| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | yihF |
| Uniprot No | P32128 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-476aa |
| 氨基酸序列 | GTQIQPGVEKFIKDFNDAKKKGEHAYDMTLSYQNFDKGFFNSRFQMQMTFDNGAPDLNIKPGQKVVFDVDVEHGPLPITMLMHGNVIPALAAAKVNLVNNELTQPLFIAAKNKSPVEATLRFAFGGSFSTTLDVAPAEYGKFSFGEGQFTFNGDGSSLSNLDIEGKVEDIVLQLSPMNKVTAKSFTIDSLARLEEKKFPVGESESKFNQINIINHGEDVAQIDAFVAKTRLDRVKDKDYINVNLTYELDKLTKGNQQLGSGEWSLIAESIDPSAVRQFIIQYNIAMQKQLAAHPELANDEVALQEVNAALFKEYLPLLQKSEPTIKQPVRWKNALGELNANLDISIADPAKSSSSTNKDIKSLNFDVKLPLNVVTETAKQLNLSEGMDAEKAQKQADKQISGMMTLGQMFQLITIDNNTASLQLRYTPGKVVFNGQEMSEEEFMSRAGRFVH |
| 预测分子量 | 66.1 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yihF重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Structural and functional analysis of the Escherichia coli YihF protein"
**作者**: Zhang Y. et al.
**摘要**: 研究通过重组表达纯化了大肠杆菌YihF蛋白，并解析其晶体结构，发现其具有类GTP酶结构域，可能在核糖体功能或应激响应中发挥作用。
2. **文献名称**: "Characterization of YihF as a stress-responsive ribosome-associated GTPase"
**作者**: Smith J.L. et al.
**摘要**: 利用重组YihF蛋白进行功能研究，发现其在氧化应激条件下与核糖体结合增强，可能通过调控翻译效率参与细菌逆境适应。
3. **文献名称**: "Functional interplay between YihF and ribosome biogenesis in Salmonella"
**作者**: Lee S. & Kim H.
**摘要**: 通过重组YihF蛋白的体外实验，证实其与核糖体亚基的相互作用，并揭示其在沙门氏菌核糖体组装中的潜在调控作用。
4. **文献名称**: "YihF/RsfA: A conserved GTPase with atypical enzymatic activity"
**作者**: Brown D.R. et al.
**摘要**: 研究重组YihF的酶学特性，发现其虽具有GTP酶结构域，但催化活性显著低于典型GTP酶，推测其可能通过构象变化而非水解作用发挥功能。
(注：以上文献信息为示例性概括，实际文献需通过数据库检索确认)
**Background of YihF Recombinant Protein**
The yihF gene, conserved across bacteria, encodes a GTP-binding protein belonging to the TRAFAC (translation factor-related) class of GTPases. Initially identified in *Escherichia coli*, YihF is implicated in stress adaptation, biofilm formation, and cellular homeostasis. While its precise molecular role remains under investigation, YihF is suggested to interact with ribosomes or translation machinery, potentially modulating protein synthesis under stress conditions. Studies link yihF deletion to increased antibiotic susceptibility, altered cell morphology, and impaired persister cell formation, highlighting its importance in bacterial survival strategies.
Recombinant YihF protein production enables detailed structural and functional studies. Using genetic engineering, the yihF gene is cloned into expression vectors, overexpressed in bacterial hosts (e.g., *E. coli*), and purified via affinity chromatography. This approach provides high-purity protein for crystallography, biochemical assays, and interaction studies. For instance, structural analyses reveal YihF’s GTPase domain architecture and nucleotide-binding motifs, offering insights into its regulatory mechanisms.
Research on YihF also explores its potential as a therapeutic target. By disrupting its GTPase activity or stress-response role, novel antimicrobials could be developed to combat resistant infections. Additionally, YihF homologs in pathogens like *Salmonella* and *Pseudomonas* underscore its broader relevance in microbial physiology.
Despite progress, knowledge gaps persist, particularly regarding YihF’s specific substrates and regulatory networks. Recombinant protein tools remain critical for deciphering its role in bacterial adaptation and virulence, positioning YihF as a focal point in both basic microbiology and applied drug discovery research.
×
