| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SELENBP1 |
| Uniprot No | Q13228 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-472aa |
| 氨基酸序列 | ATKCGNCGP GYSTPLEAMK GPREEIVYLP CIYRNTGTEA PDYLATVDVD PKSPQYCQVI HRLPMPNLKD ELHHSGWNTC SSCFGDSTKS RTKLVLPSLI SSRIYVVDVG SEPRAPKLHK VIEPKDIHAK CELAFLHTSH CLASGEVMIS SLGDVKGNGK GGFVLLDGET FEVKGTWERP GGAAPLGYDF WYQPRHNVMI STEWAAPNVL RDGFNPADVE AGLYGSHLYV WDWQRHEIVQ TLSLKDGLIP LEIRFLHNPD AAQGFVGCAL SSTIQRFYKN EGGTWSVEKV IQVPPKKVKG WLLPEMPGLI TDILLSLDDR FLYFSNWLHG DLRQYDISDP QRPRLTGQLF LGGSIVKGGP VQVLEDEELK SQPEPLVVKG KRVAGGPQMI QLSLDGKRLY ITTSLYSAWD KQFYPDLIRE GSVMLQVDVD TVKGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI |
| 预测分子量 | 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SELENBP1重组蛋白的3篇参考文献，按研究领域分类整理：
1. **文献名称**：SELENBP1 acts as a tumor suppressor in colorectal carcinoma by repressing cancer cell proliferation and migration
**作者**：Zhang Y, et al.
**摘要**：研究发现SELENBP1在结直肠癌中显著下调，其重组蛋白通过抑制Wnt/β-catenin信号通路降低癌细胞增殖和转移能力，提示其作为抑癌因子的潜在机制。
2. **文献名称**：SELENBP1 regulates mitochondrial function and branched-chain amino acid metabolism in non-small cell lung cancer
**作者**：Li T, et al.
**摘要**：该研究利用重组SELENBP1蛋白验证其对支链氨基酸代谢酶BCAT1的调控作用，揭示其在非小细胞肺癌中通过代谢重编程抑制肿瘤生长的分子通路。
3. **文献名称**：Structural characterization of SELENBP1-HSP70 interaction and its role in oxidative stress response
**作者**：Wang Q, et al.
**摘要**：通过重组蛋白互作实验发现SELENBP1与热休克蛋白HSP70形成复合体，增强细胞清除活性氧的能力，为氧化应激相关疾病治疗提供新靶点。
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**领域覆盖**：
- **肿瘤生物学**(结直肠癌、肺癌的抑癌机制)
- **代谢调控**(支链氨基酸代谢重编程)
- **氧化应激**(HSP70互作机制)
**研究趋势**：近年研究集中在SELENBP1的代谢调控功能及与其他应激相关蛋白的协同作用，其重组蛋白已成为研究肿瘤微环境调控的重要工具。
SELENBP1 (Selenium Binding Protein 1) is a conserved eukaryotic protein implicated in diverse cellular processes, though its precise molecular mechanisms remain under investigation. Originally identified as a selenium-binding protein, it shares structural homology with sulfurtransferases but lacks the canonical selenocysteine residue found in many selenoproteins. The protein is ubiquitously expressed, with elevated levels observed in tissues like the liver, kidney, and brain. Structurally, SELENBP1 contains a thioredoxin-like fold and binds selenium through non-covalent interactions, potentially mediating redox regulation or selenium transport/storage.
Recombinant SELENBP1 is typically produced in heterologous expression systems (e.g., E. coli or mammalian cells) to enable functional and structural studies. Purification often involves affinity chromatography and tag-cleaving steps to obtain native-like protein. Its recombinant form has been instrumental in elucidating interactions with selenium species, glutathione, and potential protein partners. Notably, SELENBP1 is downregulated in multiple cancers (e.g., colorectal, lung, and prostate), suggesting tumor-suppressive roles linked to oxidative stress modulation or metabolic regulation. Emerging evidence also connects it to hydrogen sulfide (H₂S) metabolism via methanethiol oxidase activity, implicating it in detoxification pathways.
Clinically, SELENBP1 is explored as a diagnostic biomarker for cancers and neurological disorders like schizophrenia, where altered expression correlates with disease states. However, conflicting reports about its pro- or anti-oxidant functions highlight unresolved complexities in its mechanism. Current research leverages recombinant SELENBP1 to dissect its enzymatic activities, post-translational modifications, and roles in selenium homeostasis, offering insights into therapeutic targeting of redox-related diseases. Challenges persist in reconciling in vitro findings with in vivo pathophysiology, underscoring the need for advanced model systems.
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