| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | XRP2 |
| Uniprot No | O75695 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-350aa |
| 氨基酸序列 | GCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI |
| 预测分子量 | 66.5kDa |
| 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. |
以下是关于重组人RP2蛋白的3篇参考文献及其简要摘要：
1. **"Structural and functional characterization of the RP2 protein involved in X-linked retinitis pigmentosa"**
*作者：K. Hurd 等*
摘要：该研究解析了人RP2蛋白的晶体结构，揭示了其与Arl3 GTP酶的相互作用机制，验证了重组RP2蛋白在调控微管稳定性和纤毛形成中的功能，为X连锁视网膜色素变性(XLRP)的致病机理提供了分子基础。
2. **"Recombinant RP2 restores lipid-modified protein trafficking in cellular models of X-linked retinitis pigmentosa"**
*作者：M. Wright 等*
摘要：通过体外表达重组RP2蛋白，研究发现其能修复患者细胞中脂修饰蛋白(如视紫红质)的转运缺陷，表明RP2在脂质代谢和光感受器细胞存活中的关键作用，为基因治疗提供了潜在靶点。
3. **"RP2 interacts with β-tubulin and regulates vesicular transport in photoreceptor cells"**
*作者：S. Khanna 等*
摘要：利用重组RP2蛋白进行互作实验，发现其直接结合β-微管蛋白并参与光感受器细胞内囊泡运输，突变型RP2导致微管网络紊乱，解释了XLRP患者视网膜退化的细胞学机制。
注：以上文献为示例性内容，实际研究中建议通过PubMed或Web of Science检索最新文献(关键词：recombinant RP2 protein, X-linked retinitis pigmentosa, ARL3 GTPase)。RP2蛋白主要与X连锁视网膜病变相关，涉及微管调控和细胞运输功能。
XRP2 is a recombinant protein engineered through advanced genetic and biotechnological approaches, designed to address specific challenges in biomedical and therapeutic applications. Its development stems from the growing demand for highly stable, bioactive molecules capable of interacting with cellular targets with enhanced precision. The protein's architecture incorporates structural motifs derived from naturally occurring proteins known for their roles in cell adhesion, signaling, or immune modulation, optimized via computational modeling and directed evolution to improve functionality.
The design of XRP2 focuses on balancing stability and bioavailability. Unlike many native proteins, it exhibits resistance to proteolytic degradation and maintains structural integrity across a broad pH range, making it suitable for oral or systemic delivery. Its modular design allows for customizable domains, enabling researchers to tailor binding affinities or incorporate functional tags for diagnostic imaging or targeted drug delivery.
Production typically involves expression in microbial or mammalian systems, followed by rigorous purification to ensure homogeneity. XRP2’s scalability and cost-effective manufacturing have positioned it as a candidate for large-scale therapeutic use, particularly in oncology, autoimmune diseases, and regenerative medicine. Preclinical studies highlight its ability to modulate inflammatory pathways or promote tissue repair, though clinical validation remains ongoing.
Ethical and regulatory considerations around recombinant technologies have guided its development pathway, emphasizing biocompatibility and minimal immunogenicity. As a versatile platform, XRP2 exemplifies the convergence of synthetic biology and translational medicine, offering a template for next-generation protein therapeutics aimed at overcoming limitations of conventional biologics.
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