| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IAH1 |
| Uniprot No | Q2TAA2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-248aa |
| 氨基酸序列 | MALCEAAGCG SALLWPRLLL FGDSITQFSF QQGGWGASLA DRLVRKCDVL NRGFSGYNTR WAKIILPRLI RKGNSLDIPV AVTIFFGAND SALKDENPKQ HIPLEEYAAN LKSMVQYLKS VDIPENRVIL ITPTPLCETA WEEQCIIQGC KLNRLNSVVG EYANACLQVA QDCGTDVLDL WTLMQDSQDF SSYLSDGLHL SPKGNEFLFS HLWPLIEKKV SSLPLLLPYW RDVAEAKPEL SLLGDGDH |
| 预测分子量 | 27,5 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IAH1重组蛋白的虚构参考文献示例(注：IAH1相关研究可能较为局限，建议核实基因/蛋白名称准确性)：
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1. **文献名称**: *Recombinant IAH1 Protein Expression and Its Role in Inflammatory Signaling*
**作者**: Zhang L, et al.
**摘要**: 研究报道了在大肠杆菌中高效表达可溶性IAH1重组蛋白的方法，并验证其通过抑制NF-κB通路减轻巨噬细胞的炎症反应，提示其作为抗炎治疗分子的潜力。
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2. **文献名称**: *Structural and Functional Characterization of IAH1: A Putative Hydrolase in Cancer Metabolism*
**作者**: Thompson M, et al.
**摘要**: 通过昆虫细胞系统表达IAH1重组蛋白，结合X射线晶体学分析其三维结构，发现其水解酶活性可能参与肿瘤代谢重编程，为靶向治疗提供依据。
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3. **文献名称**: *IAH1 Recombinant Protein Modulates Autophagy in Neurodegenerative Disease Models*
**作者**: Santos C, et al.
**摘要**: 在体外神经元模型中，纯化的IAH1蛋白通过激活AMPK/mTOR通路增强自噬，减少异常蛋白聚集，为神经退行性疾病研究提供新方向。
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**注意**：以上文献为示例性内容，实际研究中IAH1可能指代不同靶点。建议通过权威数据库(如PubMed)以准确基因名或蛋白编号(如UniProt ID)检索真实文献。
The IAH1 (Isoamyl Acetate-Hydrolyzing Esterase 1) recombinant protein is a genetically engineered enzyme derived from Saccharomyces cerevisiae, commonly studied for its role in ester metabolism. Originally identified for its ability to hydrolyze isoamyl acetate—a key ester contributing to the fruity aroma in fermented beverages—IAH1 belongs to the α/β-hydrolase superfamily. Its catalytic activity impacts flavor profiles in brewing and winemaking, making it industrially relevant.
Recombinant IAH1 is produced by cloning the IAH1 gene into expression systems (e.g., E. coli or yeast), enabling large-scale purification for functional studies. Researchers employ it to explore substrate specificity, enzymatic kinetics, and structural characteristics. Its tertiary structure, featuring a conserved catalytic triad (Ser-His-Asp), facilitates ester bond cleavage.
Beyond industrial applications, IAH1 serves as a model for understanding esterase mechanisms and metabolic engineering. Recent studies also investigate its potential in biodegradation of ester-based pollutants or synthesis of flavor compounds. However, its physiological role in native yeast—beyond ester hydrolysis—remains partially unclear, prompting ongoing research into its interactions with cellular pathways.
The protein’s recombinant form is critical for structure-function analyses, inhibitor development, and biotechnological optimization, bridging fundamental biochemistry with practical applications in food biotechnology and environmental science.
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