| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HIBADH |
| Uniprot No | P31937 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-336aa |
| 氨基酸序列 | ASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGTTLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSKKDFSSVFQFLREEETF |
| 预测分子量 | 39.0 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HIBADH重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Expression, purification, and characterization of recombinant human 3-hydroxyisobutyrate dehydrogenase"*
**作者**：Loupatty FJ. et al.
**摘要内容**：报道了人源HIBADH在大肠杆菌中的重组表达与纯化，分析了其酶动力学特性及对底物3-羟基异丁酸的特异性，为研究支链氨基酸代谢缺陷提供了工具。
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2. **文献名称**：*"Structural insights into the catalytic mechanism of 3-hydroxyisobutyrate dehydrogenase"*
**作者**：Shinahara A. et al.
**摘要内容**：通过重组HIBADH蛋白的晶体结构解析，揭示了其底物结合位点及催化机制，发现NAD+依赖性氧化还原反应的关键残基，为酶功能改造奠定基础。
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3. **文献名称**：*"HIBADH silencing induces mitochondrial dysfunction via AMPK/FOXO1 signaling in hepatocellular carcinoma"*
**作者**：Wang Y. et al.
**摘要内容**：利用重组HIBADH蛋白进行功能验证实验，发现其表达缺失通过调控AMPK/FOXO1通路影响肝癌细胞线粒体代谢，提示HIBADH在肿瘤能量代谢中的潜在作用。
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注：以上文献信息为示例性内容，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。若需具体文献DOI或发表年份，可补充说明。
**Background of HIBADH Recombinant Protein**
HIBADH (β-hydroxyisobutyryl-CoA hydrolase/dehydrogenase) is a mitochondrial enzyme critical in the catabolism of branched-chain amino acids (BCAAs), particularly valine. It catalyzes the hydrolysis of β-hydroxyisobutyryl-CoA (HIB-CoA) to free CoA and β-hydroxyisobutyrate, a key step in the metabolic pathway converting valine into succinyl-CoA for entry into the tricarboxylic acid (TCA) cycle. This process is essential for energy production and intermediary metabolism.
HIBADH dysfunction has been linked to metabolic disorders, including HIBADH deficiency, which manifests as elevated urinary β-hydroxyisobutyryl-carnitine and developmental delays. Studying HIBADH’s structure and function is vital for understanding its role in metabolic health and disease.
Recombinant HIBADH protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells*) to enable large-scale purification and functional studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate substrate specificity, kinetic properties, and interactions with potential inhibitors or activators. Structural analyses, such as X-ray crystallography, have revealed details about its active site and conformational dynamics, aiding in drug discovery efforts.
Additionally, HIBADH has garnered interest in biotechnology for its potential in synthesizing chiral intermediates for pharmaceuticals. Its ability to process CoA derivatives makes it a candidate for engineering novel biocatalysts.
Research on recombinant HIBADH continues to advance our understanding of BCAA metabolism, mitochondrial disorders, and therapeutic strategies. Its applications span basic biochemistry, clinical diagnostics, and industrial enzymology, underscoring its multifaceted significance in science and medicine.
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