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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0048 | Recombinant Protein-Anaplasma phagocytophilum 60 kDa chaperonin 55 kDa major antigen (a.a.61 to 541) | O34191 | 100 µg | 1195 | |
PP0049 | Recombinant Protein-Anaplasma phagocytophilum Granulocytic ehrlichiosis antigen (a.a.25 to 438) | O85039 | 100 µg | 1195 | |
PP0050 | Recombinant Protein-Anaplasma phagocytophilum P44 major (a.a.30 to 165) | C8YM65 | 100 µg | 1195 | |
RPP0048 | cDNA-Anaplasma phagocytophilum 60 kDa chaperonin 55 kDa major antigen (a.a.61 to 541) | O34191 | 2 µg | 2400 | |
RPP0049 | cDNA-Anaplasma phagocytophilum Granulocytic ehrlichiosis antigen (a.a.25 to 438) | O85039 | 2 µg | 2065 | |
RPP0050 | cDNA-Anaplasma phagocytophilum P44 major (a.a.30 to 165) | C8YM65 | 2 µg | 800 |
Anaplasma phagocytophilum cDNA and recombinant antigen
Anaplasma phagocytophilum is a bacterium that causes granulocytic ehrlichiosis, a disease that affects both humans and animals. It has several key proteins, including the 60 kDa chaperonin, 55 kDa Major Antigen, Granulocytic Ehrlichiosis Antigen, and P44 Major protein, that are essential for its survival and pathogenesis.
The 60 kDa chaperonin is a protein that helps the bacterium to maintain its shape and structure. It plays an important role in the folding of other proteins in Anaplasma phagocytophilum. The 55 kDa Major Antigen is a surface protein that interacts with the host’s immune system and is crucial for the bacterium’s survival.
The Granulocytic Ehrlichiosis Antigen is a protein that is found on the surface of the bacterium and is involved in the attachment and invasion of host cells. P44 Major is another surface protein that is essential for the bacterium’s survival, as it plays a critical role in evading the host’s immune system.
Anaplasma phagocytophilum is a bacterium that causes granulocytic ehrlichiosis and has several key proteins, including the 60 kDa chaperonin, 55 kDa Major Antigen, Granulocytic Ehrlichiosis Antigen, and P44 Major protein, that are essential for its survival and pathogenesis. Understanding the function of these proteins can help in the development of effective strategies to control and prevent granulocytic ehrlichiosis.
The cDNA (complementary DNA) and antigens of Anaplasma phagocytophilum 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 Anaplasma phagocytophilum, including the identification of genes involved in resistance and the evaluation of the expression of these genes.
Vaccine development: The antigens of Anaplasma phagocytophilum 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 Anaplasma phagocytophilum in clinical specimens, such as blood and serum.
Serological assays: The antigens of Anaplasma phagocytophilum 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 anaplasmosis.
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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