| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FLG |
| Uniprot No | P20930 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3838-4061aa |
| 氨基酸序列 | DSSRHSQSGQGESAGSRRSRRQGSSVSQDSDSEAYPEDSERRSESASRNHHGSSREQSRDGSRHPGSSHRDTASHVQSSPVQSDSSTAKEHGHFSSLSQDSAYHSGIQSRGSPHSSSSYHYQSEGTERQKGQSGLVWRHGSYGSADYDYGESGFRHSQHGSVSYNSNPVVFKERSDICKASAFGKDHPRYYATYINKDPGLCGHSSDISKQLGFSQSQRYYYYE |
| 预测分子量 | 39.4 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FLG(Filaggrin)重组蛋白研究的模拟参考文献示例(内容为虚构，仅用于演示格式)：
1. **《重组Filaggrin蛋白的表达及其在皮肤屏障功能研究中的应用》**
- 作者：Smith J, et al.
- 摘要：本研究通过大肠杆菌系统成功表达并纯化了重组Filaggrin蛋白，验证其促进角质层脂质排列的能力，证实其在修复皮肤屏障缺陷中的潜在应用价值。
2. **《FLG基因突变对重组Filaggrin结构稳定性的影响》**
- 作者：Brown A, et al.
- 摘要：通过体外重组技术构建了携带常见FLG突变位点的蛋白，发现突变导致Filaggrin降解加速，为遗传性鱼鳞病和湿疹的分子机制提供了实验依据。
3. **《重组Filaggrin蛋白调控角质细胞炎症反应的体外研究》**
- 作者：Lee S, et al.
- 摘要：利用重组Filaggrin处理人角质细胞，发现其可抑制IL-6和TNF-α的释放，提示其在特应性皮炎等炎症性皮肤病中的治疗潜力。
4. **《基于昆虫细胞系统的Filaggrin重组表达优化及功能鉴定》**
- 作者：Zhang Y, et al.
- 摘要：采用杆状病毒-昆虫细胞系统高效表达Filaggrin，发现其磷酸化修饰对后续分解为天然保湿因子的过程至关重要，为仿生护肤产品开发提供理论基础。
(注：以上文献为示例性内容，实际研究中需查询具体数据库获取真实文献。)
**Background of FLG Recombinant Protein**
Filaggrin (FLG) is a crucial epidermal protein encoded by the *FLG* gene, primarily expressed in the stratum granulosum of the epidermis. It plays a pivotal role in skin barrier formation by aggregating keratin intermediate filaments, facilitating the compaction of corneocytes during terminal differentiation. Post-translationally processed from its precursor, profilaggrin, filaggrin is further degraded into free amino acids and derivatives (e.g., urocanic acid), which contribute to skin hydration, pH regulation, and UV protection. Mutations in the *FLG* gene are strongly associated with impaired barrier function, leading to dermatological disorders such as atopic dermatitis, ichthyosis vulgaris, and increased susceptibility to allergic sensitization.
The development of recombinant filaggrin (rFLG) emerged to address challenges in studying filaggrin's molecular mechanisms and therapeutic potential. Native filaggrin is notoriously difficult to isolate due to its insolubility and rapid degradation in vivo. Recombinant expression systems (e.g., bacterial, yeast, or mammalian cell lines) enable scalable production of stable, purified FLG variants for experimental and clinical applications. rFLG has been instrumental in elucidating filaggrin's role in epidermal homeostasis, modeling disease pathologies, and screening barrier-restoring compounds.
Current research leverages rFLG to develop topical formulations or biologics aimed at compensating for filaggrin deficiency in genetic skin disorders. However, challenges persist, including maintaining protein stability, ensuring proper post-translational modifications, and mimicking native protein interactions. Advances in protein engineering and delivery systems continue to refine rFLG’s utility, positioning it as a promising tool for both mechanistic studies and translational dermatology.
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