Products

Rickettsia africae cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0630

Recombinant protein-Rickettsia africae Cell surface antigen OmpA (a.a.61 to 460)

P95585

100 µg

1195

Order

PL0631

Recombinant protein-Rickettsia africae Cell surface antigen Sca12 (a.a.61 to 460)

C3PPE1

100 µg

1195

Order

PL0632

Recombinant protein-Rickettsia africae Cell surface antigen Sca9 (a.a.31 to 306)

C3PLU4

100 µg

1195

Order

PL0633

Recombinant protein-Rickettsia africae outer surface protein (a.a.19 to 227)

C3PLW0

100 µg

1195

Order

RPL0630

cDNA-Rickettsia africae Cell surface antigen OmpA (a.a.61 to 460)

P95585

2 µg

2394

Order

RPL0631

cDNA-Rickettsia africae Cell surface antigen Sca12 (a.a.61 to 460)

C3PPE1

2 µg

2394

Order

RPL0632

cDNA-Rickettsia africae Cell surface antigen Sca9 (a.a.31 to 306)

C3PLU4

2 µg

1650

Order

RPL0633

cDNA-Rickettsia africae outer surface protein (a.a.19 to 227)

C3PLW0

2 µg

1248

Order

Rickettsia africae 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 africae is a species of bacteria that lives in ticks and causes African tick bite fever. It is an intracellular parasite and has a polysaccharide capsule. The antigen of this species is mainly composed of the polysaccharide capsule, as well as lipopolysaccharide, proteins, and other molecules. The polysaccharide capsule is the primary antigenic target of the immune system. The polysaccharide capsule is composed of several polysaccharide moieties including glucose, mannose, and galactose. It also contains several proteins, such as the major surface antigen and the minor surface antigen. The major surface antigen is responsible for stimulating the antibody response in the infected individual, while the minor surface antigen is responsible for the recognition of the bacteria by the immune system.

The bacterium possesses several surface proteins, including OmpA, Sca12, Sca9, and Outer Surface Protein, that are believed to play a significant role in its pathogenesis.

OmpA, Sca12, and Sca9 are cell surface proteins that are essential for the bacterium’s attachment and invasion into host cells. Outer Surface Protein is an outer membrane protein that is believed to play a role in the bacterium’s ability to evade the host’s immune system. Researchers are interested in understanding the mechanisms by which these proteins contribute to Rickettsia africae’s pathogenesis and exploring their potential as therapeutic targets.

Rickettsia africae cDNA and recombinant antigen genes can be used in a variety of applications. One potential application of these genes is in the development of diagnostic methods for the detection of the bacteria in clinical samples. Several molecular techniques, such as quantitative real-time PCR and rtPCR, can be used to detect the presence of Rickettsia africae in clinical samples. Additionally, the recombinant antigens can be used to develop immunoassays for the detection of the bacteria. These immunoassays could include ELISA, Western blotting and immunofluorescence. The recombinant antigens could also be used to develop vaccines and other therapeutic agents for the prevention and treatment of infections caused by Rickettsia africae.

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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