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Recombinant Human ldh protein

  • 中文名: L-乳酸脱氢酶A链(ldh)重组蛋白
  • 别    名: ldh;Ldh-1;Ldh1;L-lactate dehydrogenase A chain
货号: PA2000-4615
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点ldh
Uniprot No P00338
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 2-332aa
氨基酸序列ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF
预测分子量 44.1 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.

参考文献

以下是关于LDH(乳酸脱氢酶)重组蛋白的3篇示例文献概述(虚构内容,供参考):

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1. **文献名称**:*High-yield expression and purification of recombinant human LDH-A in Escherichia coli*

**作者**:Zhang Y, et al.

**摘要**:研究报道了通过大肠杆菌表达系统高效制备人源LDH-A重组蛋白的优化策略,包括密码子优化、诱导条件调整及His标签亲和层析纯化,最终获得高纯度、高活性的LDH蛋白,适用于酶动力学研究。

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2. **文献名称**:*Functional characterization of a thermostable LDH from Geobacillus sp. for industrial biocatalysis*

**作者**:Lee S, Kim J.

**摘要**:从嗜热菌中克隆LDH基因,通过毕赤酵母系统表达重组酶,证明其高温(65°C)下的稳定性及催化乳酸盐合成的能力,为工业级生物催化反应提供了潜在工具酶。

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3. **文献名称**:*Development of a LDH-based colorimetric biosensor for rapid detection of lactate in serum*

**作者**:Wang H, et al.

**摘要**:利用重组LDH与纳米材料结合构建生物传感器,实现血清乳酸的快速定量检测,灵敏度达0.1 μM,在临床诊断和运动医学中具有应用潜力。

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如需真实文献,建议检索PubMed或Web of Science,关键词:*"recombinant LDH" + "expression" / "purification" / "application"*。

背景信息

Lactate dehydrogenase (LDH) is a crucial enzyme involved in anaerobic glycolysis, catalyzing the reversible conversion of pyruvate to lactate while regenerating NAD⁺. As a metabolic enzyme, it plays a central role in cellular energy production, particularly under low-oxygen conditions. Mammalian LDH exists as tetramers composed of two major isoforms, LDH-A (muscle/heart) and LDH-B (heart/liver), with tissue-specific expression patterns influencing metabolic adaptations. Dysregulation of LDH is associated with various pathologies, including cancer, neurodegenerative diseases, and hypoxia-related disorders, making it a biomarker and therapeutic target.

Recombinant LDH proteins are engineered through genetic cloning and heterologous expression systems like *E. coli*, yeast, or mammalian cell cultures. This technology enables scalable production of highly pure, sequence-controlled enzymes for research and industrial applications. Recombinant LDH is widely used to study enzyme kinetics, metabolic pathways, and disease mechanisms. In biotechnology, it serves as a biocatalyst in biosensors, biofuel production, and NADH recycling systems. Pharmaceutical applications include drug screening platforms targeting LDH in cancers, where elevated LDH-A correlates with aggressive tumor phenotypes and chemoresistance.

The development of recombinant LDH has overcome limitations of native enzyme purification, such as low yield and batch variability. Advanced protein engineering allows customization of stability, substrate specificity, or catalytic efficiency for specialized uses. For instance, thermostable LDH variants derived from extremophiles are utilized in industrial processes. Furthermore, recombinant LDH supports diagnostic kit standardization, ensuring consistency in clinical assays measuring LDH levels as indicators of tissue damage (e.g., myocardial infarction or liver disease). Ongoing research explores engineered LDH in synthetic biology and metabolic engineering, highlighting its versatility across disciplines.

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