| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADSL |
| Uniprot No | P30566 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-484aa |
| 氨基酸序列 | MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMAAGGDHGSPDSYR SPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQE MKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCY VGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQ LTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEG DDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHK ICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTL VMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVV YPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVV KQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEE VYPLLKPYESVMKVKAELCL |
| 预测分子量 | 59 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3篇关于ADSL(腺苷琥珀酸裂解酶)重组蛋白研究的参考文献示例(注：文献信息为模拟生成，仅供参考)：
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1. **文献名称**：*Expression and Purification of Recombinant Human Adenylosuccinate Lyase in Escherichia coli*
**作者**：Zhang, L., et al.
**摘要**：研究报道了人源ADSL在大肠杆菌中的重组表达与纯化策略，通过优化诱导条件获得可溶性蛋白，并利用亲和层析和凝胶过滤法纯化，验证了重组ADSL的酶活性，为后续功能研究提供基础。
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2. **文献名称**：*Crystal Structure of Adenylosuccinate Lyase from Bacillus subtilis Reveals Substrate Binding Mechanism*
**作者**：Tanaka, K., & Watanabe, T.
**摘要**：通过X射线晶体学解析枯草芽孢杆菌ADSL重组蛋白的三维结构，揭示了底物腺苷琥珀酸和富马酸的特异性结合位点，阐明了其催化机制及关键氨基酸残基的作用。
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3. **文献名称**：*Functional Characterization of ADSL Mutants Associated with Neurological Disorders Using Recombinant Protein Assays*
**作者**：Marquez, J., et al.
**摘要**：构建ADSL缺乏症相关突变体(如p.R303C)的重组蛋白，通过体外酶活实验证明突变导致催化效率显著下降，为疾病分子机制提供实验依据。
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**提示**：实际文献建议通过PubMed或Google Scholar检索关键词“ADSL recombinant protein”、“adenylosuccinate lyase expression”获取，并关注近年结构生物学或代谢疾病领域的相关研究。
ADSL (adenylosuccinate lyase) is a critical enzyme in the purine nucleotide biosynthesis pathway, catalyzing two distinct reactions: the cleavage of adenylosuccinate to AMP and fumarate, and the conversion of succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR). This bifunctional activity links the de novo synthesis of purines to the urea cycle and folate metabolism. Genetic mutations in the ADSL gene are associated with a rare autosomal recessive metabolic disorder termed ADSL deficiency, characterized by severe neurological impairments, epilepsy, and developmental delays. Studying ADSL's structure-function relationship is essential for understanding disease mechanisms and developing therapeutic strategies.
Recombinant ADSL protein production has become a cornerstone of biochemical and clinical research. Using expression systems like E. coli or yeast, researchers produce purified ADSL variants to analyze enzymatic activity, stability, and the impact of pathogenic mutations. These studies revealed that many disease-causing mutations disrupt substrate binding or protein folding rather than directly affecting catalytic residues. Recombinant ADSL also enables structural studies through X-ray crystallography and cryo-EM, providing insights into its homotetrameric architecture and substrate recognition mechanisms.
Therapeutically, recombinant ADSL serves as a potential enzyme replacement therapy candidate, though challenges like blood-brain barrier penetration persist. It additionally facilitates high-throughput drug screening for small molecules that could stabilize mutant enzymes or enhance residual activity. Beyond clinical applications, engineered ADSL variants are explored for industrial biotechnology, leveraging its fumarate-producing capability in biosynthetic pathways. Ongoing research focuses on optimizing recombinant ADSL production, improving catalytic efficiency, and deciphering its role in cellular nucleotide homeostasis, bridging fundamental biochemistry with translational medicine.
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