| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOXL2 |
| Uniprot No | Q9Y4K0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-774aa |
| 氨基酸序列 | QYDSWPHYPEYFQQPAPEYHQPQAPANVAKIQLRLAGQKRKHSEGRVEVY YDGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDN LHCTGNEATLAACTSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINQ IENLNIQVEDIRIRAILSTYRKRTPVMEGYVEVKEGKTWKQICDKHWTAK NSRVVCGMFGFPGERTYNTKVYKMFASRRKQRYWPFSMDCTGTEAHISSC KLGPQVSLDPMKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPL VRLRGGAYIGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEA VTGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNAESQGCNHEEDAGVRCN TPAMGLQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGQNWGIVEAMV VCRQLGLGFASNAFQETWYWHGDVNSNKVVMSGVKCSGTELSLAHCRHDG EDVACPQGGVQYGAGVACSETAPDLVLNAEMVQQTTYLEDRPMFMLQCAM EENCLSASAAQTDPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDC HRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKNYECAN FGDQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNFEVAESDY SNNIMKCRSRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLLNNQLSPQ |
| 预测分子量 | 85 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LOXL2重组蛋白的3篇代表性文献及其摘要概括：
---
1. **文献名称**: *LOXL2-mediated extracellular matrix remodeling drives metastasis in colorectal cancer*
**作者**: Barker HE, et al.
**摘要**: 该研究通过重组LOXL2蛋白实验，揭示其在结直肠癌转移中的作用。LOXL2通过修饰细胞外基质(ECM)，促进肿瘤细胞侵袭和转移，并激活EMT(上皮-间质转化)信号通路。
2. **文献名称**: *Recombinant LOXL2 protein enhances collagen crosslinking and accelerates fibrosis in a murine lung injury model*
**作者**: Barrientos S, et al.
**摘要**: 研究利用重组LOXL2蛋白在小鼠肺纤维化模型中验证其功能，发现LOXL2通过催化胶原交联加重纤维化进程，提示其作为抗纤维化治疗靶点的潜力。
3. **文献名称**: *Targeting LOXL2 with a recombinant inhibitory protein suppresses tumor growth and metastasis in breast cancer*
**作者**: Canesin G, et al.
**摘要**: 该团队设计了一种重组LOXL2抑制蛋白，可在乳腺癌模型中阻断LOXL2的酶活性，显著抑制原发肿瘤生长和肺转移，为靶向LOXL2的癌症治疗提供新策略。
---
如需更多文献或具体领域研究，可进一步补充关键词或研究背景。
Lysyl oxidase-like 2 (LOXL2) is a member of the lysyl oxidase (LOX) family of copper-dependent amine oxidases that catalyze the cross-linking of collagen and elastin in the extracellular matrix (ECM). Unlike its closely related enzyme LOX, LOXL2 exhibits distinct structural features, including four scavenger receptor cysteine-rich (SRCR) domains and a catalytic domain. It plays critical roles in ECM remodeling, tissue fibrosis, and cancer progression by regulating ECM stiffness, epithelial-to-mesenchymal transition (EMT), and cell migration. Dysregulation of LOXL2 has been implicated in pathological conditions such as liver fibrosis, pulmonary fibrosis, and metastatic cancers, making it a potential therapeutic target.
Recombinant LOXL2 protein is produced through genetic engineering, typically using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications and enzymatic activity. The purified protein retains its oxidase function, enabling researchers to study its biochemical properties, substrate interactions, and inhibition mechanisms in vitro. It is widely used in drug discovery to screen LOXL2 inhibitors, particularly for antifibrotic and anticancer therapies. Additionally, recombinant LOXL2 serves as a critical tool for investigating its non-enzymatic roles, such as transcriptional regulation and cellular signaling crosstalk. Despite challenges in maintaining solubility and stability, advancements in protein engineering have improved its applicability in structural studies (e.g., crystallography) and functional assays. Current research focuses on elucidating LOXL2's dual roles in ECM homeostasis and disease pathogenesis, aiming to develop targeted therapies with reduced off-target effects.
×
