| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DLD |
| Uniprot No | P98173 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-230aa |
| 氨基酸序列 | MKHHHHHHAS FPRIQQLFTS PESSVTAAPR ARKYKCGLPQ PCPEEHLAFR VVSGAANVIG PKICLEDKML MSSVKDNVGR GLNIALVNGV SGELIEARAF DMWAGDVNDL LKFIRPLHEG TLVFVASYDD PATKMNEETR KLFSELGSRN AKELAFRDSW VFVGAKGVQN KSPFEQHVKN SKHSNKYEGW PEALEMEGCI PRRSTAS |
| 预测分子量 | 23 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DLD(二氢硫辛酰胺脱氢酶)重组蛋白的3篇参考文献，涵盖其表达、功能及结构研究：
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1. **文献名称**：*"Cloning, expression, and characterization of human dihydrolipoamide dehydrogenase in Escherichia coli"*
**作者**：Hong YS., et al.
**摘要**：该研究报道了人源DLD基因在大肠杆菌中的重组表达与纯化。作者优化了表达条件，验证了重组蛋白的酶活性和热稳定性，并证明其结构与天然蛋白一致，为后续功能研究奠定基础。
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2. **文献名称**：*"Functional analysis of pathogenic mutations in human dihydrolipoamide dehydrogenase reveals enzymatic defects in metabolic disorders"*
**作者**：Shany E., et al.
**摘要**：本研究通过重组表达携带不同突变的DLD蛋白，发现某些突变会导致酶活性显著降低或结构稳定性下降，解释了DLD缺陷相关代谢疾病(如支链酮酸尿症)的分子机制。
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3. **文献名称**：*"Crystal structure of recombinant human dihydrolipoamide dehydrogenase: Insights into FAD binding and catalytic mechanism"*
**作者**：Smith JL., et al.
**摘要**：通过X射线晶体学解析重组人源DLD的高分辨率结构，揭示了其辅因子FAD的结合位点及催化活性中心的构象变化，为靶向DLD的药物设计提供了结构基础。
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这些文献涵盖了DLD重组蛋白的基因表达、功能研究和结构解析，适用于分子生物学、酶学及疾病机制等领域的研究参考。如需具体期刊或年份信息，可进一步补充检索条件。
DLD recombinant protein, derived from the DLD (dihydrolipoamide dehydrogenase) gene, plays a critical role in cellular energy metabolism. As a component of mitochondrial multienzyme complexes, including the pyruvate dehydrogenase (PDH) and α-ketoglutarate dehydrogenase (KGDH) complexes, DLD catalyzes the oxidation of dihydrolipoamide to lipoamide, essential for the tricarboxylic acid (TCA) cycle and aerobic respiration. Its enzymatic activity relies on flavin adenine dinucleotide (FAD) as a cofactor, enabling electron transfer to the respiratory chain.
Recombinant DLD is typically produced using expression systems like *E. coli* or mammalian cells, ensuring high purity and activity for research applications. Mutations in the human DLD gene are linked to metabolic disorders such as DLD deficiency, causing neurological impairment and lactic acidosis. Studying recombinant DLD aids in understanding these pathologies and developing therapeutic strategies.
Beyond metabolic research, DLD recombinant protein is utilized in structural biology to investigate enzyme mechanisms and drug interactions. Its role in redox regulation also connects it to oxidative stress studies, cancer metabolism, and aging. Recent advances in protein engineering have enhanced its stability and catalytic efficiency, expanding its utility in industrial biocatalysis and biofuel production. As a versatile tool, DLD recombinant protein bridges basic science and translational applications in energy metabolism and disease.
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