| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPRS |
| Uniprot No | P07814 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1512aa |
| 氨基酸序列 | MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKDYKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY |
| 预测分子量 | 170,5 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EPRS重组蛋白的3篇参考文献及其摘要内容概括：
1. **文献名称**：*Structural and Functional Analysis of Human Bifunctional EPRS*
**作者**：Jia J. et al.
**摘要**：本研究通过重组表达人源EPRS蛋白，解析其晶体结构，揭示了其双功能结构域(谷氨酰和脯氨酰-tRNA合成酶活性)的协同机制，并验证了其在小分子抑制剂结合中的构象变化。
2. **文献名称**：*EPRS-Dependent Inflammatory Signaling in Macrophages*
**作者**：Kim S.H. et al.
**摘要**：利用重组EPRS蛋白，作者发现其非经典功能——通过激活NF-κB通路调控炎症因子分泌，为治疗自身免疫疾病提供了新靶点。
3. **文献名称**：*Recombinant EPRS as a Therapeutic Agent in Fibrosis Models*
**作者**：Lee Y. et al.
**摘要**：该研究通过大肠杆菌系统表达功能性重组人EPRS，证明其通过抑制TGF-β信号通路减轻小鼠肝纤维化，展示了其潜在治疗应用。
注：以上文献为示例性质，实际引用时需核实具体论文信息。
**Background of EPRS Recombinant Protein**
Eukaryotic Prolyl-tRNA Synthetase (EPRS), a member of the aminoacyl-tRNA synthetase (ARS) family, is a bifunctional enzyme that catalyzes the attachment of specific amino acids (proline and glutamic acid in some organisms) to their cognate tRNAs during protein synthesis. Unlike most ARSs, which are monofunctional, EPRS in higher eukaryotes evolved through gene fusion, combining glutamyl-prolyl-tRNA synthetase activities into a single polypeptide. This unique structure comprises N-terminal glutamyl-tRNA synthetase (ERS) and C-terminal prolyl-tRNA synthetase (PRS) domains, linked by a non-catalytic linker region.
Beyond its canonical role in translation, EPRS has gained attention for its "moonlighting" functions in non-translational pathways. It acts as a key regulator in inflammation, interferon-γ-mediated signaling, and cellular stress responses. For instance, EPRS is phosphorylated under stress, releasing it from the multi-tRNA synthetase complex (MSC) to interact with other proteins, modulating mRNA translation or immune responses.
Recombinant EPRS proteins are engineered using expression systems (e.g., *E. coli*, insect, or mammalian cells*) to produce purified, functional enzymes for structural and functional studies. These proteins enable researchers to dissect EPRS's dual enzymatic roles, its structural dynamics, and interactions with binding partners. Recombinant technology also facilitates the exploration of EPRS as a therapeutic target, particularly in autoimmune diseases and cancers, where its aberrant expression or activity is implicated.
Recent studies highlight EPRS's involvement in pathological angiogenesis and viral replication, broadening its biomedical relevance. The development of EPRS inhibitors or modulators, aided by recombinant protein platforms, represents a promising frontier in drug discovery. Overall, EPRS recombinant proteins serve as critical tools to unravel the multifunctional nature of this enzyme and its potential applications in medicine.
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