| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STYX |
| Uniprot No | Q8WUJ0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-223aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMEDVKL EFPSLPQCKE DAEEWTYPMR REMQEILPGL FLGPYSSAMK SKLPVLQKHG ITHIICIRQN IEANFIKPNF QQLFRYLVLD IADNPVENII RFFPMTKEFI DGSLQMGGKV LVHGNAGISR SAAFVIAYIM ETFGMKYRDA FAYVQERRFC INPNAGFVHQ LQEYEAIYLA KLTIQMMSPL QIERSLSVHS GTTGSLKRTH EEEDDFGTMQ VATAQNG |
| 预测分子量 | 28 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STYX重组蛋白的模拟参考文献示例(注：部分为假设性文献，实际引用需核实)：
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1. **文献名称**：*The Role of STYX Pseudophosphatase in MAPK Signaling Regulation*
**作者**：Wishart, M.J., Dixon, J.E.
**摘要**：研究揭示了STYX作为假磷酸酶通过结合MAPK通路中的关键蛋白(如ERK1/2)调控信号传导的机制，重组STYX蛋白实验表明其通过竞争性抑制影响细胞增殖与分化。
2. **文献名称**：*STYX Recombinant Protein Modulates Cell Cycle Progression in Cancer Cells*
**作者**：Smith, A.L., et al.
**摘要**：通过体外表达重组STYX蛋白，发现其干扰磷酸化依赖性蛋白降解，导致G1/S期转换阻滞，提示STYX可能通过调控泛素化通路抑制肿瘤生长。
3. **文献名称**：*Structural Insights into STYX Domain Interaction with Phosphorylated Substrates*
**作者**：Johnson, R.T., et al.
**摘要**：利用X射线晶体学解析了重组STYX蛋白与磷酸化肽段的复合物结构，阐明其假催化结构域如何模拟活性磷酸酶的底物结合，为设计靶向STYX的分子探针提供依据。
4. **文献名称**：*STYX Knockdown and Recombinant Rescue in Neuronal Development Models*
**作者**：Brown, K., et al.
**摘要**：在神经元细胞中敲低STYX导致轴突导向异常，而外源重组STYX蛋白可恢复信号通路功能，表明其在神经发育中通过调节RTK信号起关键作用。
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**注意**：以上文献为示例性质，实际研究中建议通过学术数据库(如PubMed、Web of Science)以“STYX recombinant protein”“STYX pseudophosphatase”等关键词检索最新论文。
**Background of STYX Recombinant Protein**
STYX (Serine/Threonine/Tyrosine Interacting Protein) is a pseudokinase belonging to the protein kinase superfamily. Unlike typical kinases, STYX lacks critical catalytic residues required for enzymatic activity, rendering it incapable of phosphorylating substrates. Instead, it functions as a regulatory molecule, modulating cellular signaling pathways by interacting with phosphorylated proteins or competing with active kinases and phosphatases.
The recombinant STYX protein is engineered through molecular cloning, enabling its production in heterologous systems like *E. coli* or mammalian cells. This allows for high-purity, scalable production for research purposes. Structurally, STYX retains a kinase-like domain but harbors mutations in the catalytic motif (e.g., substitution of the essential aspartate in the "HRD" motif), a hallmark of pseudokinases. These features facilitate its role as a scaffold or decoy in phosphorylation-dependent processes.
STYX is implicated in diverse cellular functions, including cell cycle regulation, apoptosis, and stress response. It interacts with mitogen-activated protein kinases (MAPKs), phosphatases (e.g., DUSPs), and components of the ubiquitin-proteasome system, influencing pathways like the ERK/MAPK cascade. Dysregulation of STYX has been linked to diseases such as cancer, neurodegenerative disorders, and metabolic syndromes, where aberrant phosphorylation signaling is a hallmark.
Recombinant STYX proteins are valuable tools for studying kinase-independent signaling mechanisms, identifying interaction partners, and screening therapeutic agents targeting pseudokinase-mediated pathways. Their use in structural studies (e.g., X-ray crystallography) has advanced understanding of pseudokinase architecture and allosteric regulation. By mimicking or disrupting STYX interactions, researchers aim to develop strategies for modulating pathological signaling networks.
In summary, STYX recombinant proteins provide insights into the regulatory roles of pseudokinases and their potential as therapeutic targets in diseases driven by signaling dysregulation.
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