| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | WDR75 |
| Uniprot No | Q8IWA0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-830 aa |
| 活性数据 | MVEEENIRVVRCGGSELNFRRAVFSADSKYIFCVSGDFVKVYSTVTEECVHILHGHRNLVTGIQLNPNNHLQLYSCSLDGTIKLWDYIDGILIKTFIVGCKLHALFTLAQAEDSVFVIVNKEKPDIFQLVSVKLPKSSSQEVEAKELSFVLDYINQSPKCIAFGNEGVYVAAVREFYLSVYFFKKKTTSRFTLSSSRNKKHAKNNFTCVACHPTEDCIASGHMDGKIRLWRNFYDDKKYTYTCLHWHHDMVMDLAFSVTGTSLLSGGRESVLVEWRDATEKNKEFLPRLGATIEHISVSPAGDLFCTSHSDNKIIIIHRNLEASAVIQGLVKDRSIFTGLMIDPRTKALVLNGKPGHLQFYSLQSDKQLYNLDIIQQEYINDYGLIQIELTKAAFGCFGNWLATVEQRQEKETELELQMKLWMYNKKTQGFILNTKINMPHEDCITALCFCNAEKSEQPTLVTASKDGYFKVWILTDDSDIYKKAVGWTCDFVGSYHKYQATNCCFSEDGSLLAVSFEEIVTIWDSVTWELKCTFCQRAGKIRHLCFGRLTCSKYLLGATENGILCCWNLLSCALEWNAKLNVRVMEPDPNSENIAAISQSSVGSDLFVFKPSEPRPLYIQKGISREKVQWGVFVPRDVPESFTSEAYQWLNRSQFYFLTKSQSLLTFSTKSPEEKLTPTSKQLLAEESLPTTPFYFILGKHRQQQDEKLNETLENELVQLPLTENIPAISELLHTPAHVLPSAAFLCSMFVNSLLLSKETKSAKEIPEDVDMEEEKESEDSDEENDFTEKVQDTSNTGLGEDIIHQLSKSEEKELRKFRKIDYSWIAAL |
| 分子量 | 120.9 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是基于WDR75蛋白研究领域的模拟参考文献(示例仅供参考，实际文献需通过学术数据库检索)：
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1. **文献名称**: **"WDR75 interacts with the DROSHA-DGCR8 complex to regulate miRNA biogenesis in human cells"**
**作者**: Zhang Y, et al.
**摘要**: 研究发现WDR75通过结合microRNA加工复合物(DROSHA-DGCR8)，调控pre-miRNA的成熟过程，RNA干扰敲低WDR75会导致miRNA生成异常，提示其在基因表达调控中的作用。
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2. **文献名称**: **"Structural characterization of recombinant human WDR75 and its role in chromatin remodeling"**
**作者**: Patel S, et al.
**摘要**: 通过重组表达人源WDR75蛋白并解析其晶体结构，揭示其WD40结构域介导的蛋白质相互作用网络，并发现其与染色质重塑复合物SWI/SNF的功能关联。
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3. **文献名称**: **"WDR75 deficiency disrupts ciliogenesis and causes developmental defects in zebrafish"**
**作者**: Lee H, et al.
**摘要**: 利用斑马鱼模型研究WDR75基因功能，发现其缺失导致纤毛形成障碍及胚胎发育异常，表明WDR75在纤毛相关信号通路中的关键作用。
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4. **文献名称**: **"Proteomic analysis of WDR75-associated complexes in cancer cell lines"**
**作者**: Chen L, et al.
**摘要**: 应用免疫共沉淀结合质谱技术，鉴定WDR75在癌细胞中结合的蛋白复合物，发现其与DNA损伤修复蛋白相互作用，可能参与肿瘤发生机制。
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**备注**：以上文献信息为模拟内容，实际研究需参考真实发表的论文。建议通过PubMed、Web of Science或Google Scholar以关键词“WDR75 protein”或“WDR75 function”检索最新文献。
WDR75 (WD repeat-containing protein 75) is a conserved eukaryotic protein belonging to the WD40 repeat family, characterized by tandem ~40-amino acid motifs forming β-propeller structures that mediate protein-protein interactions. It plays critical roles in diverse cellular processes, including RNA processing, chromatin remodeling, and ciliogenesis. In humans, WDR75 is a component of the t-UTP subcomplex within the small subunit processome, facilitating ribosomal RNA (rRNA) maturation in the nucleolus. It also interacts with the ODF2/Cenexin protein to regulate centriole appendage formation and ciliary function, linking it to cilia-related disorders. Dysregulation of WDR75 has been associated with developmental defects, cancer progression, and polycystic kidney disease. Recombinant human WDR75 protein, typically produced in bacterial or mammalian expression systems, retains its structural integrity and functional domains, enabling in vitro studies on its molecular interactions, enzymatic roles, and therapeutic targeting. Current research focuses on elucidating its precise mechanisms in ribosome biogenesis, cilia assembly, and disease pathogenesis, offering potential insights into novel biomarkers or treatment strategies for ciliopathies and proliferative disorders. Despite its established importance, many aspects of WDR75’s regulatory networks remain unexplored, necessitating further functional genomics and structural analyses.
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