| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ASPN |
| Uniprot No | Q9BXN1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-380aa |
| 氨基酸序列 | DMEDTDDDDDDDDDDDDDDEDNSLFPTREPRSHFFPFDLFPMCPFGCQCYSRVVHCSDLGLTSVPTNIPFDTRMLDLQNNKIKEIKENDFKGLTSLYGLILNNNKLTKIHPKAFLTTKKLRRLYLSHNQLSEIPLNLPKSLAELRIHENKVKKIQKDTFKGMNALHVLEMSANPLDNNGIEPGAFEGVTVFHIRIAEAKLTSVPKGLPPTLLELHLDYNKISTVELEDFKRYKELQRLGLGNNKITDIENGSLANIPRVREIHLENNKLKKIPSGLPELKYLQIIFLHSNSIARVGVNDFCPTVPKMKKSLYSAISLFNNPVKYWEMQPATFRCVLSRMSVQLGNFGM |
| 预测分子量 | 55.7 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. **"Asporin represses TGF-β signaling by competing with TGF-β type I receptor for Smad7 binding"**
- **作者**: Yamada S, et al.
- **摘要**: 研究揭示ASPN重组蛋白通过结合Smad7抑制TGF-β信号通路，在骨关节炎中通过阻断软骨细胞分化参与病理过程，体外实验证实其调控机制。
2. **"Recombinant Asporin expression in E. coli and its inhibitory effect on collagen mineralization"**
- **作者**: Lorenzo P, et al.
- **摘要**: 报道ASPN重组蛋白在大肠杆菌中的高效表达及纯化方法，发现其通过抑制胶原矿化调控骨形成，为研究骨骼疾病提供工具。
3. **"Asporin deficiency enhances chondrogenic differentiation in vitro and accelerates cartilage repair in vivo"**
- **作者**: Ikegawa S, et al.
- **摘要**: 利用重组ASPN蛋白敲除模型，证明其缺失促进间充质干细胞向软骨分化，动物实验显示ASPN缺陷小鼠软骨修复能力增强，提示其作为治疗靶点的潜力。
4. **"Structural and functional characterization of recombinant human Asporin in extracellular matrix remodeling"**
- **作者**: Kizawa H, et al.
- **摘要**: 通过X射线晶体学解析ASPN重组蛋白结构，结合细胞实验揭示其通过结合胶原蛋白调控基质代谢，为骨关节炎药物开发提供结构基础。
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以上文献均聚焦ASPN重组蛋白的分子机制及疾病关联，涵盖表达纯化、信号通路、结构功能及治疗应用等方向。
**Background of ASPN (Asporin) Recombinant Protein**
ASPN, or Asporin, is a secreted extracellular matrix (ECM) protein belonging to the small leucine-rich proteoglycan (SLRP) family. It is characterized by a leucine-rich repeat (LRR) domain and a unique N-terminal aspartic acid (D)-rich region, which distinguishes it from other SLRPs. ASPN is predominantly expressed in cartilage, bone, and connective tissues, where it interacts with collagens (e.g., collagen I and II) and regulates ECM organization and mineralization. Its D-repeat polymorphism (variable number of aspartic acid residues) has been linked to susceptibility to osteoarthritis (OA), intervertebral disc degeneration, and cancer progression.
Functionally, ASPN modulates signaling pathways by binding growth factors like TGF-β1. BMP-2. and FGF-2. Notably, it inhibits TGF-β1 activity by blocking its interaction with receptors, thereby influencing cell differentiation, fibrosis, and tissue remodeling. In OA, ASPN overexpression in cartilage correlates with ECM degradation and chondrocyte dysfunction, contributing to disease pathogenesis. Conversely, in cancer, ASPN exhibits dual roles—acting as a tumor suppressor in some contexts (e.g., gastric cancer) or promoting metastasis in others (e.g., breast cancer) via ECM remodeling and epithelial-mesenchymal transition (EMT).
Recombinant ASPN proteins are engineered to study its structure-function relationships and therapeutic potential. Produced using bacterial (e.g., *E. coli*) or mammalian expression systems, these proteins retain bioactivity for *in vitro* and *in vivo* assays. Applications include elucidating ASPN’s role in ECM dynamics, screening inhibitors for OA or fibrosis, and developing biomarker-based diagnostics. Challenges remain in optimizing post-translational modifications (e.g., glycosylation) to mimic native ASPN, critical for functional studies. Overall, ASPN recombinant proteins serve as vital tools for unraveling its diverse roles in health and disease.
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