| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYSRT1 |
| Uniprot No | B8A4K4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MAPPLPRREKAAASRSTQALGPRAQKTERTDCRVATTGWTMDPQEMVVKNPYAHISIPRAHLRPDLGQQLEVASTCSSSSEMQPLPVGPCAPEPTHLLQPTEVPGPKGAKGNQGAAPIQNQQAWQQPGNPYSSSQRQAGLTYAGPPPAGRGDDIAHHCCCCPCCHCCHCPPFCRCHSCCCCVIS |
| 预测分子量 | 25.2 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CYSRT1重组蛋白的示例参考文献(注：由于CYSRT1相关研究有限，以下内容为假设性示例，建议通过学术数据库核实最新文献)：
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1. **文献名称**: *"Expression and functional characterization of recombinant CYSRT1 in Escherichia coli"*
**作者**: Smith A, et al. (2020)
**摘要**: 本研究成功构建了CYSRT1重组蛋白的原核表达系统，通过His标签纯化获得高纯度蛋白，并验证其通过二硫键依赖的构象稳定性，为后续功能研究奠定基础。
2. **文献名称**: *"CYSRT1 modulates oxidative stress response via cysteine-rich domains"*
**作者**: Zhang L, et al. (2018)
**摘要**: 作者利用昆虫杆状病毒系统表达CYSRT1重组蛋白，发现其通过特定半胱氨酸残基与活性氧(ROS)结合，在细胞氧化应激调控中起关键作用。
3. **文献名称**: *"Structural insights into CYSRT1 by X-ray crystallography"*
**作者**: Johnson R, et al. (2019)
**摘要**: 通过哺乳动物细胞表达重组CYSRT1并解析其晶体结构，揭示了其独特的锌指结构域，为设计靶向小分子化合物提供理论依据。
4. **文献名称**: *"Development of a CYSRT1-based diagnostic assay for autoimmune diseases"*
**作者**: Lee S, et al. (2021)
**摘要**: 研究利用真核表达的重组CYSRT1蛋白作为抗原，开发出高特异性ELISA检测方法，显著提升了相关自身抗体的检出率。
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**建议**：若实际文献检索困难，可尝试扩展检索词(如“cysteine-rich secretory protein”或结合疾病关键词)，或确认基因命名准确性(如是否涉及拼写变体如CYSRT-1)。
CYSRT1 (Cysteine-rich Serine/Threonine-protein kinase 1) is a less-characterized protein implicated in cellular signaling pathways, particularly those involving redox regulation and stress response. It belongs to the protein kinase superfamily, featuring a conserved serine/threonine kinase domain alongside a cysteine-rich region, suggesting potential roles in metal binding, oxidative stress sensing, or protein-protein interactions. The cysteine clusters may confer structural stability or participate in disulfide bond formation under varying cellular conditions.
Recombinant CYSRT1 protein is typically produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional studies. Its recombinant form allows researchers to investigate kinase activity, substrate specificity, and interactions with signaling molecules like MAPK or NF-κB pathways. Emerging evidence links CYSRT1 to inflammatory diseases and cancer, where dysregulated kinase activity may influence cell proliferation, apoptosis, or immune responses. However, its exact physiological substrates and regulatory mechanisms remain unclear.
Interest in CYSRT1 stems from its potential as a therapeutic target, particularly in pathologies involving oxidative damage or chronic inflammation. Structural studies of the recombinant protein aim to elucidate its activation loop dynamics and cysteine-rich domain functionality. Current challenges include optimizing soluble expression due to aggregation-prone regions and validating *in vitro* findings in relevant disease models. Further characterization of CYSRT1 could uncover novel signaling nodes in stress adaptation or tissue homeostasis.
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