| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | Lpl |
| Uniprot No | P11152 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-474aa |
| 氨基酸序列 | ADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG |
| 预测分子量 | 55.3 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3篇关于LPL(脂蛋白脂肪酶)重组蛋白研究的参考文献摘要概括：
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1. **文献名称**: *"Recombinant human lipoprotein lipase: production in Chinese hamster ovary cells and functional characterization"*
**作者**: Liu G, Bengtsson-Olivecrona G, Olivecrona T
**摘要**: 该研究报道了在CHO细胞中高效表达重组人LPL的方法，通过优化启动子和纯化步骤获得高活性酶，证实其能有效水解乳糜微粒中的甘油三酯，并验证了其与肝素和载脂蛋白的结合特性。
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2. **文献名称**: *"Structural and functional analysis of the C-terminal domain of lipoprotein lipase using site-directed mutagenesis"*
**作者**: Wong H, Yang D, Hill JS, et al.
**摘要**: 通过定点突变技术研究LPL的C端结构域功能，发现该区域对酶活性、底物结合及与脂蛋白的相互作用至关重要，为理解LPL结构与功能的关联提供了实验依据。
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3. **文献名称**: *"Expression of functional lipoprotein lipase in prokaryotic system: challenges and solutions"*
**作者**: Zhang Y, Wang L, Liu X
**摘要**: 探讨在原核系统(大肠杆菌)中表达功能性LPL的难点，提出通过伴侣蛋白共表达和低温诱导策略提高可溶性蛋白产量，但酶活性仍低于哺乳动物系统表达产物。
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(注：以上为示例性概括，实际文献需通过PubMed或学术数据库检索。)
**Background of LPL Recombinant Protein**
Lipoprotein lipase (LPL) is a key enzyme in lipid metabolism, primarily responsible for hydrolyzing triglycerides in circulating chylomicrons and very-low-density lipoproteins (VLDL) into free fatty acids and glycerol. These products are then utilized by tissues for energy production or storage. LPL is anchored to the vascular endothelium via heparan sulfate proteoglycans and requires apolipoprotein C-II as a cofactor for optimal activity. Dysregulation of LPL function is linked to metabolic disorders, including hypertriglyceridemia, atherosclerosis, and familial LPL deficiency.
The development of recombinant LPL protein emerged from the need to study its structure-function relationships and therapeutic potential. Recombinant DNA technology enables the production of human LPL in heterologous systems, such as bacterial, yeast, or mammalian cell cultures. Mammalian systems, particularly Chinese hamster ovary (CHO) cells, are preferred for generating post-translationally modified, bioactive LPL due to their ability to perform proper glycosylation and folding.
Recombinant LPL has been instrumental in elucidating mechanisms underlying lipid metabolism, drug discovery, and gene therapy research. For instance, it aids in screening small molecules that modulate LPL activity for treating dyslipidemia. Additionally, LPL gene therapy using viral vectors encoding recombinant LPL has been explored for rare genetic disorders like familial LPL deficiency.
Challenges in LPL recombinant production include maintaining enzymatic stability and overcoming its short plasma half-life. Strategies like fusion proteins or PEGylation have been tested to enhance bioavailability. Overall, recombinant LPL serves as a vital tool for both basic research and translational applications in metabolic disease management.
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