| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | URGCP |
| Uniprot No | Q8TCY9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-931aa |
| 氨基酸序列 | MASPGIEVELLGKGHSDLGEVAPEIKASERRTAVAIADLEWREMEGDDCEFRYGDGTNEAQDNDFPTVERSRLQEMLSLLGLETYQVQKLSLQDSLQISFDSMKNWAPQVPKDLPWNFLRKLQALNADARNTTMVLDVLPDARPVEKESQMEEEIIYWDPADDLAADIYSFSELPTPDTPVNPLDLLCALLLSSDSFLQQEIALKMALCQFALPLVLPDSENHYHTFLLWAMRGIVRTWWSQPPRGMGSFREDSVVLSRAPAFAFVRMDVSSNSKSQLLNAVLSPGHRQWDCFWHRDLNLGTNAREISDGLVEISWFFPSGREDLDIFPEPVAFLNLRGDIGSHWLQFKLLTEISSAVFILTDNISKKEYKLLYSMKESTTKYYFILSPYRGKRNTNLRFLNKLIPVLKIDHSHVLVKVSSTDSDSFVKRIRAIVGNVLRAPCRRVSVEDMAHAARKLGLKVDEDCEECQKAKDRMERITRKIKDSDAYRRDELRLQGDPWRKAAQVEKEFCQLQWAVDPPEKHRAELRRRLLELRMQQNGHDPSSGVQEFISGISSPSLSEKQYFLRWMEWGLARVAQPRLRQPPETLLTLRPKHGGTTDVGEPLWPEPLGVEHFLREMGQFYEAESCLVEAGRLPAGQRRFAHFPGLASELLLTGLPLELIDGSTLSMPVRWVTGLLKELHVRLERRSRLVVLSTVGVPGTGKSTLLNTMFGLRFATGKSCGPRGAFMQLITVAEGFSQDLGCDHILVIDSGGLIGGALTSAGDRFELEASLATLLMGLSNVTVISLAETKDIPAAILHAFLRLEKTGHMPNYQFVYQNLHDVSVPGPRPRDKRQLLDPPGDLSRAAAQMEKQGDGFRALAGLAFCDPEKQHIWHIPGLWHGAPPMAAVSLAYSEAIFELKRCLLENIRNGLSNQNKNIQQLIELVRRL |
| 预测分子量 | 104,9 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URGCP重组蛋白的3-4篇参考文献示例(注：文献为虚构，仅供格式参考)：
1. **文献名称**：**"URGCP Recombinant Protein Facilitates DNA Repair in Hepatocellular Carcinoma Cells"**
**作者**：Liu et al.
**摘要**：研究通过在大肠杆菌中表达重组URGCP蛋白，揭示其在肝癌细胞中通过调控DNA损伤修复通路(如ATM/ATR)促进肿瘤耐药性的分子机制。
2. **文献名称**：**"Structural Characterization of Recombinant URGCP and Its Role in Cell Cycle Progression"**
**作者**：Gupta et al.
**摘要**：利用X射线晶体学解析重组URGCP蛋白的三维结构，发现其通过结合Cyclin D1调控G1/S期转换，为靶向癌症治疗提供结构基础。
3. **文献名称**：**"Recombinant URGCP Protein Enhances Epithelial-Mesenchymal Transition in Breast Cancer via TGF-β Signaling"**
**作者**：Kim et al.
**摘要**：通过体外实验证明重组URGCP蛋白激活TGF-β通路，促进乳腺癌细胞迁移和侵袭，提示其作为转移干预靶点的潜力。
4. **文献名称**：**"High-Yield Production of Recombinant URGCP in Insect Cells and Functional Analysis in Renal Fibrosis"**
**作者**：Martinez et al.
**摘要**：优化杆状病毒-昆虫细胞系统高效表达URGCP重组蛋白，发现其通过调控纤维化相关基因(如α-SMA)加重肾纤维化进程。
(注：以上文献为模拟生成，实际研究中请通过学术数据库检索具体文献。)
URGCP (Up-regulated in Gastric Cancer Protein), also known as RGC32 or C13ORF15. is a multifunctional protein implicated in cell cycle regulation, DNA damage response, and carcinogenesis. Initially identified as a gene overexpressed in gastric cancer, URGCP encodes a 17 kDa protein containing a conserved UPF0381 domain, though its precise molecular function remains under investigation. Studies suggest it acts as a transcriptional coactivator, enhancing the expression of cyclin D1 and c-Myc by interacting with β-catenin/TCF complexes in the Wnt/β-catenin signaling pathway. This interaction promotes cell proliferation, migration, and tumor progression. Dysregulation of URGCP has been observed in multiple cancers, including hepatocellular carcinoma, breast cancer, and glioblastoma, correlating with poor prognosis.
Recombinant URGCP proteins are typically produced using prokaryotic (e.g., E. coli) or eukaryotic expression systems (e.g., HEK293 cells) to preserve post-translational modifications. Purification often involves affinity tags like His-tag or GST-tag. These recombinant variants serve as critical tools for elucidating URGCP's structure-function relationships, biochemical interactions, and oncogenic mechanisms. They are widely used in in vitro assays, antibody production, and drug screening platforms targeting URGCP-associated pathways. Recent research also explores its role in non-cancer contexts, such as immune regulation and fibrosis. Despite progress, questions persist about its tissue-specific roles and regulatory networks, driving continued demand for high-purity recombinant URGCP in functional studies.
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