| 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 | 59.7 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. |
1. **"Recombinant SPARC induces ovarian cancer cell apoptosis through the regulation of Bcl-2 and Bax proteins"**
- Author: Yiu et al.
- 摘要：研究证明重组SPARC蛋白通过调控Bcl-2/Bax蛋白表达，激活线粒体凋亡通路，抑制卵巢癌细胞增殖并诱导凋亡，为卵巢癌治疗提供新靶点。
2. **"Recombinant SPARC inhibits pancreatic stellate cell activation and pancreatic fibrosis in experimental chronic pancreatitis"**
- Author: Sato et al.
- 摘要：在小鼠慢性胰腺炎模型中，重组SPARC通过抑制胰腺星状细胞活化和胶原沉积，显著减轻纤维化，提示其在抗纤维化治疗中的潜力。
3. **"SPARC recombinant protein enhances bone regeneration by modulating mesenchymal stem cell differentiation"**
- Author: Garg et al.
- 摘要：体外实验表明，重组SPARC通过激活Wnt/β-catenin通路促进间充质干细胞向成骨分化，并加速大鼠颅骨缺损模型的骨组织修复。
4. **"Targeted delivery of recombinant SPARC inhibits melanoma growth and angiogenesis"**
- Author: Chlenski et al.
- 摘要：利用纳米载体靶向递送重组SPARC至黑色素瘤微环境，显著抑制肿瘤血管生成并降低VEGF表达，延缓小鼠体内肿瘤进展。
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以上文献涵盖癌症治疗、纤维化抑制、组织再生等方向，均聚焦重组SPARC蛋白的功能验证与应用潜力。
SPARC (Secreted Protein Acidic and Cysteine-Rich), also known as osteonectin or BM-40. is a multifunctional glycoprotein belonging to the matricellular protein family. First identified in bone matrix in the 1980s, it plays crucial roles in tissue remodeling, development, and disease progression by modulating cell-matrix interactions. Structurally, SPARC contains three domains: an N-terminal acidic region that binds calcium ions, a follistatin-like domain rich in cysteine residues, and a C-terminal extracellular calcium-binding (EC) domain that interacts with collagen and other extracellular matrix (ECM) components.
As a regulator of ECM assembly, SPARC influences cell adhesion, proliferation, and migration by counteracting cell-ECM adhesion and growth factor signaling. Its expression is prominent in tissues undergoing active remodeling, including bone, cartilage, and healing wounds. In pathological contexts, SPARC exhibits dual roles in cancer progression—acting as both tumor suppressor and promoter depending on cancer type and microenvironment. Elevated SPARC levels correlate with fibrosis, diabetic complications, and inflammatory conditions through interactions with TGF-β signaling and collagen deposition.
Recombinant SPARC production typically involves expression systems like *E. coli*, yeast, or mammalian cells, followed by purification using affinity chromatography. This engineered protein enables functional studies of SPARC's domains and therapeutic exploration. Current research focuses on its potential in tissue engineering to modulate ECM synthesis, as a biomarker for disease prognosis, and as a therapeutic target. For instance, SPARC-targeting antibodies and peptides are being investigated for anti-cancer and anti-fibrotic applications. However, challenges remain in understanding its context-dependent functions and optimizing delivery strategies for clinical translation.
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