Rickettsia massiliae is a species of Gram-negative bacteria that belongs to the family Rickettsiaceae. It is an obligate intracellular pathogen that is transmitted to humans through tick bites. R. massiliae is known to cause a febrile illness that is similar to Mediterranean spotted fever, and it has been reported in different parts of the world, including Europe, Africa, and the Americas.

The intracytoplasmic 120 kDa protein of R. massiliae is an important virulence factor that is involved in the survival and replication of the bacterium inside host cells. It is encoded by the gene rOmpB, which is located in the bacterial chromosome. This protein is synthesized as a precursor that is then cleaved into two fragments, a 32 kDa N-terminal fragment and a 88 kDa C-terminal fragment.

The 120 kDa protein is believed to be involved in the regulation of gene expression, the modification of host cell membranes, and the evasion of host immune defenses. It has been shown to interact with several host proteins, including actin and heat shock protein 90, which may be involved in the formation of a specialized niche for the bacterium inside host cells.

The cell surface antigens Sca2 and Sca4 of R. massiliae are involved in the adhesion of the bacterium to host cells and in the modulation of the host immune response. These antigens are located in the outer membrane of the bacterium and are exposed on the surface of the bacterial cell.

Sca2 and Sca4 are both highly conserved among different species of Rickettsia, and they are believed to be involved in the initial stages of host cell invasion. They have been shown to interact with several host proteins, including integrins and laminin, which are important components of the extracellular matrix.

Rickettsia massiliae 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
• Protein Formulation: Liquid
• Source: Produced from E. coli

Rickettsia massiliae cDNA and recombinant antigens can be used for the diagnosis and treatment of infections caused by this species. They can be applied in a variety of ways, such as PCR-based assays, immunoassays, or other techniques to detect the presence of the pathogen. Additionally, they can be used to develop vaccines or therapeutic agents that can be used to effectively treat rickettsial infections.

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.