Products

Rickettsia sibirica cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0679

Recombinant protein-Rickettsia sibirica 246 Hypothetical cell surface antigen (a.a.18 to 144)

Q7PA02

100 µg

1195

Order

RPL0679

cDNA-Rickettsia sibirica 246 Hypothetical cell surface antigen (a.a.18 to 144)

Q7PA02

2 µg

756

Order

Rickettsia sibirica 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

Rickettsia sibirica is a gram-negative bacterium transmitted by ticks that causes Siberian tick typhus, a febrile illness characterized by flu-like symptoms, a rash, and a prominent eschar at the site of the tick bite. The bacterium expresses various surface antigens that play a role in its pathogenicity and immune evasion. One of these antigens is the 246 Hypothetical Cell Surface Antigen, whose structure, function, and potential implications for vaccine development are still being studied.

The 246 Hypothetical Cell Surface Antigen is a surface protein expressed by Rickettsia sibirica, a bacterium transmitted by ticks that causes Siberian tick typhus. This antigen is referred to as “hypothetical” because its exact function and role in pathogenesis are still unclear. However, studies have shown that it is immunogenic, meaning that it can elicit an immune response in the host.

The structure of the 246 Hypothetical Cell Surface Antigen is not well understood, as it has not been fully characterized. However, bioinformatic analyses have predicted that it has a size of approximately 246 amino acids and is likely to have a signal peptide for secretion and a transmembrane domain for anchoring to the cell surface.

The function of the 246 Hypothetical Cell Surface Antigen is not fully understood, but studies have shown that it is expressed on the outer surface of Rickettsia sibirica and is immunogenic. This suggests that it may play a role in the bacterium’s pathogenesis and immune evasion.

The 246 Hypothetical Cell Surface Antigen is an attractive candidate for vaccine development against Siberian tick typhus because it is immunogenic and expressed on the surface of the bacterium. However, further studies are needed to determine its exact function and role in pathogenesis, as well as its potential as a vaccine target.

The cDNA (complementary DNA) of Rickettsia sibirica can be used to study the bacterium’s molecular biology and genetics. Researchers can isolate and sequence the cDNA to identify genes that are important for the bacterium’s survival and virulence. This information can be used to develop new strategies for controlling the spread of North Asian tick typhus and other diseases caused by Rickettsia species.

Recombinant antigens, which are proteins that are produced in the laboratory using genetic engineering techniques, can be used for diagnostic tests and vaccine development for Rickettsia sibirica. Researchers can identify antigens from Rickettsia sibirica and produce them using recombinant DNA technology. These recombinant antigens can be used to develop diagnostic tests for the detection of antibodies against Rickettsia sibirica in human or animal serum samples, which can help in early diagnosis and treatment of North Asian tick typhus.

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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