| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FBLN4 |
| Uniprot No | O95967 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-443aa |
| 氨基酸序列 | SPQDS EEPDSYTECT DGYEWDPDSQ HCRDVNECLT IPEACKGEMK CINHYGGYLC LPRSAAVIND LHGEGPPPPV PPAQHPNPCP PGYEPDDQDS CVDVDECAQA LHDCRPSQDC HNLPGSYQCT CPDGYRKIGP ECVDIDECRY RYCQHRCVNL PGSFRCQCEP GFQLGPNNRS CVDVNECDMG APCEQRCFNS YGTFLCRCHQ GYELHRDGFS CSDIDECSYS SYLCQYRCIN EPGRFSCHCP QGYQLLATRL CQDIDECESG AHQCSEAQTC VNFHGGYRCV DTNRCVEPYI QVSENRCLCP ASNPLCREQP SSIVHRYMTI TSERSVPADV FQIQATSVYP GAYNAFQIRA GNSQGDFYIR QINNVSAMLV LARPVTGPRE YVLDLEMVTM NSLMSYRASS VLRLTVFVGA YTF |
| 预测分子量 | 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FBLN4(Fibulin-4)重组蛋白的3篇代表性文献，包含文献名称、作者及摘要概括：
---
1. **文献名称**: *"Fibulin-4 is essential for elastic fiber assembly and extracellular matrix development"*
**作者**: Horiguchi M, et al.
**摘要**: 该研究通过重组Fibulin-4蛋白实验，揭示了其在弹性纤维形成中的关键作用。作者发现，Fibulin-4缺失会导致细胞外基质结构异常，重组蛋白的表达可部分恢复弹性蛋白的组装能力，表明其直接参与基质交联过程。
2. **文献名称**: *"Structural and functional analysis of recombinant Fibulin-4 in vascular smooth muscle cells"*
**作者**: Sasaki T, et al.
**摘要**: 本研究利用重组Fibulin-4蛋白分析其结构域功能，发现其C端区域对结合弹性蛋白原(tropoelastin)和整合素受体至关重要，并证明重组蛋白能促进血管平滑肌细胞的黏附与迁移，为动脉疾病机制提供新见解。
3. **文献名称**: *"Mutation-specific effects on Fibulin-4 folding and extracellular matrix interactions using recombinant protein models"*
**作者**: Choudhury R, et al.
**摘要**: 通过构建携带人类疾病相关突变的重组Fibulin-4蛋白，作者发现特定突变(如E57K)会导致蛋白错误折叠和分泌减少，影响其与细胞外基质组分(如纤连蛋白)的相互作用，解释了相关遗传性结缔组织病的分子机制。
---
以上文献均聚焦于重组Fibulin-4在细胞外基质功能、结构研究及疾病模型中的应用。如需获取全文，建议通过PubMed或期刊官网检索具体标题。
Fibulin-4 (FBLN4), a member of the fibulin family of extracellular matrix (ECM) glycoproteins, plays a critical role in elastic fiber assembly and tissue integrity. Encoded by the *EFEMP2* gene, it is a calcium-binding protein characterized by tandem epidermal growth factor (EGF)-like domains and a C-terminal fibulin-type module. FBLN4 interacts with elastin, fibrillin-1. and integrins, mediating cell-matrix adhesion and ECM organization. Its functional importance is underscored by genetic links to autosomal recessive cutis laxa type 1B, arterial tortuosity syndrome, and other connective tissue disorders marked by impaired elastogenesis and vascular/structural fragility.
Recombinant FBLN4 protein is engineered for research and therapeutic applications, typically produced via mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications. Purification methods often involve affinity tags (e.g., His-tag) followed by chromatography. The recombinant form retains bioactivity, supporting in vitro studies of elastin deposition, cell adhesion, and ECM remodeling. It is also explored in tissue engineering to enhance elastogenic properties of biomaterials or as a potential therapeutic for elastin-deficient diseases. Recent studies highlight its role in modulating TGF-β signaling and vascular smooth muscle cell behavior, expanding its relevance in cardiovascular and pulmonary research. Despite progress, challenges remain in scaling production and maintaining stability for clinical use.
×
