M.Pneumoniae P30
Escherichia Coli.
Sterile Filtered clear solution.
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Description
M.Pneumoniae P30 Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 18-19kDa.
M.Pneumoniae P30 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Product Specs
Mycoplasma pneumonia, a type of atypical pneumonia, is caused by the bacterium M. pneumoniae. This infection primarily affects individuals under 40 years old, accounting for 15% to 50% of pneumonia cases in adults and even more in school-aged children. While those in crowded environments like schools and shelters are at higher risk, many patients lack identifiable risk factors. The membrane proteins P1, P30, and P116 of M. pneumoniae are recognized as adhesion factors, with P1 being the primary protein involved in colonization.
Recombinant M.Pneumoniae P30, produced in E.Coli, is a non-glycosylated polypeptide chain with a molecular weight of 18-19kDa. It features a 6 amino acid His-tag fused at the C-terminus and is purified using proprietary chromatographic techniques.
The product appears as a clear, sterile-filtered solution.
The MP-P30c solution is formulated with 25mM K2CO3, 0.025% NaN3, and PBS.
While the Recombinant MP-P30c protein remains stable at 4°C for up to one week, long-term storage below -18°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is suggested for long-term storage. It is crucial to avoid repeated freeze-thaw cycles.
The protein's purity exceeds 95%, as determined by 10% PAGE (coomassie staining).
This product is suitable for immunoassay applications.
Escherichia Coli.
Product Science Overview
Mycoplasma pneumoniae is a unique, cell wall-deficient bacterium that primarily infects the human respiratory tract. It is a significant cause of respiratory infections, including tracheobronchitis and atypical pneumonia, often referred to as “walking pneumonia.” The bacterium is particularly prevalent among school-aged children and young adults .
The P30 protein is one of the key surface proteins of Mycoplasma pneumoniae. It is associated with the bacterium’s terminal organelle, which plays a crucial role in its ability to adhere to host cells (cytadherence) and in gliding motility . The terminal organelle is a specialized structure that allows the bacterium to attach to the respiratory epithelium, facilitating colonization and infection .
Research has shown that the P30 protein is essential for the bacterium’s adherence to host cells. Mutants lacking the P30 protein exhibit significant defects in cytadherence, which impairs their ability to colonize the host . Additionally, the P30 protein is involved in the gliding motility of Mycoplasma pneumoniae, a unique form of movement that allows the bacterium to navigate the mucosal surfaces of the respiratory tract .
The recombinant P30 protein is a genetically engineered version of the native P30 protein. It is produced using recombinant DNA technology, which involves inserting the gene encoding the P30 protein into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities . This recombinant protein can be used for various research and diagnostic purposes.
The recombinant P30 protein is valuable in studying the pathogenesis of Mycoplasma pneumoniae infections. It allows researchers to investigate the specific functions of the P30 protein in cytadherence and motility, as well as its interactions with other proteins and host cell receptors . Additionally, the recombinant P30 protein can be used in serological assays to detect antibodies against Mycoplasma pneumoniae in patient samples, aiding in the diagnosis of infections .
