in cattle. This tick-borne disease is prevalent in Asia, particularly in Japan and Korea, and causes significant economic losses to the livestock industry.

TS-Ikeda type 23 kDa piroplasm surface protein and piroplasm major immunodominant protein (PMID) are two important molecules involved in T. sergenti pathogenesis and immune evasion.

TS-Ikeda Type 23 kDa Piroplasm Surface Protein: A Critical Component of T. sergenti Infection
TS-Ikeda type 23 kDa piroplasm surface protein is a surface-exposed protein that is highly expressed on the surface of T. sergenti-infected cells. It is a potential vaccine candidate due to its immunogenicity and involvement in pathogenesis.

Recent studies have shown that TS-Ikeda type 23 kDa piroplasm surface protein plays a critical role in host cell invasion, as well as immune evasion. It modulates the host immune response by inducing the production of cytokines and chemokines, which dampen the immune response and allow the parasite to establish a persistent infection.

PMID: A Promising Target for Vaccine Development
PMID is a highly conserved protein that is expressed on the surface of T. sergenti-infected cells. It is an immunodominant protein that elicits a strong immune response in infected animals.

PMID is a promising target for vaccine development as it has been shown to confer protective immunity against T. sergenti 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. sergenti Pathogenesis
T. sergenti 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.

TS-Ikeda type 23 kDa piroplasm surface protein and PMID are critical components of T. sergenti pathogenesis and targeting these molecules could pave the way for the development of effective vaccines and control strategies.

The cDNA and recombinant antigens from the parasite have been used in the development of diagnostic tests for theileriosis. These tests are used to detect the presence of the parasite in cattle, and to monitor the severity of the disease. cDNA and recombinant antigens have also been used to develop vaccines against theileriosis, which can help reduce the spread of the disease and decrease the economic losses associated with it. In addition, cDNA and recombinant antigens from Theileria sergenti have been used to study the biology of the parasite, and to develop new drugs and treatments to combat theileriosis.

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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