纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | ALDOA |
Uniprot No | P04075 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-364aa |
氨基酸序列 | PYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSNHAY |
预测分子量 | 45.3 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ALDOA重组蛋白的参考文献示例(内容为模拟虚构,仅供参考):
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1. **文献名称**:*Expression and Purification of Recombinant Human ALDOA in E. coli for Structural Analysis*
**作者**:Zhang L, et al.
**摘要**:本研究利用大肠杆菌表达系统成功克隆、表达并纯化了重组人ALDOA蛋白。通过优化诱导条件和亲和层析技术,获得高纯度蛋白,并证实其具有天然醛缩酶活性,为后续晶体结构解析提供了材料基础。
2. **文献名称**:*ALDOA Recombinant Protein Enhances Glycolytic Flux in Cancer Cell Models*
**作者**:Kim S, Patel R.
**摘要**:研究通过体外实验证实,外源性添加重组ALDOA蛋白可显著提高多种癌细胞的糖酵解速率,并促进ATP生成,提示ALDOA在肿瘤代谢重编程中的潜在调控作用。
3. **文献名称**:*Functional Characterization of ALDOA Mutants Linked to Hereditary Myopathy*
**作者**:Garcia M, et al.
**摘要**:作者构建了与遗传性肌病相关的ALDOA突变体重组蛋白,发现部分突变导致酶活性显著下降,并破坏其与F-肌动蛋白的结合能力,揭示了疾病发生的分子机制。
4. **文献名称**:*Development of a High-Throughput Screening Assay Using Recombinant ALDOA for Drug Discovery*
**作者**:Watanabe T, et al.
**摘要**:本研究开发了一种基于重组ALDOA蛋白的高通量筛选平台,用于筛选抑制其酶活性的小分子化合物,为代谢性疾病或癌症的靶向治疗提供先导化合物。
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注:以上文献信息为示例性内容,实际研究中请通过学术数据库检索具体文献。
**Background of ALDOA Recombinant Protein**
Aldolase A (ALDOA), a key glycolytic enzyme, belongs to the aldolase family and catalyzes the cleavage of fructose-1.6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde-3-phosphate during glycolysis. It is predominantly expressed in skeletal muscle and erythrocytes, playing a critical role in cellular energy metabolism. Beyond its metabolic function, ALDOA exhibits non-catalytic roles, including regulation of cytoskeletal dynamics, cell adhesion, and interactions with signaling pathways such as mTOR and Hippo.
The recombinant ALDOA protein is engineered using genetic cloning techniques, often expressed in *E. coli* or mammalian systems to ensure proper folding and post-translational modifications. Purification methods like affinity chromatography (e.g., His-tag systems) yield high-purity protein for research applications. Recombinant ALDOA serves as a vital tool for studying enzyme kinetics, metabolic disorders (e.g., ALDOA deficiency linked to hereditary myopathy and hemolytic anemia), and cancer biology, where its overexpression correlates with tumor progression and poor prognosis.
Additionally, ALDOA’s structural and functional interplay with other biomolecules (e.g., F-actin, ATP) is explored using recombinant variants. Mutational studies using recombinant protein help dissect residues critical for substrate binding or protein-protein interactions. Its role as a potential biomarker or therapeutic target in diseases underscores its biomedical relevance.
In summary, ALDOA recombinant protein bridges fundamental research and clinical applications, offering insights into metabolic regulation, disease mechanisms, and drug discovery.
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