| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALDH5A1 |
| Uniprot No | P51649 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 48-535aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAGRLAGLSAALLRTDSFVGGRWLPAAATF PVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRK WYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYG DIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVV VKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPL VSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVA GAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEE GTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLC NVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA QIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLE LKYVCYGGL |
| 预测分子量 | 55 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ALDH5A1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 and Characterization of Recombinant Human Succinic Semialdehyde Dehydrogenase (ALDH5A1)*
**作者**：Schwartz, E. I., & Johnson, J. L.
**摘要**：该研究在大肠杆菌中成功表达并纯化了重组人源ALDH5A1蛋白，验证了其催化琥珀酸半醛(SSA)转化为琥珀酸的酶活性，并优化了反应条件，为后续酶学研究和疾病模型奠定基础。
2. **文献名称**：*Kinetic Analysis of ALDH5A1 Mutants Associated with SSADH Deficiency*
**作者**：Kim, G. H., et al.
**摘要**：通过定点突变构建ALDH5A1的致病突变体，发现某些突变导致酶活显著降低或底物结合能力受损，揭示了琥珀酸半醛脱氢酶缺乏症(SSADHD)的分子机制。
3. **文献名称**：*Crystal Structure of ALDH5A1 Reveals Substrate Specificity Determinants*
**作者**：Malaspina, P., et al.
**摘要**：解析了ALDH5A1的晶体结构，明确了其底物结合口袋的关键氨基酸残基，为设计小分子抑制剂或酶活性增强剂提供了结构基础。
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如需更多文献，可补充提供具体研究方向(如疾病机制或药物开发)。
Aldehyde dehydrogenase 5A1 (ALDH5A1), also known as succinic semialdehyde dehydrogenase (SSADH), is a mitochondrial enzyme critical in the metabolism of the inhibitory neurotransmitter γ-aminobutyric acid (GABA). It catalyzes the oxidation of succinic semialdehyde (SSA) to succinate in the final step of the GABA degradation pathway, linking neurotransmitter regulation to the tricarboxylic acid (TCA) cycle. ALDH5A1 dysfunction, caused by genetic mutations, leads to SSA accumulation and subsequent conversion to neurotoxic metabolites like γ-hydroxybutyrate (GHB), resulting in a rare autosomal recessive disorder called SSADH deficiency. This condition manifests as developmental delays, hypotonia, epilepsy, and ataxia, highlighting the enzyme’s vital role in neurological health.
Recombinant ALDH5A1 protein is produced using expression systems such as *E. coli* or mammalian cells, enabling large-scale purification for functional and structural studies. Its production involves cloning the human *ALDH5A1* gene into expression vectors, followed by protein extraction and affinity chromatography (e.g., His-tag purification). The recombinant protein retains enzymatic activity, allowing researchers to investigate substrate specificity, kinetic properties, and inhibition mechanisms. It also serves as a tool for screening potential therapeutic compounds targeting SSADH deficiency or related metabolic disorders.
Studies using recombinant ALDH5A1 have advanced our understanding of its homotetrameric structure, cofactor (NAD+) binding, and mutation-induced functional impairments. Additionally, it aids in developing enzyme replacement therapies or gene-editing strategies. Beyond disease research, this protein is utilized in metabolic pathway analyses and biomarker discovery. Its availability accelerates translational research, bridging gaps between biochemical insights and clinical applications for GABA-related disorders.
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