| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FA |
| Uniprot No | P03951 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-625aa |
| 氨基酸序列 | MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV |
| 预测分子量 | 70,1 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. |
以下是为您整理的3篇与FA(范可尼贫血)重组蛋白相关的参考文献示例(注：文献信息为模拟创作，仅作格式参考)：
1. **《Recombinant FANCD2 Protein Purification and Functional Analysis in DNA Repair》**
- 作者：Smith J, et al.
- 摘要：研究通过大肠杆菌表达系统纯化FANCD2重组蛋白，验证其在范可尼贫血通路中对DNA交联损伤修复的功能，揭示其与FANCI蛋白的相互作用机制。
2. **《Expression of Functional FANCJ Helicase in Mammalian Cells for Gene Therapy Applications》**
- 作者：Chen L, et al.
- 摘要：开发哺乳动物细胞中高效表达FANCJ重组蛋白的方法，证明其在纠正范可尼贫血患者细胞中染色体不稳定性及增强化疗耐药性的潜在治疗价值。
3. **《Structural Insights into the FANCM-FAAP24 Complex by Cryo-EM》**
- 作者：Wang Y, et al.
- 摘要：利用冷冻电镜解析FANCM-FAAP24重组蛋白复合体的三维结构，阐明该复合体在范可尼贫血核心复合体组装及DNA损伤响应中的构效关系。
**说明**：以上文献为模拟示例，实际研究中请通过PubMed、Web of Science等平台检索真实发表的文献，关键词建议使用"Fanconi anemia recombinant protein"或结合具体蛋白名称(如FANCD2、FANCA等)。
**Background of FA Recombinant Proteins**
Fanconi anemia (FA) is a rare genetic disorder characterized by genomic instability, bone marrow failure, and cancer predisposition. It is caused by mutations in genes encoding proteins of the FA pathway, which coordinates DNA interstrand crosslink (ICL) repair. The FA core complex, comprising proteins such as FANCA, FANCB, and FANCC, functions as an E3 ubiquitin ligase responsible for monoubiquitinating FANCD2 and FANCI. This modification recruits downstream repair effectors to stalled replication forks, enabling homologous recombination (HR)-mediated repair.
Recombinant FA proteins are engineered using heterologous expression systems (e.g., *E. coli*, mammalian cells) to study their biochemical and structural roles. These proteins enable *in vitro* reconstitution of FA pathway activities, such as ubiquitination, DNA binding, and interactions with repair intermediates. For example, recombinant FANCD2-FANCI complexes have been critical in elucidating how monoubiquitination activates their function in ICL repair.
FA recombinant proteins also aid in modeling disease-associated mutations. By introducing pathogenic variants into recombinant constructs, researchers assess their impact on protein stability, post-translational modifications, and repair capacity. This approach has identified hypomorphic mutations that partially disrupt FA pathways, correlating with milder clinical phenotypes.
Furthermore, these proteins are tools for drug discovery. High-throughput screens using recombinant FA components aim to identify compounds that restore pathway activity in FA-deficient cells or exploit synthetic lethal interactions in cancers. Structural studies of recombinant FA complexes (e.g., FANCL-UBE2T) have guided the design of small-molecule inhibitors targeting ubiquitination enzymes.
In summary, FA recombinant proteins are pivotal for dissecting DNA repair mechanisms, understanding FA pathogenesis, and developing therapeutic strategies for FA and related cancers. Their application bridges molecular insights with translational research, highlighting the FA pathway’s broader relevance in genome maintenance.
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