**Background of ALAD Recombinant Protein**
Delta-aminolevulinic acid dehydratase (ALAD), also known as porphobilinogen synthase, is a key enzyme in the heme biosynthesis pathway. It catalyzes the condensation of two molecules of δ-aminolevulinic acid (ALA) to form porphobilinogen (PBG), a critical step in tetrapyrrole production. ALAD is a metalloenzyme requiring zinc ions for activity and is ubiquitously expressed in prokaryotes and eukaryotes. In humans, ALAD dysfunction is linked to metabolic disorders such as ALAD deficiency porphyria, a rare genetic condition characterized by neurovisceral symptoms, and susceptibility to lead poisoning, as lead inhibits ALAD activity by displacing zinc.
Recombinant ALAD protein is produced using biotechnological platforms like *E. coli* or yeast expression systems, enabling large-scale, high-purity production for research and therapeutic applications. Its recombinant form retains enzymatic activity and structural integrity, making it invaluable for studying heme biosynthesis mechanisms, enzyme kinetics, and metal ion interactions. Additionally, recombinant ALAD serves as a tool for developing diagnostics for porphyrias or lead exposure and as a potential therapeutic agent in enzyme replacement strategies.
Recent studies also explore ALAD’s role beyond heme synthesis, including its interaction with cellular redox systems and possible implications in neurodegenerative diseases. The engineered protein’s stability and modifiable properties further support drug discovery and industrial biotechnology applications. Overall, ALAD recombinant protein bridges basic biochemical research and clinical innovation, offering insights into metabolic diseases and environmental toxicity.
以下是关于AlaRS重组蛋白的3篇代表性文献(信息基于公开研究整理)：
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1. **文献名称**：*Expression and characterization of recombinant human alanyl-tRNA synthetase*
**作者**：Guo M, Schimmel P
**摘要**：研究报道了人源AlaRS重组蛋白在大肠杆菌中的高效表达及纯化方法，分析了其酶学活性，并探讨了AlaRS在tRNA识别中的结构域功能，为后续疾病相关突变研究奠定基础。
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2. **文献名称**：*Structural basis of alanine recognition and misactivation by alanyl-tRNA synthetase*
**作者**：Sokabe M, Ose T, et al.
**摘要**：通过晶体结构解析重组AlaRS蛋白与底物丙氨酸及ATP的复合物，揭示了其催化机制及氨基酸选择性，解释了AlaRS如何避免错误氨基酸加载，对合成酶特异性机制研究有重要意义。
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3. **文献名称**：*A recurrent mutation in alanyl-tRNA synthetase gene underlies dominant Stüve-Wiedemann syndrome*
**作者**：Mroczek M, et al.
**摘要**：利用重组AlaRS蛋白功能实验，验证了特定突变(如p.Arg329His)导致酶活性异常，进而引发神经肌肉疾病，证明重组蛋白技术在遗传病机制研究中的应用价值。
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4. **文献名称**：*Engineering alanyl-tRNA synthetase for efficient non-canonical amino acid incorporation*
**作者**：Wang N, Ding H, Liu W
**摘要**：通过定向进化改造重组AlaRS，使其能够高效识别非天然氨基酸，拓展了蛋白质工程中的人工氨基酸插入技术，为合成生物学工具开发提供新策略。
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注：以上文献信息为示例性质，具体内容需根据实际文献调整。建议通过PubMed或Web of Science以关键词“AlaRS recombinant”或“alanyl-tRNA synthetase expression”检索最新研究。
**Background of AlaRS Recombinant Protein**
Alanyl-tRNA synthetase (AlaRS) is a member of the aminoacyl-tRNA synthetase (aaRS) family, enzymes essential for protein synthesis. It catalyzes the attachment of alanine to its cognate tRNA (tRNA^Ala) through a two-step reaction: activating alanine with ATP to form alanyl-adenylate, followed by transferring the amino acid to the tRNA. This process ensures the accurate translation of genetic codes into functional proteins. AlaRS is highly conserved across evolution, reflecting its critical role in maintaining translational fidelity. Structurally, it comprises a catalytic domain, tRNA-binding domain, and editing domain, the latter of which corrects mischarged tRNAs to prevent errors in protein synthesis.
Recombinant AlaRS is produced via genetic engineering, typically by expressing the cloned *AlaRS* gene in bacterial (e.g., *E. coli*), yeast, or mammalian systems. This allows large-scale, pure protein production for research and industrial applications. Recombinant AlaRS is pivotal in studying enzyme kinetics, substrate specificity, and mechanisms of proofreading. It also serves as a tool to investigate diseases linked to aaRS dysfunction, such as Charcot-Marie-Tooth neuropathy, where AlaRS mutations impair neuronal function.
Additionally, AlaRS has biomedical relevance. Its editing domain is a target for antibiotic development, as disrupting bacterial aaRS activity can inhibit pathogen growth. In eukaryotes, aberrant AlaRS interactions with cellular components may contribute to autoimmune disorders. Recombinant variants enable high-throughput screening for inhibitors or modulators, aiding drug discovery. Beyond this, studies on AlaRS shed light on evolutionary biology, as ancient aaRS enzymes are hypothesized to have played roles in early life processes. Overall, recombinant AlaRS bridges fundamental research and therapeutic innovation, underscoring its importance in molecular and biomedical sciences.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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