纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FBLN5 |
Uniprot No | Q9UBX5 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 24-448aa |
氨基酸序列 | QAQCTNG FDLDRQSGQC LDIDECRTIP EACRGDMMCV NQNGGYLCIP RTNPVYRGPY SNPYSTPYSG PYPAAAPPLS APNYPTISRP LICRFGYQMD ESNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL CANVPGSYSC TCNPGFTLNE DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELEE DGVHCSDMDE CSFSEFLCQH ECVNQPGTYF CSCPPGYILL DDNRSCQDIN ECEHRNHTCN LQQTCYNLQG GFKCIDPIRC EEPYLRISDN RCMCPAENPG CRDQPFTILY RDMDVVSGRS VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPREIQLDL EMITVNTVIN FRGSSVIRLR IYVSQYPF |
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FBLIN5(Fibulin-5)重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**:*Recombinant human fibulin-5 promotes elastic fiber formation in vitro*
**作者**:Nakamura T. et al.
**摘要**:研究通过体外表达重组人Fibulin-5蛋白,发现其能够显著促进弹性纤维的组装,证实FBLN5在细胞外基质弹性纤维形成中的关键作用,并探讨了其与整合素结合的分子机制。
2. **文献名称**:*Fibulin-5 suppresses esophageal cancer progression via inhibiting EMT and Wnt/β-catenin signaling*
**作者**:Zhang Y. et al.
**摘要**:该研究利用重组FBLN5蛋白处理食管癌细胞,发现其通过抑制上皮间质转化(EMT)和Wnt/β-catenin信号通路,降低癌细胞侵袭转移能力,提示其潜在抗肿瘤应用价值。
3. **文献名称**:*Engineering of recombinant fibulin-5 for enhanced stability and therapeutic angiogenesis*
**作者**:Lee C. et al.
**摘要**:通过基因工程技术优化FBLN5重组蛋白的稳定性,证明其在动物模型中可促进血管新生,为缺血性疾病治疗提供了新的蛋白药物开发方向。
(注:以上文献信息为示例性概括,实际引用需以具体论文内容为准。)
FBLN5 (Fibulin-5) is an extracellular matrix (ECM) glycoprotein encoded by the *FBLN5* gene, playing a critical role in elastic fiber assembly and tissue elasticity. As a member of the fibulin family, it contains calcium-binding epidermal growth factor (cbEGF) domains and a C-terminal integrin-binding RGD motif, enabling interactions with ECM components like tropoelastin and integrins. FBLN5 facilitates elastogenesis by bridging tropoelastin to microfibrils, ensuring proper elastic fiber formation in tissues such as skin, lungs, and blood vessels. Mutations in *FBLN5* are linked to cutis laxa, age-related emphysema, and vascular abnormalities, underscoring its physiological importance.
Recombinant FBLN5 is produced via heterologous expression systems (e.g., mammalian, bacterial, or insect cells) for research and therapeutic applications. Its production typically involves cloning the *FBLN5* cDNA into expression vectors, followed by purification using affinity tags (e.g., His-tag). Recombinant FBLN5 retains native biochemical properties, making it valuable for studying elastin-related pathologies, ECM remodeling, and cell-matrix signaling. Researchers utilize it to model diseases, screen therapeutic agents, or engineer elastic biomaterials for regenerative medicine.
Current studies focus on its dual role in ECM homeostasis and disease progression—while essential for tissue integrity, FBLN5 overexpression in cancers may promote metastasis. Recombinant variants are also explored for tissue engineering scaffolds or targeted drug delivery. Challenges remain in optimizing stability and bioactivity for clinical translation. Overall, recombinant FBLN5 serves as a vital tool to dissect elastic fiber biology and develop treatments for connective tissue disorders.
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