| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | bsk |
| Uniprot No | P92208 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-372aa |
| 氨基酸序列 | MTTAQHQHYTVEVGDTNFTIHSRYINLRPIGSGAQGIVCAAYDTITQQNVAIKKLSRPFQNVTHAKRAYREFKLMKLVNHKNIIGLLNAFTPQRNLEEFQDVYLVMELMDANLCQVIQMDLDHDRMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKADCTLKILDFGLARTAGTTFMMTPYVVTRYYRAPEVILGMGYTENVDIWSVGCIMGEMIRGGVLFPGTDHIDQWNKIIEQLGTPSPSFMQRLQPTVRNYVENRPRYTGYSFDRLFPDGLFPNDNNQNSRRKASDARNLLSKMLVIDPEQRISVDEALKHEYINVWYDAEEVDAPAPEPYDHSVDEREHTVEQWKELIYEEVMDYEAHNTNNRTR |
| 预测分子量 | 47.0 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BSK重组蛋白研究的示例参考文献(注：以下为模拟示例，非真实文献，仅供格式参考)：
1. **文献名称**：Brassinosteroid Signaling Kinase 1 (BSK1) 的重组表达及功能分析
**作者**：Li X, et al.
**摘要**：本研究在大肠杆菌系统中成功表达并纯化了拟南芥BSK1重组蛋白，通过体外激酶实验证实其磷酸化活性，揭示了BSK1在油菜素类固醇信号传导中的关键调控作用。
2. **文献名称**：重组BSK3蛋白与BRI1受体的相互作用研究
**作者**：Wang Y, et al.
**摘要**：利用昆虫细胞表达系统制备重组BSK3蛋白，结合Pull-down实验和质谱分析，发现BSK3直接与BRI1受体胞内域结合，阐明了其在早期信号转导中的分子机制。
3. **文献名称**：BSK家族蛋白的结构解析与进化分析
**作者**：Zhang H, et al.
**摘要**：通过X射线晶体学解析了BSK5重组蛋白的三维结构，发现其激酶结构域具有独特的自抑制模体，为设计植物激素信号通路调控剂提供了结构基础。
4. **文献名称**：重组BSK蛋白在植物抗病反应中的功能验证
**作者**：Chen J, et al.
**摘要**：在毕赤酵母中高效表达BSK2重组蛋白，体内实验表明其通过磷酸化下游转录因子增强植物对病原菌的免疫响应，拓展了BSK蛋白的功能多样性研究。
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如需真实文献，建议通过PubMed、Web of Science或Google Scholar检索关键词："BSK recombinant protein"、"Brassinosteroid Signaling Kinase expression"。近年研究多聚焦于BSK蛋白的结构、信号通路及农业应用。
BSK (BRI1 SUPPRESSOR KINASE) proteins are a subgroup of receptor-like cytoplasmic kinases (RLCKs) in plants, primarily studied in the model organism *Arabidopsis thaliana*. They play a critical role in brassinosteroid (BR) signaling, a phytohormone pathway essential for plant growth, development, and stress responses. BSKs act as positive regulators downstream of the BR receptor BRI1 (BRASSINOSTEROID INSENSITIVE 1). Upon BR perception, BRI1 phosphorylates BSKs, initiating a signaling cascade that ultimately deactivates transcriptional repressors like BIN2 (BRASSINOSTEROID-INSENSITIVE 2), allowing transcription factors such as BZR1 (BRASSINAZOLE-RESISTANT 1) to regulate target genes involved in cell elongation, division, and differentiation.
Recombinant BSK proteins are engineered using heterologous expression systems (e.g., *E. coli* or insect cells) to study their biochemical properties and interaction networks. These proteins retain kinase activity and serve as tools to dissect BR signaling mechanisms in vitro, including phosphorylation events, substrate specificity, and crosstalk with other pathways. Structural studies of recombinant BSKs have provided insights into their activation loop dynamics and substrate-binding regions.
Beyond basic research, BSK recombinant proteins hold agricultural potential. Modulating BR signaling via BSK manipulation could enhance crop stress tolerance (e.g., drought, salinity) or improve yield traits. However, functional redundancy among BSK family members (12 isoforms in *Arabidopsis*) complicates their application, necessitating isoform-specific studies. Current efforts focus on optimizing recombinant production for high-throughput screening of kinase inhibitors or activators, aiming to develop BR pathway-targeted agrochemicals.
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