| 纯度 | >80 % Purified via His tag. |
| 种属 | Human |
| 靶点 | AKR1B10 |
| Uniprot No | O60218 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-316aa |
| 氨基酸序列 | MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFNAEY |
| 预测分子量 | 63.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AKR1B10重组蛋白的模拟参考文献(实际文献需根据具体研究查询)：
1. **文献名称**：Expression and purification of recombinant human AKR1B10 and its enzymatic characterization
**作者**：Zhang Y, et al.
**摘要**：本研究通过大肠杆菌表达系统成功克隆并纯化了人源AKR1B10重组蛋白，分析了其对多种羰基底物(如视黄醛、4-氧壬烯醛)的还原酶活性，证实其在脂质过氧化产物代谢中的作用。
2. **文献名称**：AKR1B10 overexpression promotes tumor progression and correlates with clinical prognosis in hepatocellular carcinoma
**作者**：Cao D, et al.
**摘要**：通过重组AKR1B10蛋白功能实验，发现其在肝癌细胞中通过调控视黄酸代谢和Wnt/β-catenin通路促进肿瘤增殖和转移，为肝癌治疗提供潜在靶点。
3. **文献名称**：Structural basis of AKR1B10 inhibitors discovered by virtual screening
**作者**：Wang L, et al.
**摘要**：利用重组AKR1B10蛋白进行晶体结构解析，结合虚拟筛选技术鉴定了新型小分子抑制剂，揭示了其与酶活性位点的相互作用机制，为抗癌药物开发奠定基础。
(注：以上为示例性内容，实际文献需通过PubMed或Web of Science等数据库检索。)
AKR1B10 (aldo-keto reductase family 1 member B10) is a NADPH-dependent enzyme belonging to the aldo-keto reductase superfamily. It catalyzes the reduction of carbonyl-containing compounds, including aldehydes, ketones, and xenobiotics, playing a role in detoxification, metabolic regulation, and lipid synthesis. Initially identified as an enzyme overexpressed in hepatocellular carcinoma, AKR1B10 has since been linked to various cancers, including lung, breast, and colorectal cancers, where its upregulation is associated with tumor progression, chemoresistance, and poor prognosis.
The recombinant AKR1B10 protein is produced via heterologous expression systems (e.g., E. coli, mammalian cells) to study its biochemical properties and pathological mechanisms. Structurally, it shares a conserved (α/β)8-barrel fold typical of AKR enzymes, with substrate specificity influenced by active-site residues. Research highlights its role in metabolizing chemotherapeutic agents (e.g., daunorubicin) and lipid-derived aldehydes like 4-hydroxynonenal, which are implicated in oxidative stress and carcinogenesis. Additionally, AKR1B10 regulates fatty acid synthesis by stabilizing acetyl-CoA carboxylase, linking it to cancer cell proliferation.
Recombinant AKR1B10 is widely used in drug discovery to screen inhibitors targeting its enzymatic activity, with potential therapeutic applications in cancer and diabetic complications. Its overexpression in tumors also positions it as a biomarker for early cancer detection. However, conflicting studies note tissue-specific roles, as AKR1B10 is downregulated in certain gastrointestinal cancers, suggesting context-dependent functions. Ongoing studies aim to clarify its dual roles in normal physiology and disease, leveraging recombinant protein tools to explore structure-function relationships and therapeutic targeting strategies.
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