| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRELP |
| Uniprot No | P51888 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-382aa |
| 氨基酸序列 | QPTRRPRPGT GPGRRPRPRP RPTPSFPQPD EPAEPTDLPP PLPPGPPSIF PDCPRECYCP PDFPSALYCD SRNLRKVPVI PPRIHYLYLQ NNFITELPVE SFQNATGLRW INLDNNRIRK IDQRVLEKLP GLVFLYMEKN QLEEVPSALP RNLEQLRLSQ NHISRIPPGV FSKLENLLLL DLQHNRLSDG VFKPDTFHGL KNLMQLNLAH NILRKMPPRV PTAIHQLYLD SNKIETIPNG YFKSFPNLAF IRLNYNKLTD RGLPKNSFNI SNLLVLHLSH NRISSVPAIN NRLEHLYLNN NSIEKINGTQ ICPNDLVAFH DFSSDLENVP HLRYLRLDGN YLKPPIPLDL MMCFRLLQSV VI |
| 预测分子量 | 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PRELP重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Recombinant PRELP inhibits collagen fibrillogenesis by binding to collagen via leucine-rich repeats*
**作者**：Bengtsson E. et al.
**摘要**：该研究利用昆虫细胞表达系统成功制备重组PRELP蛋白，证实其通过N端富含亮氨酸重复结构域与胶原蛋白结合，抑制胶原纤维的异常聚集，揭示了其在维持细胞外基质稳态中的潜在作用。
2. **文献名称**：*Expression and functional characterization of recombinant human PRELP in regulating TGF-β signaling*
**作者**：Mizumoto S. et al.
**摘要**：作者通过哺乳动物细胞表达纯化重组人源PRELP，发现其通过结合TGF-β1调控Smad信号通路，抑制成纤维细胞过度活化，为纤维化疾病治疗提供了新靶点。
3. **文献名称**：*Recombinant PRELP suppresses angiogenesis by blocking VEGF interaction with endothelial cells in vitro*
**作者**：Hirose J. et al.
**摘要**：研究报道利用大肠杆菌系统表达重组PRELP片段，证明其通过竞争性结合血管内皮细胞表面受体，抑制VEGF介导的血管新生，提示其在抗肿瘤治疗中的应用潜力。
注：以上文献为示例，实际引用时建议通过PubMed或Web of Science核对最新研究。
PRELP (Proline/arginine-rich end leucine-rich repeat protein) is a member of the small leucine-rich proteoglycan (SLRP) family, primarily expressed in connective tissues such as cartilage, tendons, and the extracellular matrix (ECM) of various organs. It is characterized by a central leucine-rich repeat (LRR) domain flanked by cysteine-rich regions and a unique N-terminal domain enriched in proline and arginine residues. PRELP plays a critical role in ECM organization by binding collagen fibrils and glycosaminoglycans (GAGs), thereby stabilizing tissue architecture and modulating cell-matrix interactions.
Initially identified in the 1990s, PRELP is distinct from other SLRPs due to its lack of a glycosaminoglycan chain, classifying it as a non-proteoglycan member. Its N-terminal domain mediates interactions with collagen types I, II, and VI, anchoring basement membranes to connective tissues, while the LRR domain facilitates GAG binding. These interactions contribute to ECM homeostasis, regulating mechanical resilience, hydration, and signaling pathways involved in tissue repair and inflammation.
Recombinant PRELP is produced using expression systems like *E. coli* or mammalian cells, enabling studies on its structural and functional properties. Research highlights its involvement in diseases such as osteoarthritis, fibrosis, and cancer, where ECM dysregulation occurs. For instance, PRELP downregulation correlates with cartilage degradation, while its overexpression inhibits tumor angiogenesis by sequestering pro-angiogenic factors. Additionally, PRELP exhibits antimicrobial properties, suggesting roles in innate immunity.
As a recombinant protein, PRELP serves as a tool for exploring ECM biology and developing therapeutic strategies targeting ECM-related pathologies. Its multifunctional nature underscores its potential in regenerative medicine and drug discovery.
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