| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOXL1 |
| Uniprot No | Q08397 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 292-574aa |
| 氨基酸序列 | DPGPEAAQA HGGDPRLGWY PPYANPPPEA YGPPRALEPP YLPVRSSDTP PPGGERNGAQ QGRLSVGSVY RPNQNGRGLP DLVPDPNYVQ ASTYVQRAHL YSLRCAAEEK CLASTAYAPE ATDYDVRVLL RFPQRVKNQG TADFLPNRPR HTWEWHSCHQ HYHSMDEFSH YDLLDAATGK KVAEGHKASF CLEDSTCDFG NLKRYACTSH TQGLSPGCYD TYNADIDCQW IDITDVQPGN YILKVHVNPK YIVLESDFTN NVVRCNIHYT GRYVSATNCK IVQS |
| 预测分子量 | 32 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LOXL1重组蛋白的示例参考文献(内容基于学术领域常见研究方向，建议通过PubMed或Google Scholar查询具体文献)：
1. **文献名称**：*"Recombinant LOXL1 Protein Attenuates Fibrosis by Regulating Collagen Crosslinking in a Mouse Model of Lung Injury"*
**作者**：Smith A, et al.
**摘要**：研究利用重组LOXL1蛋白在小鼠肺纤维化模型中验证其通过调控胶原交联抑制纤维化进展的机制，发现LOXL1重组蛋白可降低胶原沉积并改善肺功能。
2. **文献名称**：*"Structural and Functional Characterization of Recombinant LOXL1: Insights into Substrate Specificity"*
**作者**：Chen B, et al.
**摘要**：通过表达纯化重组LOXL1蛋白，结合X射线晶体学分析其三维结构，揭示了LOXL1催化结构域的关键活性位点及其对弹性蛋白的特异性结合机制。
3. **文献名称**：*"LOXL1 Gene Variants and Recombinant Protein Therapy in Pseudoexfoliation Glaucoma"*
**作者**：Johnson R, et al.
**摘要**：探讨LOXL1基因多态性与假性剥脱综合征的相关性，并证明外源性重组LOXL1蛋白可恢复患者眼内基质稳态，延缓青光眼病理进程。
4. **文献名称**：*"Targeting LOXL1 with Recombinant Proteins Inhibits Tumor Metastasis via Blocking EMT Pathways"*
**作者**：Wang Y, et al.
**摘要**：研究发现重组LOXL1蛋白可通过竞争性抑制内源性LOXL1活性，阻断上皮间质转化(EMT)，显著降低乳腺癌小鼠模型的转移潜能。
**注意**：以上为模拟文献，实际研究需通过学术数据库检索。建议使用关键词“LOXL1 recombinant protein”、“LOXL1 fibrosis/cancer/therapy”等查找最新成果。
Lysyl oxidase-like 1 (LOXL1) is a copper-dependent enzyme belonging to the lysyl oxidase family, which catalyzes the cross-linking of collagen and elastin in the extracellular matrix (ECM). It plays a critical role in maintaining tissue integrity, regulating ECM remodeling, and influencing cellular signaling pathways. LOXL1 has garnered significant attention due to its dual role in both physiological processes and disease pathogenesis. While essential for normal tissue homeostasis, dysregulation of LOXL1 is implicated in fibrotic disorders, cancer metastasis, and exfoliation syndrome (a risk factor for glaucoma).
Recombinant LOXL1 protein is engineered using genetic cloning techniques, typically expressed in mammalian or bacterial systems to ensure proper folding and post-translational modifications. This bioengineered form retains enzymatic activity and structural domains, including the catalytic copper-binding site and scavenger receptor cysteine-rich (SRCR) domains, enabling functional studies. Researchers utilize recombinant LOXL1 to investigate its mechanistic contributions to ECM stiffening, epithelial-mesenchymal transition (EMT), and tumor microenvironment modulation. In cancer, LOXL1 promotes metastasis by enhancing stromal remodeling and facilitating cancer cell invasion. Conversely, in fibrotic diseases, its overexpression drives pathological collagen cross-linking, leading to organ dysfunction.
Therapeutic strategies targeting LOXL1. including inhibitory antibodies or small molecules, are under exploration for anti-fibrotic and anti-metastatic therapies. Additionally, LOXL1 polymorphisms linked to exfoliation syndrome highlight its clinical relevance in ophthalmology. Recombinant LOXL1 serves as a vital tool for drug screening, structural studies, and elucidating molecular interactions in disease models. Challenges remain in understanding tissue-specific regulation and balancing therapeutic inhibition without disrupting normal ECM functions. Ongoing research aims to refine LOXL1-targeted interventions while addressing safety and efficacy in preclinical and clinical settings.
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