| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | algL |
| Uniprot No | O52195 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-374aa |
| 氨基酸序列 | AEALVPPKGYYAPVDIRKGEAPACPVVPEPFTGELVFRSKYEGSDAARST LNEEAEKAFRTKTAPITQIERGVSRMVMRYMEKGRAGDLECTLAWLDAWA EDGALLTTEYNHTGKSMRKWALGSLAGAYLRLKFSSSQPLAAYPEQARRI ESWFAKVGDQVIKDWSDLPLKRINNHSYWAAWAVMAAGVATNRRPLFDWA VEQFHIAAGQVDSNGFLPNELKRRQRALAYHNYSLPPLMMVAAFALANGV DLRGDNDGALGRLAGNVLAGVEKPEPFAERAGDEDQDMEDLETDAKFSWL EPYCALYSCSPALRERKAEMGPFKNFRLGGDVTRIFDPAEKSPRSTVGKR D |
| 预测分子量 | 59 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algL重组蛋白的虚构参考文献示例，供参考：
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1. **"Cloning and Expression of algL Gene in Escherichia coli for Alginate Lyase Production"**
*Authors: Smith A, et al.*
摘要：本研究成功克隆铜绿假单胞菌的algL基因，并在大肠杆菌中实现重组表达。纯化的重组酶显示高效降解藻酸盐活性，最适作用温度为40°C，pH 7.5.为工业应用奠定基础。
2. **"Characterization of Recombinant AlgL Lyase for Biofilm Disruption in Pseudomonas aeruginosa"**
*Authors: Johnson B, et al.*
摘要：通过重组表达AlgL蛋白，证实其可有效降解铜绿假单胞菌生物被膜中的藻酸盐基质，为抗生物被膜治疗提供潜在酶制剂。
3. **"Thermostability and Kinetic Analysis of Recombinant AlgL from Pseudomonas spp."**
*Authors: Lee C, et al.*
摘要：系统分析了重组AlgL的热稳定性与动力学参数，发现其在50°C以下保持稳定，Km值为2.3 mM，适用于褐藻加工中的高温处理工艺。
4. **"Biotechnological Application of Recombinant AlgL in Brown Algae Saccharification"**
*Authors: Zhang Y, et al.*
摘要：优化重组AlgL与纤维素酶协同作用，显著提高褐藻糖胶转化为可发酵糖的效率，为生物燃料生产提供新策略。
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注：以上文献为示例性内容，实际研究中请通过学术数据库检索真实文献。
AlgL is a recombinant protein derived from alginate lyase, an enzyme that specifically catalyzes the degradation of alginate, a linear polysaccharide composed of β-D-mannuronate (M) and α-L-guluronate (G) residues. Naturally produced by bacteria such as *Pseudomonas aeruginosa* and *Azotobacter vinelandii*, AlgL plays a critical role in alginate biosynthesis and remodeling by cleaving glycosidic bonds via a β-elimination mechanism. Its ability to depolymerize alginto oligosaccharides or monomers has garnered significant interest in biotechnological and biomedical applications.
Recombinant AlgL is engineered through heterologous expression systems, typically in *Escherichia coli*, to ensure high purity and yield for industrial or therapeutic use. This protein is particularly valued for its potential in treating cystic fibrosis, where chronic *P. aeruginosa* infections produce thick alginate-rich biofilms in patient airways. By disrupting these biofilms, AlgL enhances antibiotic efficacy and reduces pulmonary complications. Additionally, its enzymatic activity is leveraged in biorefinery processes to convert brown algae biomass—a renewable alginate source—into fermentable sugars for biofuel production.
Structurally, AlgL belongs to the polysaccharide lyase family, with conserved catalytic residues and a substrate-binding cleft that determines its specificity for M- or G-rich alginate regions. Studies using X-ray crystallography and mutagenesis have elucidated its mechanism, enabling protein engineering to optimize stability, activity, and pH tolerance. Recent advances also explore immobilized AlgL for continuous bioprocessing and its synergy with other enzymes in biomass degradation. As a sustainable alternative to chemical alginate processing, recombinant AlgL exemplifies the intersection of microbial enzymology and green biotechnology, addressing challenges in healthcare, energy, and environmental sustainability.
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