纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ALDOS |
Uniprot No | P19099 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 25-503aa |
氨基酸序列 | GTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQGYEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELSLEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRPERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQEDIKMVYSFILRPGTSPLLTFRAIN |
预测分子量 | 71.0 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ALDOS重组蛋白的3篇参考文献示例:
1. **"Expression and Characterization of Recombinant Human Aldolase A in Escherichia coli"**
*作者:Smith J, et al. (2018)*
**摘要**:研究报道了在大肠杆菌中高效表达人源ALDOS A重组蛋白的方法,通过优化纯化流程获得高活性酶,用于糖酵解途径的动力学分析。
2. **"Functional Analysis of Recombinant Aldolase B in Hereditary Fructose Intolerance Models"**
*作者:Chen L, et al. (2020)*
**摘要**:利用昆虫细胞系统表达重组ALDOS B,揭示其突变体酶活缺陷,为遗传性果糖不耐症机制研究提供依据。
3. **"Biotechnological Production of Thermostable Aldolase from Archaea for Industrial Applications"**
*作者:Tanaka K, et al. (2019)*
**摘要**:从嗜热古菌中克隆ALDOS基因,在重组系统中表达耐高温醛缩酶,应用于合成生物学中的碳链延长反应。
(注:以上文献为示例性内容,实际引用时需核实具体文献信息。)
**Background of ALDOS Recombinant Protein**
ALDOS (Aldolase) recombinant protein is a genetically engineered form of the aldolase enzyme, primarily known for its role in glycolysis and gluconeogenesis. Aldolases are lyases that catalyze the cleavage of fructose-1.6-bisphosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P), a critical step in energy metabolism. The enzyme exists in multiple isoforms across organisms, with aldolase A (ALDOA) predominantly expressed in muscle, aldolase B (ALDOB) in liver, and aldolase C (ALDOC) in brain tissue.
Recombinant ALDOS proteins are produced using expression systems like *E. coli* or mammalian cells, enabling high-purity, scalable production for research and therapeutic applications. Their development stems from the need to study aldolase’s structure-function relationships, metabolic roles, and involvement in diseases. For instance, aldolase deficiencies are linked to hereditary fructose intolerance (ALDOB mutations) and certain cancers where metabolic reprogramming occurs.
Beyond basic enzymology, ALDOS recombinant proteins serve as tools in drug discovery, particularly for targeting metabolic disorders or pathogens relying on glycolysis, such as *Plasmodium* (malaria parasite). They also aid in structural studies, as aldolase’s conserved β-barrel fold and metal-ion-dependent mechanism provide insights into enzyme evolution and catalysis.
Recent advancements highlight ALDOS’s non-metabolic roles, including cytoskeletal interactions and regulation of cellular processes like autophagy. These multifunctional attributes make recombinant aldolase a valuable reagent for interdisciplinary research, bridging biochemistry, molecular biology, and medicine. Its applications extend to diagnostics, where aldolase levels serve as biomarkers, and biotechnology, supporting enzyme-driven synthesis in industrial processes. Overall, ALDOS recombinant proteins exemplify the intersection of traditional enzymology and modern genetic engineering.
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