Products

Atopobium rimae cDNA and Antigen

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

Order

PP0058

Recombinant Protein-Atopobium rimae  60 kDa chaperonin (a.a.61 to 546)

B9CN95

100 µg

1195

Order

PP0059

Recombinant Protein-Atopobium rimae  Outer surface protein (a.a.40 to 368)

B9CLC8

100 µg

1195

Order

RPP0057

cDNA-Atopobium rimae  Antigen B (a.a.35 to 137)

B9CN39

2 µg

800

Order

RPP0058

cDNA-Atopobium rimae  60 kDa chaperonin (a.a.61 to 546)

B9CN95

2 µg

2425

Order

RPP0059

cDNA-Atopobium rimae  Outer surface protein (a.a.40 to 368)

B9CLC8

2 µg

1640

Order

Atopobium rimae 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

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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