| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOX |
| Uniprot No | P28300 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 174-417aa |
| 氨基酸序列 | PYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY |
| 预测分子量 | 35.3 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. |
1. **"Recombinant lysyl oxidase propeptide protein inhibits growth and promotes apoptosis of pre-existing murine breast cancer xenografts"**
*Authors: Bais MV, Ozdener GB, Sonenshein GE, Trackman PC*
摘要：研究利用大肠杆菌系统表达重组LOX前肽蛋白，验证其抑制乳腺癌细胞生长并诱导凋亡的作用机制，通过小鼠模型证实可抑制肿瘤生长。
2. **"Expression, purification, and functional analysis of recombinant human lysyl oxidase variants in E. coli"**
*Authors: Kagan HM, Li W, Smith-Mungo L*
摘要：优化人源LOX在大肠杆菌中的重组表达与纯化流程，分析不同结构域缺失突变体的酶活性及底物特异性，为功能研究提供工具蛋白。
3. **"LOX collagen remodelling in idiopathic pulmonary fibrosis: a structural and kinetic study using recombinant enzyme"**
*Authors: Rodriguez HM, Vadas O, Jenkins G*
摘要：通过昆虫细胞系统表达重组LOX蛋白，解析其催化胶原交联的动力学特征，并证明其在肺纤维化病理模型中的异常活化机制。
4. **"Engineering a thermostable lysyl oxidase for biomedical applications through directed evolution"**
*Authors: Chen T, Yu J, Weiss SJ*
摘要：采用定向进化技术改造LOX蛋白的热稳定性，提升其在体外组织工程支架制备中的应用效能，显著增强胶原基材料的机械性能。
Lysyl oxidase (LOX) is a copper-dependent amine oxidase critical for extracellular matrix (ECM) remodeling and tissue homeostasis. It catalyzes the cross-linking of collagen and elastin fibers by oxidizing lysine residues, a process essential for maintaining structural integrity in connective tissues, blood vessels, and organs. Dysregulation of LOX activity is linked to fibrosis, cardiovascular diseases, and cancer metastasis, highlighting its dual role in physiological and pathological processes.
Recombinant LOX proteins are engineered using genetic cloning techniques to express the enzyme in heterologous systems, such as *E. coli*, yeast, or mammalian cell lines. These systems enable large-scale production of purified LOX for research and therapeutic applications. Recombinant LOX retains enzymatic activity and structural stability, allowing studies on its molecular mechanisms, substrate specificity, and interaction with ECM components. Notably, post-translational modifications (e.g., proteolytic activation by BMP-1) are often replicated in mammalian systems to ensure functional maturity.
In biomedical research, recombinant LOX is used to investigate fibrotic diseases, where excessive ECM cross-linking leads to organ dysfunction. Inhibitors targeting LOX are explored as antifibrotic or anticancer agents. Conversely, LOX supplementation shows potential in tissue engineering to enhance scaffold stability for regenerative medicine. Challenges remain in optimizing expression yields, minimizing aggregation, and preserving activity during purification. Advances in protein engineering, such as fusion tags or codon optimization, continue to improve recombinant LOX production, bridging gaps between basic research and clinical translation.
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