| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Osbpl11 |
| Uniprot No | Q9BXB4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-747aa |
| 氨基酸序列 | MQGGEPVSTM KVSESEGKLE GQATAVTPNK NSSCGGGISS SSSSRGGSAK GWQYSDHMEN VYGYLMKYTN LVTGWQYRFF VLNNEAGLLE YFVNEQSRNQ KPRGTLQLAG AVISPSDEDS HTFTVNAASG EQYKLRATDA KERQHWVSRL QICTQHHTEA IGKNNPPLKS RSFSLASSSN SPISQRRPSQ NAISFFNVGH SKLQSLSKRT NLPPDHLVEV REMMSHAEGQ QRDLIRRIEC LPTSGHLSSL DQDLLMLKAT SMATMNCLND CFHILQLQHA SHQKGSLPSG TTIEWLEPKI SLSNHYKNGA DQPFATDQSK PVAVPEEQPV AESGLLAREP EEINADDEIE DTCDHKEDDL GAVEEQRSVI LHLLSQLKLG MDLTRVVLPT FILEKRSLLE MYADFMSHPD LFIAITNGAT AEDRMIRFVE YYLTSFHEGR KGAIAKKPYN PIIGETFHCS WKMPKSEVAS SVFSSSSTQG VTNHAPLSGE SLTQVGSDCY TVRFVAEQVS HHPPVSGFYA ECTERKMCVN AHVWTKSKFL GMSIGVTMVG EGILSLLEHG EEYTFSLPCA YARSILTVPW VELGGKVSVN CAKTGYSASI TFHTKPFYGG KLHRVTAEVK HNITNTVVCR VQGEWNSVLE FTYSNGETKY VDLTKLAVTK KRVRPLEKQD PFESRRLWKN VTDSLRESEI DKATEHKHTL EERQRTEERH RTETGTPWKT KYFIKEGDGW VYHKPLWKII PTTQPAE |
| 预测分子量 | 83,6 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Osbpl11重组蛋白的3篇参考文献示例(基于公开信息概括，部分内容为假设性描述)：
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1. **文献名称**: *Osbpl11 regulates vesicular transport and lipid metabolism in mammalian cells*
**作者**: Lehto, M., et al.
**摘要**: 研究探讨了Osbpl11(氧化固醇结合蛋白样蛋白11)在细胞内脂质转运和代谢中的作用，通过重组蛋白技术发现其与高尔基体膜结合并参与胆固醇动态平衡调控。
2. **文献名称**: *Structural insights into the lipid-binding properties of recombinant Osbpl11*
**作者**: Im, Y.J., et al.
**摘要**: 利用重组Osbpl11蛋白解析了其PH结构域与磷脂酰肌醇磷酸(PIPs)的结合机制，揭示了其在细胞内膜运输中的分子基础。
3. **文献名称**: *Osbpl11 deficiency disrupts cellular cholesterol homeostasis via impaired NPC1 interaction*
**作者**: Kang, S., et al.
**摘要**: 通过构建Osbpl11重组蛋白突变体，发现其与尼曼-匹克C1蛋白(NPC1)的相互作用缺陷导致溶酶体胆固醇外排障碍，可能与遗传性耳聋相关。
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**备注**：以上文献为示例性质，实际研究可能需通过PubMed或Google Scholar检索关键词“Osbpl11 recombinant”或“OSBPL11 function”获取。若需具体文献，建议补充更详细的研究背景或实验方向。
**Background of OSBPL11 Recombinant Protein**
OSBPL11 (Oxysterol-binding protein-like 11), also known as ORP11. belongs to the OSBP-related protein (ORP) family, which is involved in lipid metabolism, intracellular signaling, and vesicular transport. These proteins typically contain conserved domains, such as a pleckstrin homology (PH) domain and a ligand-binding domain, enabling interactions with membranes, sterols, or other lipids. OSBPL11 is implicated in regulating cholesterol homeostasis and lipid trafficking, particularly between the Golgi apparatus, endosomes, and plasma membrane.
The recombinant OSBPL11 protein is engineered for in vitro studies to elucidate its molecular functions. By expressing the protein in bacterial or mammalian systems, researchers can study its structure, lipid-binding specificity, and interactions with partner proteins (e.g., VAP proteins at membrane contact sites). Dysregulation of OSBPL11 has been linked to metabolic disorders, atherosclerosis, and cancer, highlighting its potential role in disease pathways. For instance, OSBPL11 may influence cell proliferation and apoptosis by modulating cholesterol distribution or signaling cascades like the PI3K/AKT pathway.
Recombinant OSBPL11 is also utilized to develop assays for drug screening, aiming to identify compounds that modulate its activity. Studies suggest its involvement in endocytic pathways and autophagy, further linking lipid metabolism to cellular stress responses. Despite progress, the precise mechanisms of OSBPL11 remain partially unresolved, necessitating further structural and functional research. Overall, OSBPL11 recombinant protein serves as a critical tool for decoding its biological roles and therapeutic potential in lipid-related diseases.
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