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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0051 | Recombinant Protein-Arcobacter butzleri Acid membrane antigen A (a.a.31 to 348) | A8EVQ0 | 100 µg | 1195 | |
PP0052 | Recombinant Protein-Arcobacter butzleri surface antigen protein (a.a.34 to 434) | A8EU47 | 100 µg | 1195 | |
PP0053 | Recombinant Protein-Arcobacter butzleri Cpn60 groEL protein (a.a.61 to 544) | A8ERY3 | 100 µg | 1195 | |
RPP0051 | cDNA-Arcobacter butzleri Acid membrane antigen A (a.a.31 to 348) | A8EVQ0 | 2 µg | 1585 | |
RPP0052 | cDNA-Arcobacter butzleri surface antigen protein (a.a.34 to 434) | A8EU47 | 2 µg | 2000 | |
RPP0053 | cDNA-Arcobacter butzleri Cpn60 groEL protein (a.a.61 to 544) | A8ERY3 | 2 µg | 2415 |
Arcobacter butzleri cDNA and recombinant antigen
Arcobacter butzleri is a Gram-negative bacterium commonly found in food and water sources. It has been associated with various gastrointestinal illnesses, including diarrhea, abdominal pain, and fever. Understanding the function and importance of specific proteins produced by this bacterium is critical to developing effective treatments and prevention strategies for Arcobacter butzleri infections. In this article, we will explore the role of three key proteins produced by Arcobacter butzleri: Acid membrane antigen A, surface antigen protein, and Cpn60 groEL protein.
Acid membrane antigen A
Acid membrane antigen A (AMA) is a protein produced by Arcobacter butzleri that is involved in the bacterium’s ability to adhere to and invade host cells. AMA has been shown to stimulate an immune response in infected hosts, making it a potential target for vaccine development.
Surface antigen protein
Surface antigen protein (Sap) is another protein produced by Arcobacter butzleri that is involved in the bacterium’s ability to adhere to host cells. Sap is expressed on the surface of the bacterium and is thought to play a role in its pathogenesis.
Cpn60 groEL protein
Cpn60 groEL protein is a chaperonin protein produced by Arcobacter butzleri that 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 Arcobacter butzleri, making it a potential target for diagnostic tests.
The cDNA (complementary DNA) and recombinant antigens of Arcobacter butzleri have various applications in the fields of molecular biology and infectious disease, 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 Arcobacter butzleri, including the identification of genes involved in resistance and the evaluation of the expression of these genes.
Vaccine development: The recombinant antigens of Arcobacter butzleri 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 Arcobacter butzleri in clinical specimens, such as feces and water samples.
Serological assays: The recombinant antigens of Arcobacter butzleri 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 or animal serum. These assays can be used for the diagnosis of Arcobacter 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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