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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0296 | Recombinant Protein-Coxiella burnetii 10 kDa chaperonin Protein Cpn10 (a.a.21 to 96) | P19422 | 100 µg | 1195 | |
PP0297 | Recombinant Protein-Coxiella burnetii 17 kDa common-antigen (a.a.27 to 150) | A9KBM9 | 100 µg | 1195 | |
PP0298 | Recombinant Protein-Coxiella burnetii 60 kDa chaperonin Cpn60 (a.a.61 to 552) | P19421 | 100 µg | 1195 | |
PP0299 | Recombinant Protein-Coxiella burnetii Lipoprotein antigen (a.a.26 to 396) | B6J4R2 | 100 µg | 1195 | |
PP0300 | Recombinant Protein-Coxiella burnetii P1 (a.a.29 to 252) | Q83EK8 | 100 µg | 1195 | |
PP0301 | Recombinant Protein-Coxiella burnetii Surface antigen (a.a.11 to 142) | A9ZLH5 | 100 µg | 1195 | |
RPP0296 | cDNA-Coxiella burnetii 10 kDa chaperonin Protein Cpn10 (a.a.21 to 96) | P19422 | 2 µg | 800 | |
RPP0297 | cDNA-Coxiella burnetii 17 kDa common-antigen (a.a.27 to 150) | A9KBM9 | 2 µg | 800 | |
RPP0298 | cDNA-Coxiella burnetii 60 kDa chaperonin Cpn60 (a.a.61 to 552) | P19421 | 2 µg | 2455 | |
RPP0299 | cDNA-Coxiella burnetii Lipoprotein antigen (a.a.26 to 396) | B6J4R2 | 2 µg | 1850 | |
RPP0300 | cDNA-Coxiella burnetii P1 (a.a.29 to 252) | Q83EK8 | 2 µg | 1115 | |
RPP0301 | cDNA-Coxiella burnetii Surface antigen (a.a.11 to 142) | A9ZLH5 | 2 µg | 800 |
Coxiella burnetii cDNA and recombinant antigen
Coxiella burnetii is a highly infectious intracellular bacterium that causes Q fever in humans and animals. This bacterium is known for its ability to evade the host immune system, which makes it a significant threat to public health. In this article, we will discuss the importance of several key proteins of Coxiella burnetii, including the 10 kDa chaperonin Protein Cpn10, 17 kDa common-antigen, 60 kDa chaperonin Cpn60, Lipoprotein antigen, P1, and Surface antigen.
Understanding Coxiella burnetii Proteins: Coxiella burnetii produces a range of proteins that are essential for its survival and replication inside host cells. These proteins play critical roles in evading the host immune system and establishing a successful infection. Let’s take a closer look at some of the most important proteins produced by this bacterium.
10 kDa Chaperonin Protein Cpn10: The 10 kDa chaperonin Protein Cpn10, also known as GroES, is a key component of the bacterial chaperonin system. This protein is essential for the folding and assembly of other Coxiella burnetii proteins, which is critical for the bacterium’s survival inside host cells. The Cpn10 protein has been identified as a potential target for the development of new antibiotics to treat Q fever.
17 kDa Common-Antigen: The 17 kDa common-antigen is a highly conserved protein that is produced by Coxiella burnetii. This protein is involved in the bacterium’s ability to establish a successful infection and evade the host immune system. The 17 kDacommon antigen is also used in laboratory tests for the diagnosis of Q fever.
60 kDa Chaperonin Cpn60: The 60 kDa chaperonin Cpn60, also known as GroEL, is another key component of the bacterial chaperonin system. This protein is essential for the folding and assembly of other Coxiella burnetiiproteins and has been shown to play a critical role in the bacterium’s pathogenesis.
Lipoprotein Antigen, P1, and Surface Antigen: Coxiella burnetii also produces a range of other proteins that are involved in its pathogenesis, including the Lipoprotein antigen, P1, and Surface antigen. The Lipoprotein antigen is involved in the bacterium’s ability to evade the host immune system, while P1 is a protein that has been identified as a potential vaccine candidate. The Surface antigen is involved in the bacterium’s ability to attach to host cells and establish an infection.
Coxiella burnetii is a highly infectious intracellular bacterium that causes Q fever in humans and animals. Its ability to evade the host immune system and establish a successful infection is due, in part, to the production of a range of key proteins, including the 10 kDa chaperonin Protein Cpn10, 17 kDa common-antigen, 60 kDa chaperonin Cpn60, Lipoprotein antigen, P1, and Surface antigen. Further research into these proteins could lead to the development of new treatments and vaccines for Q fever.
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.
One application of C. burnetii cDNA is in the identification of virulence factors. By sequencing and analyzing cDNA libraries, researchers can identify genes that are important for the pathogenesis of the bacterium, providing insights into the mechanisms of infection.
Recombinant antigens derived from C. burnetii have been used in the development of diagnostic tests for Q fever. These tests are based on the detection of antibodies against specific antigens in the patient’s serum. Recombinant antigens have been shown to have improved sensitivity and specificity compared to traditional diagnostic tests, making them useful tools for the rapid and accurate diagnosis of Q fever.
Another application of recombinant antigens is in the development of a vaccine for Coxiella burnetii. Several recombinant antigens have been shown to elicit a protective immune response in animal models and are being evaluated in preclinical and clinical trials.
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