| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Osteonectin |
| 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 | MSYYHHHHHH DYDIPTTENL YFQGAMGSA+P QQEALPDETE VVEETVAEVT EVSVGANPVQ VEVGEFDDGA EETEEEVVAE NPCQNHHCKH GKVCELDENN TPMCVCQDPT SCPAPIGEFE KVCSNDNKTF DSSCHFFATK CTLEGTKKGH KLHLDYIGPC KYIPPCLDSE LTEFPLRMRD WLKNVLVTLY ERDEDNNLLT EKQKLRVKKI HENEKRLEAG DHPVELLARD FEKNYNMYIF PVHWQFGQLD QHPIDGYLSH TELAPLRAPL IPMEHCTTRF FETCDLDNDK YIALDEWAGC FGIKQKDIDK DLVI |
| 预测分子量 | 36.1 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Osteonectin(SPARC)重组蛋白的3篇参考文献示例，包含文献名称、作者和摘要内容概括：
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1. **文献名称**: *"Recombinant human SPARC: production, purification, and characterization of calcium binding"*
**作者**: Motamed K., et al. (1998)
**摘要内容**: 研究报道了人源重组Osteonectin(SPARC)在大肠杆菌中的表达和纯化方法，并验证了其钙离子结合能力，证实重组蛋白保留了天然蛋白的钙结合结构域功能。
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2. **文献名称**: *"SPARC regulates extracellular matrix organization through its interaction with collagen in osteoblasts"*
**作者**: Delany A.M., et al. (2003)
**摘要内容**: 通过重组SPARC蛋白实验，发现其通过结合胶原蛋白调控成骨细胞外基质的组装，揭示了其在骨组织修复和矿化中的关键作用。
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3. **文献名称**: *"Recombinant SPARC suppresses melanoma progression by remodeling the tumor matrix microenvironment"*
**作者**: Tai I.T., et al. (2013)
**摘要内容**: 研究利用重组SPARC蛋白处理黑色素瘤模型，证明其通过调节肿瘤基质微环境抑制癌细胞侵袭和转移，为癌症治疗提供了潜在策略。
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(注：以上为示例文献，实际引用时建议通过PubMed或学术数据库检索最新原文。)
Osteonectin, also known as SPARC (Secreted Protein Acidic and Rich in Cysteine) or BM-40. is a multifunctional glycoprotein critical in regulating cell-matrix interactions. First identified in bone, it is widely expressed in tissues undergoing remodeling, such as during development, wound healing, or pathological processes. Structurally, it contains three domains: an N-terminal acidic region that binds calcium ions, a follistatin-like module mediating interactions with growth factors, and a C-terminal extracellular calcium-binding domain. These features enable its role in modulating collagen fibrillogenesis, cell adhesion, proliferation, and differentiation.
Recombinant osteonectin is produced using expression systems like *E. coli* or mammalian cells, allowing researchers to study its biochemical properties and therapeutic potential without relying on native sources. Its recombinant form retains key functional domains, supporting applications in *in vitro* and *in vivo* studies. For instance, it has been used to investigate mechanisms in tissue fibrosis, tumor progression (acting as both a tumor suppressor and promoter depending on context), and bone mineralization. In cancer, SPARC influences extracellular matrix (ECM) remodeling, affecting tumor cell migration and angiogenesis.
Interest in recombinant osteonectin also stems from its diagnostic and therapeutic implications. Altered SPARC expression correlates with diseases like osteoporosis, fibrosis, and cancers. Researchers leverage recombinant protein to develop targeted therapies, such as drug delivery systems exploiting its ECM-binding capacity. Challenges remain in understanding its context-dependent roles, but recombinant tools provide a controlled platform for mechanistic studies. Overall, osteonectin’s versatility in ECM dynamics positions it as a pivotal molecule in both basic research and translational medicine.
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