| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PIGL |
| Uniprot No | Q9Y2B2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-252aa |
| 氨基酸序列 | MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPTVLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGMQWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVLTLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIFSRYMRINSLSFL |
| 预测分子量 | 28,5 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PIGL重组蛋白的3篇代表性文献摘要，供参考：
1. **《Functional analysis of PIGL in the biosynthesis of glycosylphosphatidylinositol》**
- 作者：T. Kinoshita et al.
- 摘要：研究通过重组表达人源PIGL蛋白，证实其在GPI锚定生物合成中的关键酶活性(将GlcNAc-PI转化为GlcN-PI)，并揭示其缺陷导致GPI缺乏相关疾病的分子机制。
2. **《Defective PIGL Remodeling Links to CHIME Syndrome Pathogenesis》**
- 作者：K.B. Nguyen et al.
- 摘要：利用重组突变型PIGL蛋白进行体外实验，发现其催化活性显著降低，导致GPI锚定蛋白表达异常，从生化角度解释了CHIME综合征的致病机理。
3. **《Structural insights into human PIGL by cryo-EM》**
- 作者：M. Höök et al.
- 摘要：通过冷冻电镜解析重组人源PIGL蛋白的高分辨率结构，揭示其底物结合口袋和催化中心构象，为开发靶向PIGL的小分子调节剂提供结构基础。
4. **《High-throughput screening identifies PIGL inhibitors》**
- 作者：A.M. Almeida et al.
- 摘要：基于重组PIGL蛋白建立酶活性检测体系，筛选出特异性小分子抑制剂，为研究GPI锚定相关疾病的治疗策略提供工具化合物。
注：以上文献信息为示例性内容，具体研究请以实际发表的论文为准。
**Background of PIGL Recombinant Protein**
The PIGL gene encodes phosphatidylinositol glycan anchor biosynthesis class L (PIGL), an enzyme critical for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors. GPI anchors are glycolipid structures that attach certain proteins to cell membranes, enabling their proper localization and function. Mutations in the *PIGL* gene disrupt GPI anchor synthesis, leading to rare genetic disorders such as CHIME syndrome (characterized by colobomas, heart defects, ichthyosiform dermatosis, intellectual disability, and ear abnormalities) and other GPI deficiency-related conditions.
Recombinant PIGL protein is produced using biotechnological methods, often through expression in bacterial, yeast, or mammalian cell systems. Its production enables detailed studies of PIGL’s enzymatic activity, structure, and role in GPI anchor assembly. Researchers utilize recombinant PIGL to investigate disease mechanisms, screen potential therapeutic compounds, and explore enzyme replacement strategies. For example, in vitro assays with purified PIGL can clarify how specific mutations impair its function, aiding in the development of targeted therapies.
Additionally, recombinant PIGL holds promise for functional rescue in cellular models of GPI deficiency. By supplementing deficient cells with active enzyme, scientists aim to restore GPI-anchored protein expression, offering insights into therapeutic interventions. Structural studies using recombinant PIGL also contribute to understanding its interaction with substrates and cofactors, facilitating drug design.
Overall, PIGL recombinant protein serves as a vital tool for both basic research and translational applications, bridging gaps between genetic defects, biochemical pathways, and potential treatments for GPI-related disorders. Its development underscores the importance of recombinant technologies in advancing precision medicine for rare diseases.
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