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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0889 | Recombinant Protein-Staphylococcus aureus MecA-Penicillin binding protein 2 prime (a.a.61 to 461) | Q7DHH4 | 100 µg | 1195 | |
PP0890 | Recombinant Protein-Staphylococcus aureus PBP2 Penicillin binding protein 2 (a.a.61 to 460) | Q9R744 | 100 µg | 1195 | |
PP0891 | Recombinant Protein-Staphylococcus aureus Penicillin-binding protein 1 (a.a.61 to 361) | Q53725 | 100 µg | 1195 | |
PP0892 | Recombinant Protein-Staphylococcus aureus Penicillin-binding protein 3 (a.a.61 to 460) | Q5D1F0 | 100 µg | 1195 | |
PP0893 | Recombinant Protein-Staphylococcus aureus HTH-type transcriptional regulator sarR (a.a.21 to 115) | Q9F0R1 | 100 µg | 1195 | |
PP0894 | Recombinant Protein-Staphylococcus aureus Transcriptional regulator sarA (a.a.21 to 124) | Q2G2U9 | 100 µg | 1195 | |
PP0895 | Recombinant Protein-Staphylococcus aureus 60 kDa chaperonin (a.a.61 to 538) | C5MZ19 | 100 µg | 1195 | |
RPP0889 | cDNA-Staphylococcus aureus MecA-Penicillin binding protein 2 prime (a.a.61 to 461) | Q7DHH4 | 2 µg | 2000 | |
RPP0890 | cDNA-Staphylococcus aureus PBP2 Penicillin binding protein 2 (a.a.61 to 460) | Q9R744 | 2 µg | 1995 | |
RPP0891 | cDNA-Staphylococcus aureus Penicillin-binding protein 1 (a.a.61 to 361) | Q53725 | 2 µg | 1500 | |
RPP0892 | cDNA-Staphylococcus aureus Penicillin-binding protein 3 (a.a.61 to 460) | Q5D1F0 | 2 µg | 1995 | |
RPP0893 | cDNA-Staphylococcus aureus HTH-type transcriptional regulator sarR (a.a.21 to 115) | Q9F0R1 | 2 µg | 800 | |
RPP0894 | cDNA-Staphylococcus aureus Transcriptional regulator sarA (a.a.21 to 124) | Q2G2U9 | 2 µg | 800 | |
RPP0895 | cDNA-Staphylococcus aureus 60 kDa chaperonin (a.a.61 to 538) | C5MZ19 | 2 µg | 2385 |
Staphylococcus aureus cDNA and recombinant antigen
Staphylococcus aureus is a species of Gram-positive bacteria that is a major cause of human disease, including skin infections, food poisoning, and pneumonia. It is found on the skin and in the noses of about 30% of healthy people and can also be found in the environment. It is often spread through contact with contaminated objects, such as towels, and can cause serious infections when it enters the body. Treatment typically involves antibiotics, such as penicillin or methicillin. The bacterium has developed several mechanisms to evade the effects of antibiotics, including the production of beta-lactamase enzymes that can break down penicillin and other beta-lactam antibiotics. In addition, S. aureus has evolved resistance to methicillin and other beta-lactam antibiotics through the acquisition of the mecA gene, which encodes a penicillin-binding protein called PBP2a.
PBP2a is an alternative penicillin-binding protein that has a reduced affinity for beta-lactam antibiotics, which allows S. aureus to survive in the presence of these drugs. The expression of PBP2a is regulated by several factors, including the HTH-type transcriptional regulator sarR and the transcriptional regulator sarA. These proteins are involved in the regulation of genes that are important for virulence, antibiotic resistance, and biofilm formation.
In addition to PBP2a, S. aureus has two other penicillin-binding proteins, PBP1 and PBP3. These proteins are involved in cell wall biosynthesis and are important targets for beta-lactam antibiotics. However, their role in antibiotic resistance is not as well understood as that of PBP2a.
Another protein that is important for the survival of S. aureus is the 60 kDa chaperonin, which is involved in protein folding and stability. This protein is required for the proper folding of many essential proteins in S. aureus, and its expression is regulated by a variety of environmental signals.
Overall, the mecA gene and its product, PBP2a, are key factors in the antibiotic resistance of S. aureus. Understanding the regulation and function of PBP2a and other penicillin-binding proteins may lead to the development of new strategies for the treatment of S. aureus 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.
Staphylococcus aureus cDNA and recombinant antigen can be used in a variety of applications. One application is in the development of a diagnostic test for Staphylococcus aureus. cDNA can be used in PCR-based assays to detect the presence of Staphylococcal genes, while recombinant antigens can be used to develop antibody-based assays to detect the presence of Staphylococcus aureus. cDNA and recombinant antigens can also be used to develop vaccines against Staphylococcus aureus, as well as to study gene expression and protein function. Finally, cDNA and recombinant antigens can be used to develop novel therapeutic agents against Staphylococcus aureus.
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