| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 1/50-1/200 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | Diaphorase; Dihydrolipoamide dehydrogenase; DLDD; DLDH; GCSL; LAD; lipoamide dehydrogenase; Lipoamide reductase; Lipoyl dehydrogenase; PHE3 |
| Entrez GeneID | 1738 |
| WB Predicted band size | Calculated MW: 54 kDa; Observed MW: 54 kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Mouse,Rat |
| Immunogen | A synthetic peptide of human Lipoamide Dehydrogenase |
| Formulation | Purified antibody in TBS with 0.05% sodium azide,0.05%BSA and 50% glycerol. |
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以下是3篇关于Lipoamide Dehydrogenase(LAD/DLD)抗体的相关文献概览：
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1. **文献名称**：*Antibody-based profiling of mitochondrial enzymes in human skeletal muscle*
**作者**：Smith J, et al.
**摘要**：该研究开发了特异性识别人类骨骼肌线粒体Lipoamide Dehydrogenase的单克隆抗体，验证了其在Western blot和免疫组织化学中的应用，成功检测到线粒体复合物中DLD蛋白的表达水平变化，为代谢疾病研究提供工具。
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2. **文献名称**：*Dihydrolipoamide dehydrogenase deficiency: a novel mutation and antibody-based diagnostic approach*
**作者**：Lee S, et al.
**摘要**：通过构建针对DLD C端结构域的多克隆抗体，建立了ELISA检测方法，用于快速筛查DLD缺乏症患者血液样本，发现与神经退行性病变相关的突变位点，推动遗传代谢病诊断技术发展。
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3. **文献名称**：*Targeting redox vulnerability in cancer cells via Lipoamide Dehydrogenase inhibition*
**作者**：Zhang Y, et al.
**摘要**：利用商业化兔源抗LAD抗体(货号ab12345)，研究团队验证了DLD在肺癌细胞中的高表达，并通过抗体介导的功能抑制实验，证明抑制DLD可增强癌细胞对氧化应激的敏感性，提出其作为抗癌靶点的潜力。
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4. **文献名称**：*Cross-species reactivity of anti-LAD antibodies in zebrafish models*
**作者**：Garcia R, et al.
**摘要**：评估了多种哺乳动物来源的LAD抗体在斑马鱼胚胎中的交叉反应性，发现某克隆号抗体可特异性识别斑马鱼DLD同源蛋白，为利用该模式生物研究线粒体功能障碍机制提供实验依据。
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注：以上文献为虚拟示例，实际引用时需检索PubMed等数据库获取真实文献(可尝试关键词：LAD antibody, DLD antibody, dihydrolipoamide dehydrogenase antibody)。如需近期文献，建议筛选2020年后发表的抗体应用类研究。
Lipoamide dehydrogenase (LDH), also known as dihydrolipoamide dehydrogenase, is a mitochondrial flavoenzyme critical in energy metabolism. It serves as the E3 component of multienzyme complexes like pyruvate dehydrogenase and α-ketoglutarate dehydrogenase, catalyzing the oxidation of dihydrolipoamide to lipoamide while transferring electrons to NAD⁺, generating NADH. LDH is essential for glucose homeostasis, amino acid metabolism, and the tricarboxylic acid (TCA) cycle. Structurally, it forms a homodimer with FAD-binding domains and redox-active disulfide bonds.
Antibodies targeting LDH are widely used in research to study its expression, localization, and function in metabolic pathways. These tools enable detection via Western blotting, immunohistochemistry, and immunofluorescence, aiding investigations into diseases linked to LDH dysfunction, such as mitochondrial disorders, neurodegenerative diseases (e.g., Alzheimer’s and Parkinson’s), diabetes, and cancer. Mutations in the *LDH* gene can cause E3 deficiency, a rare metabolic disorder characterized by neurological impairment and lactic acidosis.
LDH antibodies are also employed to explore redox regulation and oxidative stress mechanisms, as the enzyme plays a dual role in antioxidant defense and reactive oxygen species (ROS) production. Validation of antibody specificity is crucial, often confirmed using knockout models or siRNA knockdown. Commercial antibodies vary in clonality (monoclonal/polyclonal) and host species, with applications spanning basic research, diagnostics, and therapeutic development targeting metabolic dysregulation.
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