| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLFN12L |
| Uniprot No | Q6IEE8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-588aa |
| 氨基酸序列 | MDLARKEFLRGNGLAAGKMNISIDLDTNYAELVLNVGRVTLGENNRKKMK DCQLRKQQNENVSRAVCALLNSGGGVIKAEVENKGYSYKKDGIGLDLENS FSNMLPFVPNFLDFMQNGNYFHIFVKSWSLETSGPQIATLSSSLYKRDVT SAKVMNASAALEFLKDMEKTGGRAYLRPEFPAKRACVDVQEESNMEALAA DFFNRTELGYKEKLTFTESTHVEIKNFSTEKLLQRITEILPQYVSAFANT DGGYLFVGLNEDKEVIGFKAEKSYLTKLEEVTKNSIGKLPVHHFCVEKGT INYLCKFLGVYDKGRLCGYVYALRVERFCCAVFAKKPDSWHVKDNRVKQL TEKEWIQFMVDSEPVCEELPSPASTSSPVSQSYPLREYINFKIQPLRYHL PGLSEKITCAPKTFCRNLFSQHEGLKQLICEEMGSVNKGSLIFSRSWSLD LGLQENHKVLCDALLISQDKPPVLYTFHMVQDEEFKDYSTQTAQTLKQKL AKIGGYTKKVCVMTKIFYLSPEGKTSCQYDLNSQVIYPESYYWTTAQTMK DLEKALSNILPKENQIFLFVCLFRFCLFVCWFVCFFLR |
| 预测分子量 | 72 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SLFN12L重组蛋白的假设性参考文献(基于Schlafen家族蛋白研究的常见方向概括，实际文献可能需要进一步验证)：
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1. **文献名称**：*"Recombinant SLFN12L inhibits viral replication by targeting RNA helicase activity"*
**作者**：Li, X. et al. (2018)
**摘要**：本研究成功表达并纯化了重组SLFN12L蛋白，发现其通过结合病毒RNA解旋酶抑制多种RNA病毒的复制，为抗病毒治疗提供了新靶点。
2. **文献名称**：*"Structural insights into the nucleic acid-binding domain of SLFN12L"*
**作者**：Zhang, Y. et al. (2020)
**摘要**：通过X射线晶体学解析了SLFN12L重组蛋白的核酸结合结构域，揭示了其与单链DNA/RNA相互作用的分子机制，表明其在基因组稳定性中的作用。
3. **文献名称**：*"SLFN12L recombinant protein enhances chemosensitivity in colorectal cancer cells"*
**作者**：Wang, H. et al. (2021)
**摘要**：研究发现重组SLFN12L蛋白可通过诱导细胞周期阻滞和凋亡，增强结肠癌细胞对化疗药物的敏感性，提示其潜在临床应用价值。
4. **文献名称**：*"SLFN12L interacts with ribosomes to regulate translation fidelity under stress conditions"*
**作者**：Chen, R. et al. (2022)
**摘要**：利用重组SLFN12L蛋白进行体外实验，证明其在应激条件下通过结合核糖体调控翻译保真度，可能参与细胞应激响应通路。
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注：SLFN12L的研究文献可能较少，以上内容基于Schlafen蛋白家族(如SLFN5、SLFN11)的典型研究方向推测。建议通过**PubMed**或**Google Scholar**以“SLFN12L recombinant”为关键词检索最新文献。
Schlafen family member 12-like (SLFN12L) is a relatively understudied protein belonging to the Schlafen (SLFN) gene family, which is evolutionarily conserved across mammals and implicated in cell differentiation, immune regulation, and tumor suppression. The SLFN family shares structural features including an N-terminal AAA ATPase domain and a C-terminal divergent region, though SLFN12L's exact domain architecture remains less defined compared to well-characterized members like SLFN5 or SLFN11. This protein is classified as a "long" Schlafen (>70 kDa) based on its predicted molecular weight, though its functional distinctions from paralogs remain unclear.
Recombinant SLFN12L protein refers to the genetically engineered form produced in heterologous expression systems (e.g., E. coli, mammalian cells) for functional studies. Its production addresses challenges in isolating native SLFN12L due to low endogenous expression levels and technical limitations in detecting Schlafen proteins. Preliminary evidence suggests SLFN12L may possess nucleic acid-binding or nuclease activity typical of Schlafen proteins, potentially influencing viral defense mechanisms or cell cycle arrest. Unlike SLFN11's established role in blocking DNA replication under stress, SLFN12L's specific molecular interactions and enzymatic properties require further validation.
Interest in recombinant SLFN12L stems from the Schlafen family's therapeutic relevance, particularly in oncology (chemosensitivity modulation) and virology (interferon-mediated antiviral responses). Structural characterization of the recombinant protein could clarify its regulatory mechanisms, such as potential phosphorylation sites or partnerships with immune signaling molecules like STAT1. Current research gaps include defining its subcellular localization patterns, post-translational modifications, and species-specific functional variations. Commercial availability of SLFN12L recombinant protein remains limited, underscoring the need for optimized expression protocols to support biochemical assays and antibody development.
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