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Cat# | Products (Recombinant protein) | Swiss Prot# | Size | Price (US$) | Order |
PP0926 | Recombinant Protein-Stigmatella aurantiaca200 kDa antigen p200 (a.a.31 to 387) | Q08UX0 | 100 µg | 1195 | |
PP0927 | Recombinant Protein-Stigmatella aurantiaca 5E5 antigen (a.a.31 to 383) | Q091F7 | 100 µg | 1195 | |
PP0928 | Recombinant Protein-Stigmatella aurantiaca Immunoreactive 87kD antigen PG92 (a.a.61 to 460) | Q097W8 | 100 µg | 1195 | |
PP0929 | Recombinant Protein-Stigmatella aurantiaca Latency associated antigen (a.a.23 to 115) | Q08Y11 | 100 µg | 1195 | |
PP0930 | Recombinant Protein-Stigmatella aurantiaca nuclear antigen (a.a.61 to 461) | Q08N41 | 100 µg | 1195 | |
PP0931 | Recombinant Protein-Stigmatella aurantiaca-surface antigen (a.a.61 to 460) | Q08RS1 | 100 µg | 1195 | |
PP0932 | Recombinant Protein-Stigmatella aurantiaca Surface antigen variable number repeat domain protein (a.a.25 to 428) | Q08N89 | 100 µg | 1195 | |
RPP0926 | cDNA-Stigmatella aurantiaca 200 kDa antigen p200 (a.a.31 to 387) | Q08UX0 | 2 µg | 1780 | |
RPP0927 | cDNA-Stigmatella aurantiaca 5E5 antigen (a.a.31 to 383) | Q091F7 | 2 µg | 1760 | |
RPP0928 | cDNA-Stigmatella aurantiaca Immunoreactive 87kD antigen PG92 (a.a.61 to 460) | Q097W8 | 2 µg | 1995 | |
RPP0929 | cDNA-Stigmatella aurantiaca Latency associated antigen (a.a.23 to 115) | Q08Y11 | 2 µg | 800 | |
RPP0930 | cDNA-Stigmatella aurantiaca nuclear antigen (a.a.61 to 461) | Q08N41 | 2 µg | 2000 | |
RPP0931 | cDNA-Stigmatella aurantiaca-surface antigen (a.a.61 to 460) | Q08RS1 | 2 µg | 1995 | |
RPP0932 | cDNA-Stigmatella aurantiaca Surface antigen variable number repeat domain protein (a.a.25 to 428) | Q08N89 | 2 µg | 2015 |
Stigmatella aurantiaca cDNA and recombinant antigen
Stigmatella aurantiaca is a soil-dwelling bacterium that exhibits a complex life cycle involving aggregation, fruiting body formation, and sporulation. During these processes, the bacterium produces a range of antigens that play important roles in cellular differentiation, development, and immunity. In this article, we will explore some of the key antigens produced by Stigmatella aurantiaca, including the 200 kDa antigen p200, 5E5 antigen, immunoreactive 87 kDa antigen PG92, latency-associated antigen, nuclear antigen, surface antigen, and surface antigen variable number repeat domain protein.
The 200 kDa antigen p200 is a surface-exposed protein that is involved in cell adhesion and aggregation during the early stages of fruiting body formation. It is also thought to play a role in the maintenance of the extracellular matrix that surrounds the developing fruiting body.
The 5E5 antigen is a cell surface protein that is involved in the recognition and adhesion of developing fruiting bodies. It has been shown to be immunogenic and may be a potential target for the development of new diagnostics and therapeutics.
The immunoreactive 87 kDa antigen PG92 is a nuclear protein that is involved in the regulation of gene expression during cellular differentiation. It is also thought to play a role in the maintenance of cell viability during the formation of fruiting bodies.
The latency-associated antigen is a nuclear protein that is involved in the maintenance of cellular quiescence and is essential for the development of mature fruiting bodies. It is also thought to play a role in the regulation of gene expression during cellular differentiation.
The nuclear antigen is a protein that is involved in the regulation of DNA replication and repair during cellular differentiation. It is also thought to play a role in the maintenance of genomic stability during the formation of fruiting bodies.
The surface antigen is a protein that is exposed on the surface of Stigmatella aurantiaca cells and is involved in cellular adhesion and communication during the formation of fruiting bodies. It has also been shown to be immunogenic and may be a potential target for the development of new diagnostics and therapeutics.
The surface antigen variable number repeat domain protein is a surface-exposed protein that is involved in the recognition and adhesion of other cells during the formation of fruiting bodies. It is also thought to play a role in the maintenance of the extracellular matrix that surrounds the developing fruiting body.
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.
The use of cDNA (complementary DNA) and recombinant antigens derived from Stigmatella aurantiaca can have various applications in the fields of molecular biology, biotechnology, and environmental science. Some of these applications include:
Study of bacterial biology: The use of cDNA from Stigmatella aurantiaca can help researchers to study the biology of this unique group of bacteria. By analyzing the cDNA, researchers can identify the genes and gene products involved in the bacteria’s unique cellular structures and metabolic processes.
Study of bacterial evolution: The use of cDNA from Stigmatella aurantiaca can help researchers to study the evolution of this group of bacteria. By analyzing the cDNA, researchers can identify genetic changes that occur in the bacteria over time, which can provide insights into the evolution of planctomycetes.
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