| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLUD1 |
| Uniprot No | P00367 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 54-558aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGKHGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY NEAGVTFTEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY NEAGVTFT |
| 预测分子量 | 58 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GLUD1重组蛋白的参考文献示例(注：文献为模拟示例，实际引用需核实具体来源)：
1. **文献名称**：*"Expression and purification of recombinant human GLUD1 in Escherichia coli: kinetic characterization and regulatory properties"*
**作者**：Smith A, et al.
**摘要**：报道了人源GLUD1在大肠杆菌中的重组表达与纯化，分析了其酶动力学特性及变构调节机制，揭示了ATP和亮氨酸对酶活性的调控作用。
2. **文献名称**：*"Crystal structure of glutamate dehydrogenase 1 (GLUD1) reveals insights into hyperinsulinism/hyperammonemia-associated mutations"*
**作者**：Johnson R, et al.
**摘要**：通过X射线晶体学解析了GLUD1的三维结构，结合重组蛋白功能实验，阐明了致病突变如何破坏酶活性并导致高胰岛素血症/高血氨综合征。
3. **文献名称**：*"Functional analysis of GLUD1 mutants using recombinant protein models: implications for neurological disorders"*
**作者**：Lee S, et al.
**摘要**：利用重组GLUD1突变体蛋白，研究其酶活性和热稳定性变化，发现特定突变与神经退行性疾病的相关性，为靶向治疗提供依据。
4. **文献名称**：*"Development of a high-throughput assay for GLUD1 activity using recombinant protein and its application in drug screening"*
**作者**：Zhang Y, et al.
**摘要**：基于重组GLUD1蛋白建立了高通量活性检测体系，成功筛选出小分子抑制剂，为代谢性疾病药物开发提供新工具。
如需实际文献，建议通过PubMed或Web of Science搜索关键词“GLUD1 recombinant expression”或“GLUD1 structure-function”获取最新研究。
**Background of GLUD1 Recombinant Protein**
Glutamate dehydrogenase 1 (GLUD1) is a mitochondrial enzyme central to amino acid and energy metabolism, catalyzing the reversible oxidative deamination of glutamate to α-ketoglutarate while reducing NAD⁺ to NADH. This reaction links carbon and nitrogen metabolism, impacting the tricarboxylic acid (TCA) cycle, ammonia detoxification, and neurotransmitter synthesis. GLUD1 is highly expressed in tissues with active metabolic demands, such as the liver, pancreas, brain, and kidney, and its activity is regulated by allosteric effectors (e.g., GTP, ADP) and post-translational modifications.
Dysregulation of GLUD1 is implicated in metabolic disorders, hyperinsulinism-hyperammonemia syndrome (HI/HA), and neurodegenerative diseases. Gain-of-function mutations in GLUD1. for instance, cause HI/HA by disrupting insulin secretion and ammonia homeostasis. Conversely, reduced GLUD1 activity is observed in hepatic encephalopathy and certain cancers, highlighting its dual role in health and disease.
Recombinant GLUD1 protein, produced via heterologous expression systems (e.g., E. coli, mammalian cells), serves as a critical tool for studying enzyme kinetics, structural biology, and disease mechanisms. Its production typically involves cloning the GLUD1 gene into expression vectors, optimizing conditions for solubility and activity, and purifying the protein using affinity chromatography. Recombinant GLUD1 enables high-throughput screening for modulators, aiding drug discovery for metabolic and neurological disorders. Additionally, it is used in diagnostic assays to detect GLUD1 autoantibodies linked to autoimmune conditions.
Research leveraging recombinant GLUD1 has advanced understanding of its regulatory networks, substrate specificity, and pathological variants, offering insights into therapeutic targeting and biomarker development. Its applications span biochemistry, clinical diagnostics, and precision medicine, underscoring its versatility in both basic and translational research.
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