| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | proA |
| Uniprot No | P07004 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-417aa |
| 氨基酸序列 | MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSEIILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQVCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALKSCGLPAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESVEIAEALKVIVNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLQAGPAKVVAVKAEEYDDEFLSLDLNVKIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYKWIGIGDYTIRA |
| 预测分子量 | 48.7 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. |
以下是关于proA重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Cloning and Expression of Protein A in Escherichia coli"*
**作者**：Hjelm, H., et al.
**摘要**：该研究报道了通过基因工程技术将金黄色葡萄球菌的Protein A基因克隆至大肠杆菌表达系统，成功实现了重组Protein A的高效表达，并验证了其与IgG Fc段的特异性结合能力，为规模化生产提供了基础方案。
2. **文献名称**：*"Structural and Functional Analysis of Recombinant Protein A in Antibody Purification"*
**作者**：Akerström, B., & Björck, L.
**摘要**：作者系统研究了重组Protein A的结构域功能及其在抗体纯化中的应用，发现其不同结构域对IgG亚型的结合亲和力存在差异，并提出了优化层析条件的策略以提高纯化效率。
3. **文献名称**：*"Engineering Alkali-Stable Protein A Mimetics for Industrial-Scale Antibody Purification"*
**作者**：Hober, S., et al.
**摘要**：本研究通过蛋白质工程改造重组Protein A，增强了其在强碱性条件下的稳定性，解决了传统Protein A在工业纯化中易变性的问题，显著降低了抗体生产的成本。
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以上文献涵盖重组Protein A的克隆表达、功能优化及工业应用，适用于抗体纯化领域的研究参考。如需具体文献来源，建议通过PubMed或Google Scholar按标题及作者检索全文。
ProA, or Protein A, is a well-characterized bacterial cell wall protein originally isolated from *Staphylococcus aureus*. It gained prominence due to its high affinity for the Fc region of immunoglobulin G (IgG), enabling it to bind antibodies with remarkable specificity. This unique property has made it an indispensable tool in immunology and biotechnology, particularly in antibody purification. Native Protein A, however, has limitations, including immunogenicity and instability under harsh conditions, prompting the development of recombinant versions.
Recombinant Protein A (proA) is engineered using genetic modification techniques to optimize its functionality and compatibility with industrial processes. By expressing the gene in heterologous hosts like *E. coli* or mammalian cells, researchers produce a purified, consistent product devoid of native bacterial contaminants. The recombinant form retains the critical IgG-binding domains—typically five homologous regions—while allowing modifications to enhance stability, reduce immunogenicity, or adjust binding specificity. For instance, alkali-tolerant mutants have been developed to withstand cleaning-in-place (CIP) procedures in biomanufacturing.
In biopharmaceutical applications, proA is widely used in affinity chromatography columns to capture monoclonal antibodies (mAbs) during downstream processing. Its role in ensuring high-purity antibody yields has solidified its importance in therapeutic protein production. Beyond purification, proA is utilized in diagnostic assays, immunoprecipitation, and antibody detection due to its reliable interaction with IgG.
Recent advancements focus on engineering fusion proteins or ligand mimics to address cost and scalability challenges. Despite alternatives like Protein G or synthetic ligands, proA remains a gold standard owing to its balance of binding efficiency and ease of use. Ongoing research explores its potential in novel therapeutic platforms, underscoring its enduring relevance in biomedical sciences.
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