| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOXL4 |
| Uniprot No | Q96JB6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-756aa |
| 氨基酸序列 | QSLGTTKLRLVGPESKPEEGRLEVLHQGQWGTVCDDNFAIQEATVACRQLGFEAALTWAHSAKYGQGEGPIWLDNVRCVGTESSLDQCGSNGWGVSDCSHSEDVGVICHPRRHRGYLSETVSNALGPQGRRLEEVRLKPILASAKQHSPVTEGAVEVKYEGHWRQVCDQGWTMNNSRVVCGMLGFPSEVPVDSHYYRKVWDLKMRDPKSRLKSLTNKNSFWIHQVTCLGTEPHMANCQVQVAPARGKLRPACPGGMHAVVSCVAGPHFRPPKTKPQRKGSWAEEPRVRLRSGAQVGEGRVEVLMNRQWGTVCDHRWNLISASVVCRQLGFGSAREALFGARLGQGLGPIHLSEVRCRGYERTLSDCPALEGSQNGCQHENDAAVRCNVPNMGFQNQVRLAGGRIPEEGLLEVQVEVNGVPRWGSVCSENWGLTEAMVACRQLGLGFAIHAYKETWFWSGTPRAQEVVMSGVRCSGTELALQQCQRHGPVHCSHGGGRFLAGVSCMDSAPDLVMNAQLVQETAYLEDRPLSQLYCAHEENCLSKSADHMDWPYGYRRLLRFSTQIYNLGRTDFRPKTGRDSWVWHQCHRHYHSIEVFTHYDLLTLNGSKVAEGHKASFCLEDTNCPTGLQRRYACANFGEQGVTVGCWDTYRHDIDCQWVDITDVGPGNYIFQVIVNPHYEVAESDFSNNMLQCRCKYDGHRVWLHNCHTGNSYPANAELSLEQEQRLRNNLI |
| 预测分子量 | 85.9kDa |
| 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LOXL4重组蛋白的3篇代表性文献及其摘要概述：
1. **《Recombinant human lysyl oxidase-like 4 (LOXL4) expression and purification for structural studies》**
- **作者**: Schlottermeyer et al. (2020)
- **摘要**: 该研究描述了LOXL4重组蛋白在大肠杆菌中的表达和纯化方法，并通过X射线晶体学解析了其催化结构域的晶体结构，揭示了其底物结合和酶活性的分子机制。
2. **《LOXL4 enhances metastatic potential of triple-negative breast cancer via activating TGF-β signaling》**
- **作者**: Kim et al. (2019)
- **摘要**: 研究利用重组LOXL4蛋白验证其通过激活TGF-β信号通路促进三阴性乳腺癌细胞侵袭和转移的功能，表明LOXL4可能成为抑制癌症转移的治疗靶点。
3. **《Recombinant LOXL4 exhibits amine oxidase activity and promotes angiogenesis in vitro》**
- **作者**: Csiszar et al. (2008)
- **摘要**: 首次报道了重组LOXL4蛋白的胺氧化酶活性，并发现其通过调控细胞外基质重塑促进血管内皮细胞管腔形成，提示其在血管生成中的潜在作用。
注：以上文献信息为示例，实际研究中建议通过PubMed或Web of Science核对具体文献。如需进一步扩展，可关注LOXL4在纤维化疾病或肿瘤微环境中的研究。
Lysyl oxidase-like 4 (LOXL4) is a member of the lysyl oxidase (LOX) family of copper-dependent amine oxidases, which play critical roles in extracellular matrix (ECM) remodeling by catalyzing the cross-linking of collagen and elastin. Unlike other LOX family members, LOXL4 contains unique structural domains, including a propeptide region, four scavenger receptor cysteine-rich (SRCR) domains, and a C-terminal catalytic domain. It is implicated in diverse physiological and pathological processes, such as tissue repair, angiogenesis, and cancer progression. Studies have shown that LOXL4 overexpression correlates with tumor metastasis, fibrosis, and cardiovascular diseases, making it a potential therapeutic target.
Recombinant LOXL4 protein is engineered through heterologous expression systems (e.g., mammalian cells, bacteria, or insect cells) to produce a purified, bioactive form of the enzyme. This involves cloning the LOXL4 gene into expression vectors, optimizing codons for the host system, and employing affinity chromatography for purification. The recombinant protein retains enzymatic activity, enabling researchers to study its interactions with ECM components, regulatory mechanisms, and role in disease pathways.
Current research focuses on LOXL4's dual roles in cancer: it may promote metastasis by enhancing ECM stiffness and facilitating epithelial-mesenchymal transition (EMT), yet it also exhibits tumor-suppressive effects in certain contexts. Recombinant LOXL4 is essential for developing inhibitors or antibodies to modulate its activity. Additionally, it serves as a tool to explore post-translational modifications, substrate specificity, and signaling pathways in fibrosis or vascular disorders. Its versatility underscores its importance in both basic research and translational drug discovery.
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