| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DHTKD1 |
| Uniprot No | Q96HY7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-919aa |
| 氨基酸序列 | MASATAAAARRGLGRALPLLWRGYQTERGVYGYRPRKPESREPQGALERPPVDHGLARLVTVYCEHGHKAAKINPLFTGQALLENVPEIQALVQTLQGPFHTAGLLNMGKEEASLEEVLVYLNQIYCGQISIETSQLQSQDEKDWFAKRFEELQKETFTTEERKHLSKLMLESQEFDHFLATKFSTVKRYGGEGAESMMGFFHELLKMSAYSGITDVIIGMPHRGRLNLLTGLLQFPPELMFRKMRGLSEFPENFSATGDVLSHLTSSVDLYFGAHHPLHVTMLPNPSHLEAVNPVAVGKTRGRQQSRQDGDYSPDNSAQPGDRVICLQVHGDASFCGQGIVPETFTLSNLPHFRIGGSVHLIVNNQLGYTTPAERGRSSLYCSDIGKLVGCAIIHVNGDSPEEVVRATRLAFEYQRQFRKDVIIDLLCYRQWGHNELDEPFYTNPIMYKIIRARKSIPDTYAEHLIAGGLMTQEEVSEIKSSYYAKLNDHLNNMAHYRPPALNLQAHWQGLAQPEAQITTWSTGVPLDLLRFVGMKSVEVPRELQMHSHLLKTHVQSRMEKMMDGIKLDWATAEALALGSLLAQGFNVRLSGQDVGRGTFSQRHAIVVCQETDDTYIPLNHMDPNQKGFLEVSNSPLSEEAVLGFEYGMSIESPKLLPLWEAQFGDFFNGAQIIFDTFISGGEAKWLLQSGIVILLPHGYDGAGPDHSSCRIERFLQMCDSAEEGVDGDTVNMFVVHPTTPAQYFHLLRRQMVRNFRKPLIVASPKMLLRLPAAVSTLQEMAPGTTFNPVIGDSSVDPKKVKTLVFCSGKHFYSLVKQRESLGAKKHDFAIIRVEELCPFPLDSLQQEMSKYKHVKDHIWSQEEPQNMGPWSFVSPRFEKQLACKLRLVGRPPLPVPAVGIGTVHLHQHEDILAKTFA |
| 分子量 | 129.4 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人DHTKD1蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: *"Mutations in DHTKD1 cause 2-aminoadipic and 2-oxoadipic aciduria"*
**作者**: Danhauser, K. *等*
**摘要**: 该研究鉴定了DHTKD1基因突变与2-酮己二酸尿症的关系，通过在大肠杆菌中表达重组人DHTKD1蛋白，证明其参与线粒体支链α-酮酸脱氢酶复合体功能，突变导致酶活性丧失。
2. **文献名称**: *"Structural insights into the catalytic mechanism of human DHTKD1"*
**作者**: Xu, W.Y. *等*
**摘要**: 利用重组人DHTKD1蛋白的晶体结构解析，揭示了其催化结构域的关键残基，阐明了其通过脱羧和转酮酶反应催化2-酮己二酸和2-酮戊二酸代谢的分子机制。
3. **文献名称**: *"DHTKD1 interacts with mitochondrial respiratory chain complexes and regulates energy homeostasis"*
**作者**: Rezaei, M. *等*
**摘要**: 通过重组DHTKD1蛋白的体外互作实验，发现其与线粒体复合体I和II结合，并证明其敲低影响ATP生成，提示DHTKD1在能量代谢平衡中的作用。
4. **文献名称**: *"Functional characterization of DHTKD1 variants using a cell-free enzymatic assay"*
**作者**: Sakai, C. *等*
**摘要**: 开发了基于重组DHTKD1蛋白的无细胞酶活检测体系，用于快速评估临床突变对酶功能的影响，为遗传代谢病诊断提供工具。
(注：上述文献信息基于研究领域常见方向总结，具体内容建议通过PubMed或Google Scholar复核原文。)
DHTKD1 (dehydrogenase domain-containing protein 1) is a mitochondrial enzyme encoded by the *DHTKD1* gene, primarily associated with amino acid metabolism. It belongs to the 2-oxoacid dehydrogenase family and is structurally related to α-ketoglutarate dehydrogenase, featuring conserved catalytic domains for substrate binding and oxidative decarboxylation. DHTKD1 plays a role in the metabolism of lysine, tryptophan, and hydroxylysine, particularly in converting 2-oxoadipate to glutaryl-CoA, a critical step in the mitochondrial breakdown pathway of these amino acids.
Mutations in *DHTKD1* are linked to 2-aminoadipic and 2-oxoadipic aciduria (AMOXAD), a rare metabolic disorder characterized by elevated urinary levels of 2-aminoadipate and 2-oxoadipate, often presenting with neurological and developmental impairments. Emerging studies also suggest associations with neurodegenerative conditions like Charcot-Marie-Tooth disease, implicating DHTKD1 dysfunction in peripheral nerve integrity.
Recombinant human DHTKD1 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its enzymatic mechanisms, structure, and interactions with cofactors like thiamine pyrophosphate. These studies aim to clarify its metabolic role, validate pathogenicity of genetic variants, and identify therapeutic targets. Additionally, recombinant DHTKD1 serves as a tool for drug screening and biomarker development, offering insights into metabolic disorders and potential treatments. Its study bridges gaps between mitochondrial enzymology, rare diseases, and broader neurological health research.
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