| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPC2 |
| Uniprot No | P61916 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-151aa |
| 氨基酸序列 | EPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVTFTSNIQSKS SKAVVHGILM GVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYPSIKLVVEWQ LQDDKNQSLF CWEIPVQIVSHL |
| 预测分子量 | 17 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NPC2重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
1. **"Recombinant NPC2 Protein Restores Cholesterol Homeostasis in Cellular Models of Niemann-Pick Type C Disease"**
*作者：Li, X., et al.*
**摘要**：研究利用昆虫细胞系统表达重组NPC2蛋白，证实其能有效逆转NPC1缺陷细胞中的胆固醇堆积，为潜在治疗策略提供依据。
2. **"Structural and Functional Characterization of Human NPC2 Expressed in Yeast"**
*作者：Zhang, Y., & Wang, Q.*
**摘要**：通过酵母表达系统获得高纯度重组人NPC2蛋白，结合实验和分子模拟揭示其与胆固醇结合的关键结构域及动态机制。
3. **"Efficient Production of Biologically Active Recombinant NPC2 via Mammalian Cell Culture"**
*作者：Gupta, R., et al.*
**摘要**：采用哺乳动物HEK293细胞表达重组NPC2.验证其与溶酶体膜蛋白NPC1的协同作用，显著增强体外胆固醇转运效率。
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*注：以上文献为示例性概括，实际引用需根据具体研究通过学术数据库(如PubMed、Web of Science)检索。*
NPC2 (Niemann-Pick type C2) is a small, conserved lysosomal protein critical for intracellular cholesterol trafficking. It binds and transfers cholesterol within the lysosomal lumen in cooperation with NPC1. a transmembrane protein, to facilitate cholesterol export to cellular membranes. Mutations in the NPC2 gene cause Niemann-Pick disease type C (NP-C), a rare lysosomal storage disorder characterized by cholesterol and lipid accumulation, leading to progressive neurological deterioration and organ dysfunction.
Structurally, NPC2 is a 16 kDa glycoprotein with a hydrophobic pocket that specifically binds cholesterol. Its β-sandwich fold and conserved carbohydrate-binding domain enable interactions with vesicle membranes. Recombinant NPC2 proteins are generated using expression systems like *E. coli* or mammalian cells, often tagged for purification. These engineered proteins retain functional cholesterol-binding capacity and are essential tools for studying NP-C pathology, lysosomal biology, and cholesterol homeostasis.
Research applications include *in vitro* assays to dissect cholesterol transport mechanisms, drug screening for NP-C therapeutics, and structural studies to map mutation-induced functional defects. Recombinant NPC2 also holds therapeutic potential, such as enzyme replacement strategies or gene therapy vectors. Its role extends beyond NP-C, with emerging links to viral entry (e.g., Ebola) and immune modulation, highlighting broader biomedical relevance.
In summary, recombinant NPC2 bridges basic science and translational medicine, offering insights into lysosomal disorders and enabling targeted therapeutic development.
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