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Recombinant Human OGDH protein

  • 中文名: 酮戊二酸脱氢酶(OGDH)重组蛋白
  • 别    名: OGDH;2-oxoglutarate dehydrogenase complex component E1
货号: PA1000-9134
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点OGDH
Uniprot No Q02218
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间41-427aa
氨基酸序列SAPVAAEPFLSGTSSNYVEEMYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDESDLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFETPGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSENGVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINRVTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVRPRERRARQIVKAPCSSMEFRSPT
预测分子量59.1kDa
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.

参考文献

以下是关于OGDH重组蛋白的3篇参考文献示例(注:以下文献为虚构示例,仅用于演示格式):

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1. **标题**:High-Yield Expression and Functional Analysis of Recombinant Human OGDH in a Bacterial System

**作者**:Chen X, Li R, Park H.

**摘要**:本研究报道了在大肠杆菌中高效表达人源OGDH重组蛋白的优化策略,通过亲和层析和尺寸排阻色谱纯化获得高纯度蛋白。酶活实验证实重组OGDH具有与天然酶相似的催化活性,适用于体外代谢研究。

2. **标题**:Crystallographic Study of the OGDH Complex: Implications for Substrate Binding and Disease Mutations

**作者**:Müller T, Schmidt A, Yamamoto M.

**摘要**:利用重组表达的人源OGDH复合体进行X射线晶体结构解析,揭示了其底物结合口袋的关键构象变化,并分析了与遗传性神经疾病相关的突变位点对酶活性的影响。

3. **标题**:Recombinant OGDH Ameliorates Mitochondrial Dysfunction in a Cellular Model of Leigh Syndrome

**作者**:Gomez S, Patel K, Kim D.

**摘要**:在Leigh综合征细胞模型中,外源性重组OGDH蛋白通过恢复线粒体酮戊二酸代谢,显著改善ATP生成和氧化应激,提示其潜在治疗价值。

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**说明**:以上文献为示例,实际文献需通过PubMed、Google Scholar等平台检索(关键词:*OGDH recombinant protein*)。真实文献可能包括:

- 重组OGDH的表达优化(如使用昆虫细胞/哺乳动物系统)、

- 酶动力学或结构生物学研究、

- 在代谢疾病或癌症中的功能探索等方向。

背景信息

OGDH (Oxoglutarate Dehydrogenase) is a critical mitochondrial enzyme complex that plays a central role in the tricarboxylic acid (TCA) cycle, a fundamental metabolic pathway for cellular energy production. As a component of the α-ketoglutarate dehydrogenase complex (KGDHC), OGDH catalyzes the oxidative decarboxylation of α-ketoglutarate to succinyl-CoA, linking carbon metabolism with NADH generation and ATP synthesis. Dysregulation of OGDH activity has been implicated in various pathological conditions, including neurodegenerative diseases (e.g., Alzheimer's and Parkinson's), metabolic disorders, and cancer, making it a significant target for biomedical research.

Recombinant OGDH proteins are engineered through molecular cloning techniques, typically expressed in prokaryotic (e.g., E. coli) or eukaryotic systems (e.g., mammalian or insect cells) to ensure proper folding and post-translational modifications. These recombinant versions retain enzymatic activity while offering advantages such as high purity, scalability, and reduced batch-to-batch variability compared to native isoforms isolated from tissues. Researchers employ OGDH recombinant proteins to investigate enzyme kinetics, substrate specificity, and inhibitor screening, particularly for developing therapeutic agents targeting mitochondrial dysfunction. Structural studies using recombinant OGDH have also advanced understanding of its catalytic mechanism and interaction with cofactors like thiamine pyrophosphate (TPP) and lipoic acid.

Recent applications extend to disease modeling and drug discovery platforms, where recombinant OGDH helps elucidate metabolic reprogramming in cancer cells or neuronal energy deficits. However, challenges persist in maintaining the enzyme's stability during purification and replicating its native multi-subunit complex structure. Ongoing efforts focus on optimizing expression systems and cryopreservation techniques to enhance functional integrity for both basic research and clinical translation.

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