Products

Theileria cervi cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0760

Recombinant protein-Theileria cervi Heat shock protein 70 (a.a.61 to 460)

Q0WY76

100 µg

1195

Order

RPL0760

cDNA-Theileria cervi Heat shock protein 70 (a.a.61 to 460)

Q0WY76

2 µg

2394

Order

Theileria cervi 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 cervi is a parasitic protozoan that infects deer and causes a disease known as theileriosis. This disease can have serious consequences for the health of the infected animals, and it can even be fatal in some cases. One of the key proteins involved in the pathogenesis of T. cervi is the heat shock protein 70 (HSP70).

HSP70 is a chaperone protein that plays a critical role in protecting cells from stress. It is involved in a wide range of cellular processes, including protein folding, protein trafficking, and quality control. HSP70 is also known to be involved in the immune response to infectious agents, including parasites like T. cervi.

In T. cervi, HSP70 is thought to play a key role in the survival and proliferation of the parasite within the host. The protein is expressed on the surface of the parasite, where it may help the parasite evade the host immune system. HSP70 may also be involved in the transport of other parasite proteins across the parasite membrane.

Research has shown that HSP70 is a highly conserved protein across different species of Theileria, including T. annulata, T. parva, and T. equi. This suggests that the protein plays a critical role in the biology of these parasites, and that it may be a promising target for the development of new anti-parasitic drugs.

In addition to HSP70, other proteins have also been identified as potential drug targets in T. cervi. These include the polymorphic antigen (Ta9), the proliferating cell nuclear antigen (PCNA), and the surface protein (TaSP and d). Each of these proteins plays a critical role in the survival and proliferation of the parasite within the host and may therefore be a promising target for the development of new therapies.

Theileria cervi cDNA and recombinant antigen can be used in diagnosis, vaccine development, and in the development of diagnostic tests and therapeutic agents.

1. Diagnosis: Theileria cervi cDNA and recombinant antigen can be used to detect Theileria cervi infection. For example, a PCR-based assay has been developed to detect the presence of the parasite in blood samples. This assay is highly sensitive and specific and can be used for the diagnosis of Theileria cervi in both clinical and veterinary settings.

2. Vaccine development: Recombinant antigens from Theileria cervi can be used to develop subunit vaccines that induce the production of antibodies against the parasite, thus providing protection against infection.

3. Diagnostic tests: Theileria cervi cDNA and recombinant antigen can be used to develop diagnostic tests that can detect the presence of the parasite in the blood. These tests can be used to diagnose and monitor the progression of Theileria cervi 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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