| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | srtA |
| Uniprot No | Q9S446 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-206aa |
| 氨基酸序列 | MHHHHHHKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKD KSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIA GHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGV LDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK |
| 预测分子量 | 27 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srtA(Sortase A)重组蛋白的3篇代表性文献及其摘要内容概括：
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1. **文献名称**：*Sortase-catalyzed protein anchoring in Gram-positive bacteria*
**作者**：Mazmanian, S. K., et al.
**摘要**：该研究首次鉴定了金黄色葡萄球菌中Sortase A(srtA)的酶活性，证明其通过识别LPXTG基序催化细胞壁蛋白的锚定过程，为后续蛋白工程应用奠定理论基础。
2. **文献名称**：*Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus*
**作者**：Ton-That, H., et al.
**摘要**：作者纯化并表征了重组srtA蛋白的转肽酶活性，揭示了其在切割LPXTG基序及介导蛋白交联中的关键作用，为体外酶活实验提供了方法学支持。
3. **文献名称**：*Sortase-mediated protein ligation for site-specific bioconjugation*
**作者**：Popp, M. W., & Ploegh, H. L.
**摘要**：本文开发了基于srtA的蛋白连接技术，利用其特异性识别LPXTG序列的特性，实现了体外高效、位点特异性的蛋白标记与偶联，拓展了其在生物医学工程中的应用。
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以上文献涵盖了srtA的功能机制、酶学性质及工程应用，可作为相关研究的重要参考。如需更多方向(如结构优化或药物开发)的文献，可进一步补充。
Sortase A (SrtA) is a calcium-dependent transpeptidase originally identified in *Staphylococcus aureus*, where it plays a critical role in anchoring surface proteins to the bacterial cell wall. This enzyme catalyzes a unique covalent bond-forming reaction by recognizing a conserved LPXTG motif in substrate proteins. SrtA cleaves the threonine-glycine (T-G) bond within this motif and links the carboxyl group of threonine to the amino group of pentaglycine cross-bridges in the cell wall, enabling surface protein display—a process vital for bacterial adhesion, immune evasion, and infection.
The recombinant form of SrtA (rSrtA) has been widely engineered for biotechnological applications due to its ability to perform site-specific ligation under mild conditions. Unlike traditional chemical conjugation methods, rSrtA enables precise, efficient, and biocompatible protein modifications, making it valuable in protein engineering, biomaterial functionalization, and therapeutic development. For example, rSrtA is employed to conjugate antibodies, peptides, or fluorescent tags to target molecules for diagnostics, drug delivery, or imaging.
Research on rSrtA has expanded to include engineered variants with enhanced catalytic activity, altered substrate specificity, or improved stability. These modifications address limitations of the wild-type enzyme, such as calcium dependency or slow kinetics, broadening its utility in synthetic biology and industrial processes. Additionally, rSrtA’s role in studying bacterial pathogenesis has fueled antimicrobial strategies targeting sortase-mediated pathways.
Overall, recombinant SrtA bridges microbiology and biotechnology, offering a versatile tool for covalent protein labeling, hybrid biomolecule assembly, and novel therapeutic design, while its study continues to inform both basic science and applied innovations.
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