| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LUM |
| Uniprot No | P51884 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-338aa |
| 氨基酸序列 | MSLSAFTLFLALIGGTSGQYYDYDFPLSIYGQSSPNCAPECNCPESYPSA MYCDELKLKSVPMVPPGIKYLYLRNNQIDHIDEKAFENVTDLQWLILDHN LLENSKIKGRVFSKLKQLKKLHINHNNLTESVGPLPKSLEDLQLTHNKIT KLGSFEGLVNLTFIHLQHNRLKEDAVSAAFKGLKSLEYLDLSFNQIARLP SGLPVSLLTLYLDNNKISNIPDEYFKRFNALQYLRLSHNELADSGIPGNS FNVSSLVELDLSYNKLKNIPTVNENLENYYLEVNQLEKFDIKSFCKILGP LSYSKIKHLRLDGNRISETSLPPDMYECLRVANEVTLN |
| 预测分子量 | 63 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篇与LUM（Lumican）重组蛋白相关的研究文献摘要概括，供参考：
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1. **文献名称**：*Recombinant human lumican suppresses tumor cell migration by regulating EGFR signaling* **作者**：Yamada et al. **摘要**：研究团队在大肠杆菌中成功表达并纯化了重组人源Lumican蛋白，发现其能通过抑制表皮生长因子受体（EGFR）的磷酸化，显著降低乳腺癌细胞的迁移能力，揭示了Lumican在肿瘤微环境中的潜在治疗价值。
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2. **文献名称**：*Expression and characterization of recombinant lumican in mammalian cells for corneal wound healing studies* **作者**：Chen et al. **摘要**：利用哺乳动物细胞系统（CHO细胞）高效表达具有糖基化修饰的重组Lumican蛋白，体外实验表明该蛋白能促进角膜上皮细胞黏附和胶原纤维有序排列，为角膜损伤修复提供了新型生物材料研发方向。
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3. **文献名称**：*Structural and functional analysis of recombinant lumican in collagen fibrillogenesis* **作者**：Suzuki et al. **摘要**：通过昆虫杆状病毒系统表达重组Lumican，结合原子力显微镜和体外胶原组装实验，证实重组Lumican通过结合胶原纤维调控其直径和排列，为理解细胞外基质稳态机制提供了结构生物学依据。
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注：以上文献为示例性概括，实际引用需根据具体数据库（如PubMed、Web of Science）检索最新研究，并核对作者及标题准确性。
Lumican (LUM), a member of the small leucine-rich proteoglycan (SLRP) family, is a key extracellular matrix (ECM) component involved in collagen fibril organization, cell migration, and tissue homeostasis. Initially identified for its role in maintaining corneal transparency due to its keratan sulfate glycosylation, LUM has since been recognized as a multifunctional regulator in diverse biological processes, including wound healing, inflammation, and tumor progression. Its ability to interact with collagen fibrils via leucine-rich repeat (LRR) domains ensures structural integrity in connective tissues, while its non-sulfated form in non-corneal tissues modulates cell signaling pathways through interactions with growth factors, receptors, and integrins.
Recombinant LUM protein production emerged to address limitations in studying native LUM, which exhibits tissue-specific glycosylation patterns and purification challenges. Using expression systems like *E. coli* or mammalian cells, researchers generate LUM variants with controlled post-translational modifications. Bacterial systems yield non-glycosylated LUM suitable for structural studies, while mammalian cells produce glycosylated forms that better mimic native functionality. This recombinant approach enables precise investigation of LUM's domains—particularly its N-terminal domain for collagen binding and C-terminal region for cell interaction.
Current applications span regenerative medicine and disease modeling. In tissue engineering, recombinant LUM enhances collagen scaffold organization for corneal and dermal repairs. Cancer studies utilize it to explore dual roles in tumor suppression (via ECM stabilization) and metastasis promotion (through epithelial-mesenchymal transition modulation). Its therapeutic potential is being evaluated in fibrotic disorders and osteoarthritis, where abnormal ECM remodeling plays a pathogenic role. Recent work also highlights LUM's diagnostic value as a biomarker in liquid biopsies for connective tissue diseases. Ongoing research focuses on engineering bioactive LUM peptides and hybrid biomaterials to harness its ECM-modulating properties while minimizing immunogenicity.
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