| 纯度 | >90%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | map |
| Uniprot No | P0AE18 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-264aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAISIKTPEDIEKMRVAGRLAAEVLEMIEP YVKPGVSTGELDRICNDYIVNEQHAVSACLGYHGYPKSVCISINEVVCHG IPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTIMGERLCRITQ ESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEE PQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSL SAQYEHTIVVTDNGCEILTLRKDDTIPAIISHDE |
| 预测分子量 | 32 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
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**Background of Recombinant MAP Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. MAP (Microorganism-Associated Proteins) recombinant proteins, specifically, are designed to mimic antigenic components of pathogens or host-derived molecules involved in immune responses. Their development stems from advancements in molecular cloning, expression systems, and protein purification techniques since the 1970s.
The concept hinges on inserting target gene sequences into vectors (e.g., plasmids), which are then introduced into host organisms like *E. coli*, yeast, or mammalian cells. These hosts act as "factories" to produce the desired protein. For MAP proteins, this often involves expressing pathogen-derived antigens (e.g., viral surface proteins or bacterial toxins) in a controlled, scalable manner. This approach bypasses the need to culture dangerous pathogens, enhancing safety and reproducibility.
MAP recombinant proteins are pivotal in vaccine development. For instance, hepatitis B vaccines utilize recombinant hepatitis B surface antigen (HBsAg) produced in yeast. Similarly, HPV vaccines employ recombinant capsid proteins to elicit protective immunity. Beyond vaccines, they serve as diagnostic tools (e.g., ELISA antigens) and therapeutic agents, such as cytokine therapies or monoclonal antibodies.
Challenges persist, including ensuring proper protein folding, post-translational modifications (e.g., glycosylation), and scalability. Eukaryotic systems (e.g., CHO cells) are often preferred for complex proteins, while prokaryotic systems (e.g., *E. coli*) offer cost-effective solutions for simpler structures. Innovations like codon optimization and fusion tags have further improved yield and functionality.
Overall, recombinant MAP proteins exemplify the synergy between genetic engineering and immunology, enabling safer, targeted interventions against infectious diseases, cancers, and autoimmune disorders. Their continued refinement underscores their centrality in modern medicine.
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