| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UTE |
| Uniprot No | Q13336 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-389aa |
| 氨基酸序列 | MEDSPTMVRVDSPTMVRGENQVSPCQGRRCFPKALGYVTGDMKELANQLKDKPVVLQFIDWILRGISQVVFVNNPVSGILILVGLLVQNPWWALTGWLGTVVSTLMALLLSQDRSLIASGLYGYNATLVGVLMAVFSDKGDYFWWLLLPVCAMSMTCPIFSSALNSMLSKWDLPVFTLPFNMALSMYLSATGHYNPFFPAKLVIPITTAPNISWSDLSALELLKSIPVGVGQIYGCDNPWTGGIFLGAILLSSPLMCLHAAIGSLLGIAAGLSLSAPFEDIYFGLWGFNSSLACIAMGGMFMALTWQTHLLALGCALFTAYLGVGMANFMAEVGLPACTWPFCLATLLFLIMTTKNSNIYKMPLSKVTYPEENRIFYLQAKKRMVESPL |
| 预测分子量 | 42,5 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. |
以下是模拟生成的关于“UTE重组蛋白”的参考文献示例(仅供格式参考，建议通过学术数据库查询真实文献)：
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1. **文献名称**：*Expression and Functional Analysis of Recombinant UTE Protein in E. coli*
**作者**：Smith A, et al.
**摘要**：研究利用大肠杆菌系统高效表达UTE重组蛋白，优化了诱导条件及纯化步骤，并通过体外实验验证其与靶分子的结合活性，为后续疾病机制研究提供工具。
2. **文献名称**：*Structural Characterization of UTE Protein and Its Role in Cellular Signaling*
**作者**：Lee B, et al.
**摘要**：通过冷冻电镜解析了UTE重组蛋白的三维结构，揭示了其独特的结构域分布，并证明其在调控细胞凋亡通路中的关键作用。
3. **文献名称**：*Recombinant UTE Protein as a Novel Biomarker for Autoimmune Diseases*
**作者**：Chen C, et al.
**摘要**：探讨UTE重组蛋白在类风湿性关节炎患者血清中的高表达现象，证实其作为潜在诊断标志物的临床价值。
4. **文献名称**：*High-Yield Production of UTE Fusion Protein for Therapeutic Antibody Development*
**作者**：Wang X, et al.
**摘要**：开发了一种哺乳动物细胞表达系统，规模化生产具有生物活性的UTE-Fc融合蛋白，为抗体药物研发提供新策略。
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**注意**：以上内容为模拟示例，实际文献需通过PubMed、Google Scholar等平台检索关键词“recombinant UTE protein”或结合具体研究领域细化搜索。
**Background of UTE Recombinant Protein**
Recombinant proteins, engineered through genetic modification, are produced by inserting target DNA sequences into host organisms (e.g., *E. coli*, yeast, or mammalian cells*) to express specific proteins. UTE recombinant protein, while not a universally standardized term, may refer to a customized or proprietary protein designed for specialized applications, potentially in biomedical research, therapeutics, or diagnostics. The "UTE" designation could denote unique structural features, functional properties, or target-specific modifications tailored for experimental or clinical use.
Recombinant technology enables precise control over protein production, ensuring high purity, scalability, and reproducibility—critical for research consistency and therapeutic safety. UTE recombinant proteins may be optimized for enhanced stability, solubility, or binding affinity, addressing challenges like aggregation or degradation in native proteins. Such modifications often involve codon optimization, fusion tags (e.g., His-tag for purification), or site-directed mutagenesis to improve functionality.
In drug development, recombinant proteins like monoclonal antibodies, enzymes, or cytokines have revolutionized treatments for cancers, autoimmune diseases, and genetic disorders. If UTE represents a therapeutic candidate, it might target specific pathways, receptors, or biomarkers, potentially offering advantages over conventional therapies. For instance, engineered proteins with extended half-lives or reduced immunogenicity are prioritized in biopharmaceutical pipelines.
Additionally, UTE recombinant proteins could serve as tools in structural biology (e.g., crystallography), diagnostic assays, or vaccine development. Their production in cost-effective microbial systems accelerates large-scale manufacturing, though complex proteins may require eukaryotic hosts for proper post-translational modifications.
Overall, UTE recombinant protein exemplifies the versatility of genetic engineering in creating tailored biomolecules to meet evolving scientific and medical demands, bridging gaps between laboratory discovery and real-world application.
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