| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPARC |
| Uniprot No | P09486 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-303aa |
| 氨基酸序列 | APQQEALPDETEVVEETVAEVTEVSVGANPVQVEVGEFDDGAEETEEEVVAENPCQNHHCKHGKVCELDENNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIPPCLDSELTEFPLRMRDWLKNVLVTLYERDEDNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQKDIDKDLVI |
| 预测分子量 | 59.7kDa |
| 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3篇关于SPARC重组蛋白的经典文献摘要概括：
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1. **文献名称**：*Structural and functional analysis of recombinant human SPARC*
**作者**：Schultz, C. et al.
**摘要**：报道了利用大肠杆菌表达重组人SPARC蛋白的方法，并验证其抑制内皮细胞迁移和血管生成的功能，证实其与胶原结合的结构域关键区域。
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2. **文献名称**：*SPARC regulates extracellular matrix organization through its modulation of cell adhesion*
**作者**：Lane, T.F. & Sage, E.H.
**摘要**：通过哺乳动物细胞系统表达重组SPARC，发现其通过调控整合素信号通路抑制细胞粘附，影响细胞外基质的动态重塑。
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3. **文献名称**：*Recombinant SPARC suppresses tumor growth through dual anti-angiogenic and pro-apoptotic mechanisms*
**作者**：Chlenski, A. et al.
**摘要**：研究重组SPARC在神经母细胞瘤模型中的作用，显示其通过抑制血管生成和诱导肿瘤细胞凋亡显著降低肿瘤体积。
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4. **文献名称**：*Crystal structure of the SPARC (BM-40) C-terminal domain*
**作者**：Hohenester, E. et al.
**摘要**：解析了重组SPARC蛋白C端结构域的晶体结构，揭示了其与钙离子结合及调控细胞外基质组装的分子机制。
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以上研究覆盖了重组SPARC的表达方法、功能机制及结构解析，均为基础与转化研究的重要参考。
SPARC (Secreted Protein Acidic and Rich in Cysteine), also known as osteonectin or BM-40. is a calcium-binding glycoprotein that plays a multifaceted role in regulating cell-matrix interactions. Initially identified in bone matrix, SPARC is part of the "matrisome" – a group of extracellular matrix (ECM)-associated proteins. Its modular structure includes an N-terminal acidic domain, a follistatin-like cysteine-rich domain, and a C-terminal ECM-binding domain, enabling interactions with collagen, growth factors (e.g., VEGF, PDGF), and cell surface receptors.
Functionally, SPARC acts as a matricellular protein, modulating cell proliferation, migration, differentiation, and tissue remodeling. It influences collagen fibrillogenesis, growth factor bioavailability, and angiogenesis through ECM reorganization. SPARC's context-dependent roles are evident in embryonic development, wound healing, and pathological conditions like fibrosis and cancer. In oncology, it exhibits dual behavior – acting as a tumor suppressor by inhibiting cell cycle progression in some cancers while promoting metastasis through epithelial-mesenchymal transition (EMT) in others.
Recombinant SPARC production typically involves molecular cloning of human SPARC cDNA into expression vectors (e.g., E. coli, mammalian systems), followed by purification via affinity chromatography. This engineered protein retains native binding capabilities, making it valuable for in vitro studies of ECM dynamics, drug discovery targeting tumor-stroma interactions, and biomarker development. Recent therapeutic exploration includes SPARC-mediated drug delivery, leveraging its affinity for albumin in tumors. Despite progress, challenges remain in understanding its tissue-specific signaling and optimizing recombinant forms for clinical applications.
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