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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0057 | Recombinant Protein-Atopobium rimae Antigen B (a.a.35 to 137) | B9CN39 | 100 µg | 1195 | |
PP0058 | Recombinant Protein-Atopobium rimae 60 kDa chaperonin (a.a.61 to 546) | B9CN95 | 100 µg | 1195 | |
PP0059 | Recombinant Protein-Atopobium rimae Outer surface protein (a.a.40 to 368) | B9CLC8 | 100 µg | 1195 | |
RPP0057 | cDNA-Atopobium rimae Antigen B (a.a.35 to 137) | B9CN39 | 2 µg | 800 | |
RPP0058 | cDNA-Atopobium rimae 60 kDa chaperonin (a.a.61 to 546) | B9CN95 | 2 µg | 2425 | |
RPP0059 | cDNA-Atopobium rimae Outer surface protein (a.a.40 to 368) | B9CLC8 | 2 µg | 1640 |
Atopobium rimae cDNA and recombinant antigen
Atopobium rimae is a Gram-positive bacterium found in the oral microbiome of humans. While it is considered a commensal bacterium, it has been associated with various oral infections, including periodontitis and endodontic infections. Understanding the function and importance of specific proteins produced by this bacterium is critical to developing effective treatments and prevention strategies for Atopobium rimae infections. In this article, we will explore the role of three key proteins produced by Atopobium rimae : Antigen B, 60 kDa chaperonin, and outer surface protein.
Antigen B
Antigen B is a protein produced by Atopobium rimae that has been shown to stimulate an immune response in infected hosts. This protein is thought to play a role in the pathogenesis of Atopobium rimae infections by allowing the bacterium to evade host immune defenses.
60 kDa chaperonin
The 60 kDa chaperonin protein produced by Atopobium rimae is involved in the folding and assembly of other proteins necessary for the bacterium’s survival. This protein has been shown to be highly conserved across different strains of Atopobium rimae , making it a potential target for diagnostic tests.
Outer surface protein
The outer surface protein (Osp) produced by Atopobium rimae is involved in the bacterium’s ability to adhere to host cells. Osp has been shown to be highly antigenic, making it a potential target for vaccine development.
The cDNA (complementary DNA) and recombinant antigens of Atopobium rimae have various applications in the fields of molecular biology and oral health, including:
Gene expression analysis: The cDNA can be used as a template to synthesize complementary RNA (cRNA) which can then be used for microarray or RNA sequencing (RNA-seq) analysis to study gene expression patterns in the bacterium under different conditions.
Antimicrobial resistance studies: The cDNA can be used to study the mechanisms of antibiotic resistance in Atopobium rimae , including the identification of genes involved in resistance and the evaluation of the expression of these genes.
Vaccine development: The recombinant antigens of Atopobium rimae can be used to develop subunit vaccines against the bacterium. These antigens can stimulate the immune system to mount a response against the pathogen.
Diagnostics: The cDNA can be used to develop real-time PCR (polymerase chain reaction) assays for the rapid and sensitive detection of Atopobium rimae in clinical specimens, such as saliva, dental plaque, and gingival tissues.
Serological assays: The recombinant antigens of Atopobium rimae can be used to develop serological assays, such as ELISA (enzyme-linked immunosorbent assay), to detect the presence of antibodies against the bacterium in human serum. These assays can be used for the diagnosis of Atopobium rimae 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.
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