| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LIPF |
| Uniprot No | P07098 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-398aa |
| 氨基酸序列 | LFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK |
| 预测分子量 | 50.1 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LIPF(胃脂肪酶)重组蛋白的3-4篇参考文献的简化概括：
1. **文献名称**：*Expression and characterization of recombinant human gastric lipase in insect cells*
**作者**：Carrière, F., et al.
**摘要**：研究利用杆状病毒-昆虫细胞系统成功表达重组人胃脂肪酶(LIPF)，纯化后酶活性与天然酶相似，为大规模生产提供方法。
2. **文献名称**：*Structural and functional analysis of human gastric lipase using site-directed mutagenesis*
**作者**：Roussel, A., et al.
**摘要**：通过定点突变技术研究LIPF重组蛋白的催化机制，发现关键氨基酸残基对脂肪酶活性和底物特异性的影响。
3. **文献名称**：*Recombinant human gastric lipase for the treatment of pancreatic insufficiency*
**作者**：Moreau, H., et al.
**摘要**：评估重组LIPF在胰腺外分泌功能不足模型中的疗效，显示其能有效改善脂肪消化，具有潜在临床应用价值。
4. **文献名称**：*Stability and pH-dependent activity of recombinant human gastric lipase*
**作者**：Bénarouche, A., et al.
**摘要**：研究重组LIPF在不同pH条件下的稳定性与活性变化，揭示其在胃酸环境中的适应性机制。
注：以上内容为文献核心内容的简化概括，具体引用时需核对原文信息。
**Background of LIPF Recombinant Protein**
LIPF (Lysosomal Acid Lipase Family) recombinant protein is a genetically engineered form of the lysosomal acid lipase enzyme, which plays a critical role in lipid metabolism. Naturally produced in humans, lysosomal acid lipase (LAL) is encoded by the *LIPA* gene and functions within lysosomes to hydrolyze cholesteryl esters and triglycerides into free cholesterol and fatty acids. These breakdown products are essential for cellular energy production, membrane synthesis, and hormone regulation.
Deficiencies in endogenous LAL activity are linked to severe metabolic disorders, such as Wolman disease and cholesteryl ester storage disease (CESD), characterized by pathological lipid accumulation in lysosomes. To address these conditions, recombinant LIPF proteins are developed using biotechnological platforms (e.g., mammalian, yeast, or bacterial expression systems). These systems enable large-scale production of functional LAL enzymes with high purity and bioactivity.
Recombinant LIPF proteins are designed to mimic the native enzyme’s structure and function, often undergoing post-translational modifications (e.g., glycosylation) to enhance stability and efficacy. Therapeutic applications include enzyme replacement therapy (ERT) for LAL-deficient patients, aiming to reduce lipid storage and mitigate organ damage. Beyond clinical use, recombinant LIPF serves as a tool for studying lysosomal biology, lipid trafficking, and drug screening.
Research continues to optimize production methods, delivery mechanisms (e.g., PEGylation for prolonged circulation), and tissue targeting to improve therapeutic outcomes. Challenges remain in ensuring long-term efficacy, minimizing immune responses, and addressing accessibility for rare disease treatments. Overall, LIPF recombinant protein represents a critical advancement in bridging molecular biology with therapeutic innovation for metabolic disorders.
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