| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RIFK |
| Uniprot No | Q969G6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-155aa |
| 氨基酸序列 | MRHLPYFCRG QVVRGFGRGS KQLGIPTANF PEQVVDNLPA DISTGIYYGW ASVGSGDVHK MVVSIGWNPY YKNTKKSMET HIMHTFKEDF YGEILNVAIV GYLRPEKNFD SLESLISAIQ GDIEEAKKRL ELPEHLKIKE DNFFQVSKSK IMNGH |
| 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. |
| 生物活性 | Measured by its ability to combine with the substrate ATP and riboflavin reaction produces the ADP ability to measure. The specific activity is 3681.943 pmoL/min/μg, as measured under the described conditions. |
以下是关于RIFK重组蛋白的假设性参考文献示例(注：RIFK蛋白名称可能存在拼写或术语差异，建议核实具体名称)：
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1. **标题**：Expression and Purification of Recombinant RIFK Protein in *E. coli*
**作者**：Smith A, et al.
**摘要**：研究报道了在大肠杆菌系统中高效表达RIFK重组蛋白的方法，通过优化诱导条件和亲和层析技术获得高纯度蛋白，为后续功能研究奠定基础。
2. **标题**：Structural Characterization of RIFK and Its Role in Cellular Signaling
**作者**：Johnson L, et al.
**摘要**：通过X射线晶体学解析RIFK蛋白的三维结构，揭示其与激酶结构域的相互作用，提出其在细胞凋亡信号通路中的潜在调控机制。
3. **标题**：RIFK Recombinant Protein Enhances Antiviral Immune Response *In Vivo*
**作者**：Wang Y, et al.
**摘要**：在小鼠模型中验证了RIFK重组蛋白通过激活TLR通路增强抗病毒免疫应答的效果，为疫苗佐剂开发提供实验依据。
4. **标题**：Functional Analysis of RIFK in Cancer Cell Metastasis
**作者**：Chen R, et al.
**摘要**：体外实验表明，RIFK重组蛋白可通过抑制MMP-9表达显著降低肿瘤细胞的迁移和侵袭能力，提示其作为抗癌靶点的潜力。
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建议根据实际研究方向，在PubMed或Google Scholar中检索更准确的文献(如替换为“RIF1”或“重组干扰素”等关键词)。
**Background of RIFK Recombinant Protein**
Recombinant proteins, such as RIFK, are engineered through genetic modification to express specific protein sequences in host organisms like *E. coli*, yeast, or mammalian cells. RIFK, a synthetic or modified variant of a naturally occurring protein, is designed to enhance stability, solubility, or functional properties for research or therapeutic applications. Its development often stems from the need to study protein interactions, signaling pathways, or immune responses in controlled experimental settings.
The design of RIFK typically involves cloning the target gene into an expression vector, followed by transfection into a host system for large-scale production. Advanced purification techniques, such as affinity chromatography, ensure high purity and bioactivity. RIFK may incorporate tags (e.g., His-tag, FLAG-tag) to facilitate detection or purification.
In research, RIFK is utilized to investigate molecular mechanisms in diseases like cancer, autoimmune disorders, or infections. For instance, if RIFK mimics a cytokine or receptor, it could be used to study cell signaling or block pathogenic pathways. In therapeutics, recombinant proteins like RIFK hold promise as biologics, offering targeted treatments with fewer side effects compared to small-molecule drugs.
Challenges in RIFK production include maintaining proper folding, post-translational modifications (if using eukaryotic hosts), and scalability. Innovations in synthetic biology and bioprocessing continue to optimize yields and functionality.
Overall, RIFK represents a critical tool in both basic science and translational medicine, bridging the gap between molecular discovery and clinical applications. Its versatility underscores the growing importance of recombinant protein technology in addressing complex biological questions and advancing personalized therapies.
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