| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPRKB |
| Uniprot No | Q9Y3C4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-175aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL |
| 预测分子量 | 22 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TPRKB重组蛋白的假设性参考文献示例(注：TPRKB相关研究较为小众，以下内容为模拟创作，仅供参考)：
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1. **文献名称**: *TPRKB interacts with DNA-PKcs and regulates DNA double-strand break repair*
**作者**: Smith A, et al.
**摘要**: 本研究通过重组表达人源TPRKB蛋白，发现其与DNA-PK复合物(DNA-PKcs)直接结合，并通过调控激酶活性促进非同源末端连接(NHEJ)修复通路。实验表明，TPRKB缺失会导致细胞对电离辐射敏感性增加。
2. **文献名称**: *Structural insights into TPRKB’s role in cell cycle progression*
**作者**: Lee J, et al.
**摘要**: 利用X射线晶体学解析了重组TPRKB蛋白的TPR结构域三维结构，揭示其通过结合Cyclin B1调控G2/M期转换的分子机制，为靶向细胞周期异常疾病的药物设计提供依据。
3. **文献名称**: *Recombinant TPRKB enhances p53 stability under oxidative stress*
**作者**: Zhang Y, et al.
**摘要**: 通过体外重组TPRKB蛋白实验，证明其与p53蛋白的相互作用可抑制MDM2介导的泛素化降解，从而增强细胞在氧化应激条件下的基因组稳定性。
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**注意**：以上内容为基于TPRKB可能功能的模拟创作，实际文献需通过学术数据库(如PubMed、Web of Science)以“TPRKB”“recombinant protein”等关键词检索确认。若研究领域或蛋白名称存在拼写误差，建议结合具体背景调整检索策略。
**Background of TPRKB Recombinant Protein**
TPRKB (TPR-containing protein kinase B) is a recombinant protein engineered to study cellular signaling pathways, particularly those involving protein-protein interactions and kinase activity. The "TPR" (tetratricopeptide repeat) domain is a structural motif known for mediating protein-protein interactions, often serving as a scaffold to assemble multiprotein complexes. TPRKB incorporates this domain alongside a kinase domain, suggesting its role in regulating phosphorylation-dependent signaling cascades.
Recombinant TPRKB is typically produced using expression systems like *E. coli* or mammalian cells, enabling large-scale purification for functional studies. Its design allows researchers to dissect mechanisms underlying cellular processes such as cell cycle regulation, stress responses, and DNA repair. For instance, TPRKB has been implicated in pathways involving chaperone proteins and kinases like Aurora B, which are critical for mitotic progression and genomic stability.
The protein’s modular structure—combining TPR-mediated binding and enzymatic activity—makes it a valuable tool for *in vitro* assays, drug screening, and structural biology. Studies using recombinant TPRKB have provided insights into how scaffold proteins coordinate signaling specificity and amplification. Additionally, dysregulation of TPR-containing proteins has been linked to cancers and neurodegenerative diseases, positioning TPRKB as a potential therapeutic target or biomarker.
Recent advances in recombinant technology, including codon optimization and fusion tags, have enhanced TPRKB’s solubility and activity, addressing challenges in studying large, multi-domain proteins. Ongoing research aims to map its interaction networks and validate its roles in disease models, bridging structural biology with translational applications.
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