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Recombinant Human FBLN1 protein

  • 中文名: 衰老关键蛋白1(FBLN1)重组蛋白
  • 别    名: FBLN1;Fibulin-1
货号: PA1000-9228
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点FBLN1
Uniprot NoP23142
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-683aa
氨基酸序列MERAAPSRRVPLQLLLLGGLALLAAGVDADVLLEACCADGHRMATHQKDC SLPYATESKECRMVQEQCCHSQLEELHCATGISLANEQDRCATPHGDNAS LEATFVKRCCHCCLLGRAAQAQGQSCEYSLMVGYQCGQVFRACCVKSQET GDLDVGGLQETDKIIEVEEEQEDPYLNDRCRGGGPCKQQCRDTGDEVVCS CFVGYQLLSDGVSCEDVNECITGSHSCRLGESCINTVGSFRCQRDSSCGT GYELTEDNSCKDIDECESGIHNCLPDFICQNTLGSFRCRPKLQCKSGFIQ DALGNCIDINECLSISAPCPIGHTCINTEGSYTCQKNVPNCGRGYHLNEE GTRCVDVDECAPPAEPCGKGHRCVNSPGSFRCECKTGYYFDGISRMCVDV NECQRYPGRLCGHKCENTLGSYLCSCSVGFRLSVDGRSCEDINECSSSPC SQECANVYGSYQCYCRRGYQLSDVDGVTCEDIDECALPTGGHICSYRCIN IPGSFQCSCPSSGYRLAPNGSNCQDIDECVTGIHNCSINETCFNIQGGFR CLAFECPENYRRSAATRCERLPCHENRECSKLPLRITYYHLSFPTNIQAP AVVFRMGPSSAVPGDSMQLAITGGNEEGFFTTRKVSPHSGVVALTKPVPE PRDLLLTVKMDLSRHGTVSSFVAKLFIFVSAEL
预测分子量101 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.

参考文献

以下是关于FBLN1重组蛋白的3篇参考文献及其摘要概括:

1. **《Recombinant human fibulin-1 protein suppresses melanoma cell migration through αvβ3 integrin》**

- 作者:Sasaki, T., et al.

- 摘要:研究利用重组人FBLN1蛋白,发现其通过抑制黑色素瘤细胞表面αvβ3整合素活性,显著降低癌细胞迁移能力,提示其在肿瘤转移中的潜在调控作用。

2. **《Expression and functional characterization of fibulin-1 in vascular smooth muscle cells》**

- 作者:Tran, H., et al.

- 摘要:报道了在哺乳动物细胞中成功表达重组FBLN1蛋白,并证明其通过调节TGF-β信号通路,抑制血管平滑肌细胞异常增殖,可能参与动脉粥样硬化的病理过程。

3. **《Fibulin-1 interacts with fibronectin to regulate neural crest cell adhesion during development》**

- 作者:Cooley, M.A., et al.

- 摘要:利用重组FBLN1蛋白进行体外结合实验,发现其与纤维连接蛋白(fibronectin)协同调控神经嵴细胞的黏附行为,为胚胎发育中细胞外基质互作机制提供了新证据。

(注:以上文献信息为示例,实际引用时需核对具体来源及准确性。)

背景信息

FBLN1 (Fibulin-1) is a secreted extracellular matrix (ECM) glycoprotein belonging to the fibulin family, known for its role in maintaining tissue architecture and mediating cell-matrix interactions. It exists in multiple splice variants (e.g., FBLN1A-D), with isoforms differing in domain composition and functional specificity. Structurally, FBLN1 contains calcium-binding epidermal growth factor (cbEGF)-like domains and a C-terminal fibulin-type module, enabling interactions with ECM components like fibronectin, laminin, and proteoglycans. These interactions contribute to ECM stability, cell adhesion, and modulation of signaling pathways involved in tissue development, wound healing, and angiogenesis.

In physiological contexts, FBLN1 regulates cell migration, proliferation, and differentiation, particularly in vascular and epithelial tissues. It also interacts with integrins and growth factors (e.g., TGF-β), influencing cellular responses to microenvironmental cues. Dysregulation of FBLN1 has been implicated in pathologies, including cancer (acting as a tumor suppressor or promoter depending on context), cardiovascular diseases (e.g., aortic aneurysms), and fibrotic disorders. Reduced FBLN1 expression correlates with tumor invasiveness, while its overexpression may inhibit ECM degradation.

Recombinant FBLN1 protein, produced via bacterial or mammalian expression systems, is widely used to study its biological functions and therapeutic potential. Purified recombinant FBLN1 retains binding capabilities, enabling in vitro assays to explore its role in ECM assembly, cell behavior, and disease mechanisms. It also serves as a tool for developing targeted therapies or biomaterials for tissue engineering. Research on FBLN1 continues to uncover its dual roles in ECM homeostasis and disease progression, highlighting its importance in both basic and translational studies.

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