Recombinant Human SVEP1 protein

中文名： 含寿司、血管性血友病因子A型、表皮生长因子和短共有重复序列结构域蛋白1(SVEP1)重组蛋白
别名： SVEP1；C9orf13；CCP22；SELOB；Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1

货号: PA2000-4824

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	SVEP1
Uniprot No	Q4LDE5
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	736-827aa
氨基酸序列	GDFICTPDNTGVNCTLTCLEGYDFTEGSTDKYYCAYEDGVWKPTYTTEWPDCAKKRFANHGFKSFEMFYKAARCDDTDLMKKFSEAFETTLG
预测分子量	17.6 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SVEP1重组蛋白的3篇参考文献示例(注：文献信息为模拟生成，仅供参考)：

1. **文献名称**: *SVEP1 is a Human Coronary Disease Risk Locus that Promotes Atherosclerosis*

**作者**: M. K. Miller et al.

**摘要**: 该研究通过基因关联分析发现SVEP1基因变异与冠状动脉疾病风险相关，并利用重组SVEP1蛋白实验证明其通过整合素信号通路促进血管平滑肌细胞炎症反应和动脉粥样硬化斑块形成。

2. **文献名称**: *Structural Basis of SVEP1-Integrin Interaction in Cell Adhesion*

**作者**: T. Chen & L. R. Hsieh

**摘要**: 文章解析了重组SVEP1蛋白的晶体结构，揭示了其von Willebrand因子结构域与整合素α9β1结合的分子机制，为靶向SVEP1的抑制剂设计提供了结构基础。

3. **文献名称**: *Recombinant SVEP1 Production in Mammalian Cells and its Role in Tumor Angiogenesis*

**作者**: S. Park et al.

**摘要**: 研究建立了HEK293细胞表达系统生产功能性重组SVEP1蛋白，证实其通过调控VEGF信号通路促进肿瘤血管生成，提示SVEP1可能作为癌症治疗的潜在靶点。

(注：实际文献需通过PubMed/Google Scholar等平台检索关键词“SVEP1 recombinant protein”或结合具体研究领域筛选。)

背景信息

SVEP1 (Sushi, von Willebrand factor type A, EGF, and pentraxin domain-containing protein 1), also known as polydom, is a large extracellular matrix glycoprotein implicated in cell adhesion, signaling, and tissue development. Structurally, it contains multiple conserved domains, including sushi repeats, von Willebrand factor type A (vWA) domains, epidermal growth factor (EGF)-like motifs, and a C-terminal pentraxin domain, which collectively mediate interactions with integrins and other extracellular components. SVEP1 is broadly expressed in tissues such as blood vessels, bone, and cartilage, and plays critical roles in embryonic development, particularly in cardiovascular and skeletal systems.

Functionally, SVEP1 interacts with integrin α9β1. modulating cellular processes like adhesion, migration, and proliferation. It regulates vascular smooth muscle cell behavior and arterial stiffness, linking it to cardiovascular pathologies. Studies also associate SVEP1 variants with coronary artery disease, hypertension, and osteoporosis. Intriguingly, SVEP1 exhibits dual roles in cancer, acting as a tumor suppressor by inhibiting angiogenesis in some contexts or promoting metastasis in others, depending on the tumor microenvironment.

Recombinant SVEP1 protein is typically produced in mammalian or insect cell systems to preserve post-translational modifications (e.g., glycosylation) essential for its biological activity. This engineered protein serves as a vital tool for studying SVEP1-dependent signaling pathways, structural interactions, and its therapeutic potential. Current research focuses on elucidating its role in disease mechanisms, developing diagnostic biomarkers, and exploring targeted therapies for cardiovascular disorders and cancer. Its multifunctional nature and disease associations make SVEP1 a compelling subject for translational research.