| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FIL1d |
| Uniprot No | Q9UBH0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-155aa |
| 氨基酸序列 | VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAGKVIKGEE ISVVPNRWLD ASLSPVILGV QGGSQCLSCG VGQEPTLTLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTVPEADQPV RLTQLPENGG WNAPITDFYF QQCD |
| 预测分子量 | 16.8 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FIL1d重组蛋白的虚构参考文献示例(请注意，FIL1d重组蛋白的名称可能是假设的，实际文献需通过学术数据库查询)：
1. **文献名称**: "Structural and Functional Characterization of Recombinant FIL1d Protein in Plant Immunity"
**作者**: Zhang L. et al.
**摘要**: 本研究解析了FIL1d重组蛋白的晶体结构，发现其通过激活MAPK信号通路增强植物对真菌病原体的抗性，为开发新型抗病蛋白提供了理论基础。
2. **文献名称**: "FIL1d Recombinant Protein Enhances Wound Healing in Mammalian Models"
**作者**: Smith J.R., Patel K.
**摘要**: 通过体外和小鼠实验，证明FIL1d重组蛋白能显著促进成纤维细胞迁移和胶原沉积，提示其作为创伤修复治疗剂的潜力。
3. **文献名称**: "Optimization of FIL1d Expression in E. coli for Industrial-scale Production"
**作者**: Gupta S. et al.
**摘要**: 开发了一种高效的大肠杆菌表达系统，通过密码子优化和发酵条件调控，使FIL1d重组蛋白产量提高3倍，降低了工业化生产成本。
4. **文献名称**: "FIL1d Recombinant Protein as a Novel Biomarker for Early Cancer Detection"
**作者**: Tanaka M. et al.
**摘要**: 在血清学筛选中发现FIL1d重组蛋白与多种癌症(如结直肠癌、乳腺癌)早期阶段显著相关，特异性达92%，具有临床诊断价值。
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**提示**：以上为模拟文献，实际研究中请通过PubMed、ScienceDirect等平台检索真实文献(关键词：FIL1d recombinant protein + 研究领域)。若FIL1d为特定领域蛋白(如植物免疫、肿瘤学)，建议补充背景信息以缩小检索范围。
FIL1d recombinant protein is an engineered protein derivative designed to mimic or enhance specific functional domains of native proteins involved in cellular adhesion, signaling, or extracellular matrix (ECM) interactions. The "FIL1" designation typically refers to fibrinogen-like or fibronectin-related domains, which are critical in mediating cell-surface interactions, wound healing, and tissue remodeling. The "d" suffix often indicates a modified or truncated version optimized for stability, solubility, or targeted activity.
Originally derived from fibrinogen or related ECM proteins, FIL1d retains conserved binding motifs that interact with integrins, growth factor receptors, or other ECM components. This makes it valuable in biomedical research for studying cell migration, angiogenesis, or regenerative processes. Its recombinant production involves cloning the gene encoding the functional domain into bacterial or mammalian expression systems, followed by purification using affinity chromatography. This ensures high purity and reproducibility, addressing challenges associated with isolating native proteins from biological sources.
FIL1d has applications in tissue engineering, where it serves as a scaffold component to promote cell attachment and differentiation. It is also used in drug delivery systems to enhance targeting or biocompatibility. In disease models, FIL1d helps investigate pathologies linked to ECM dysregulation, such as fibrosis, cancer metastasis, or chronic inflammation. Recent studies explore its potential in 3D cell culture systems to better replicate in vivo microenvironments.
Despite its utility, limitations include potential immunogenicity in therapeutic contexts and variability in post-translational modifications depending on the expression host. Ongoing research focuses on engineering hybrid proteins or PEGylation to improve functionality and reduce adverse effects. As a tool, FIL1d exemplifies the convergence of protein engineering and translational medicine, offering insights into both fundamental biology and clinical applications.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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