| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HADH |
| Uniprot No | Q16836 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 13-314aa |
| 氨基酸序列 | SSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERGDAS KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFIVDGWHEM DAENPLHQPS PSLNKLVAEN KFGKKTGEGF YKYK |
| 预测分子量 | 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3篇关于HADH重组蛋白的参考文献示例(注：文献信息为模拟生成，仅供参考)：
1. **文献名称**：Recombinant Human HADH: Expression, Purification, and Enzymatic Characterization
**作者**：Smith J, et al.
**摘要**：报道了人源HADH基因在大肠杆菌中的重组表达及纯化方法，证实重组蛋白具有羟基酰基-CoA脱氢酶活性，并优化了其反应最适pH和温度条件。
2. **文献名称**：Structural Insights into HADH Deficiency-Related Mutations via Recombinant Protein Analysis
**作者**：Wang L, et al.
**摘要**：通过重组表达携带致病突变体的HADH蛋白，结合晶体结构解析，揭示了突变导致酶活性丧失的分子机制，为遗传性HADH缺乏症提供理论依据。
3. **文献名称**：Recombinant HADH Assay Development for Neonatal Hypoglycemia Screening
**作者**：Chen X, et al.
**摘要**：开发了基于重组HADH蛋白的比色检测方法，用于新生儿低血糖症中脂肪酸氧化障碍的快速筛查，验证了其临床检测灵敏度和特异性。
4. **文献名称**：Functional Rescue of HADH Knockout Mice by Recombinant Protein Therapy
**作者**：Kimura T, et al.
**摘要**：在HADH基因敲除小鼠模型中，通过静脉注射重组HADH蛋白成功缓解了脂肪酸代谢异常，证明了蛋白质替代治疗的潜在应用价值。
**Background of HADH Recombinant Protein**
HADH (Hydroxyacyl-CoA Dehydrogenase), also known as 3-hydroxyacyl-CoA dehydrogenase, is a mitochondrial enzyme critical in fatty acid β-oxidation. It catalyzes the oxidation of medium- and short-chain 3-hydroxyacyl-CoAs to 3-ketoacyl-CoAs, coupled with NAD⁺ reduction to NADH, thereby contributing to cellular energy production. This enzyme is particularly active in tissues with high metabolic demands, such as the liver, heart, and skeletal muscle.
The recombinant HADH protein is produced using biotechnological methods, typically through heterologous expression in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems. Recombinant technology allows for high-purity, scalable production of the enzyme, enabling research into its structural and functional properties. For instance, studies employ recombinant HADH to investigate substrate specificity, catalytic mechanisms, and interactions with other β-oxidation enzymes.
Clinically, HADH deficiency is linked to inherited metabolic disorders, such as hyperinsulinemic hypoglycemia and myopathy, characterized by impaired fatty acid oxidation. Recombinant HADH serves as a vital tool for developing diagnostic assays and screening for mutations in the *HADH* gene. Additionally, it aids in exploring therapeutic strategies, including enzyme replacement or small-molecule modulators.
Recent structural analyses using recombinant HADH have revealed insights into its dimeric conformation and active-site architecture, informing drug design. Beyond disease research, the enzyme’s role in lipid metabolism has implications for understanding obesity, diabetes, and cardiovascular diseases.
In summary, recombinant HADH protein bridges basic biochemical research and clinical applications, offering a versatile platform to dissect metabolic pathways, model diseases, and innovate diagnostics or therapies.
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