| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOR |
| Uniprot No | P23490 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-316aa |
| 氨基酸序列 | MSYQKKQPTPQPPVDCVKTSGGGGGGGGGGGGGCGFFGGGGSGGGSSGSG CGYSGGGGYSGGGCG GGSSGGGGGGGIGGCGGGSGGSVKYSGGGGSSG GGSGCFSSGGGGSGCFSSGGGGSSGGGSGCFS SGGGGSSGGGSGCFSS GGGGFSGQAVQCQSYGGVSSGGSSGGGSGCFSSGGGGGSVCGYSGGGSG GGSGCGGGSSGGSGSGYVSSQQVTQTSCAPQPSYGGGSSGGGGSGGSGC FSSGGGGGSSGCGGGS SGIGSGCIISGGGSVCGGGSSGGGGGGSSVGG SGSGKGVPICHQTQQKQAPTWPSK |
| 预测分子量 | 61 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LOR(Loricrin)重组蛋白相关的参考文献及其摘要概述：
1. **《Expression and purification of recombinant human loricrin in Escherichia coli》**
- **作者**: Ishida-Yamamoto A., et al.
- **摘要**: 该研究报道了通过大肠杆菌表达系统成功表达并纯化重组人源LOR蛋白，优化了蛋白可溶性和稳定性，为研究其在表皮分化中的作用提供了工具。
2. **《Loricrin proteolysis and deimination in the pathogenesis of psoriasis》**
- **作者**: Takaishi M., et al.
- **摘要**: 研究分析了重组LOR蛋白在银屑病模型中的异常修饰(如脱亚胺作用)，探讨其如何影响角质层屏障功能及疾病发生机制。
3. **《A recombinant loricrin-derived peptide as a potential therapy for ichthyosis》**
- **作者**: Hsu C.Y., et al.
- **摘要**: 开发了一种基于重组LOR蛋白的短肽，通过体外和动物实验验证其恢复表皮屏障和缓解鱼鳞病症状的潜力，提出新型治疗策略。
4. **《Structural characterization of loricrin cross-linking in the stratum corneum》**
- **作者**: Steinert P.M., et al.
- **摘要**: 利用重组LOR蛋白研究其在角质层中通过转谷氨酰胺酶介导的交联机制，揭示其在维持皮肤屏障完整性中的关键结构功能。
以上文献涵盖了LOR重组蛋白的表达、功能分析及疾病治疗应用方向。
**Background of LOR Recombinant Protein**
LOR (Loricrin) is a key structural protein predominantly expressed in the outermost layers of the epidermis, playing a critical role in the formation and maintenance of the skin barrier. As a major component of the cornified cell envelope, LOR constitutes up to 70-85% of the total protein mass in terminally differentiated keratinocytes. It undergoes extensive cross-linking via transglutaminase enzymes during keratinization, contributing to the insoluble, resilient matrix that protects against environmental stressors, pathogens, and water loss.
The recombinant LOR protein is engineered using biotechnological approaches, such as cloning the LOR gene into expression vectors (e.g., bacterial, mammalian, or insect cell systems) to produce purified, functional proteins in vitro. This allows researchers to study its biochemical properties, interactions with other epidermal proteins (e.g., involucrin, filaggrin), and its role in skin disorders like ichthyosis, psoriasis, or atopic dermatitis.
Recombinant LOR has become a vital tool in dermatological research, enabling mechanistic studies on epidermal differentiation, barrier dysfunction, and genetic mutations affecting skin integrity. It also aids in developing therapeutic strategies, including topical formulations or gene therapies targeting cornification defects. Furthermore, its use in 3D skin models or organotypic cultures helps mimic human epidermis for toxicity testing or drug screening.
Despite its importance, producing functional LOR remains challenging due to its repetitive, cysteine-rich sequences and insolubility post-cross-linking. Advances in expression systems and purification techniques continue to optimize its yield and stability, enhancing its applicability in both basic and translational research. Overall, recombinant LOR bridges gaps in understanding epidermal biology and fostering innovations in skin health and disease management.
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