| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Fam111a |
| Uniprot No | Q96PZ2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-611aa |
| 氨基酸序列 | MSCKKQRSRKHSVNEKCNMKIEHYFSPVSKEQQNNCSTSLMRMESRGDPR ATTNTQAQRFHSPKKNPEDQTMPQNRTIYVTLKVNHRRNQDMKLKLTHSE NSSLYMALNTLQAVRKEIETHQGQEMLVRGTEGIKEYINLGMPLSCFPEG GQVVITFSQSKSKQKEDNHIFGRQDKASTECVKFYIHAIGIGKCKRRIVK CGKLHKKGRKLCVYAFKGETIKDALCKDGRFLSFLENDDWKLIENNDTIL ESTQPVDELEGRYFQVEVEKRMVPSAAASQNPESEKRNTCVLREQIVAQY PSLKRESEKIIENFKKKMKVKNGETLFELHRTTFGKVTKNSSSIKVVKLL VRLSDSVGYLFWDSATTGYATCFVFKGLFILTCRHVIDSIVGDGIEPSKW ATIIGQCVRVTFGYEELKDKETNYFFVEPWFEIHNEELDYAVLKLKENGQ QVPMELYNGITPVPLSGLIHIIGHPYGEKKQIDACAVIPQGQRAKKCQER VQSKKAESPEYVHMYTQRSFQKIVHNPDVITYDTEFFFGASGSPVFDSKG SLVAMHAAGFAYTYQNETRSIIEFGSTMESILLDIKQRHKPWYEEVFVNQ QDVEMMSDEDL |
| 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. |
以下是关于Fam111a重组蛋白的3篇参考文献(示例为虚构内容，仅供格式参考)：
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1. **Title**: *Structural and Functional Analysis of FAM111A Recombinant Protein in DNA Repair*
**Authors**: Smith J.R., Tanaka A., Lee C.
**摘要**: 本研究通过重组表达纯化FAM111A蛋白，解析其晶体结构，揭示了其核酸酶活性结构域。实验表明FAM111A通过水解单链DNA参与DNA损伤修复，突变体实验证明其活性缺失导致细胞对辐射敏感性增加。
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2. **Title**: *FAM111A Recombinant Protein Interaction with Viral Helicase in Host-pathogen Conflict*
**Authors**: Gonzalez L.M., Zhang Q., Patel S.
**摘要**: 利用重组FAM111A蛋白进行体外互作实验，发现其直接结合多种病毒解旋酶(如SV40 T抗原)。研究提出FAM111A可能通过干扰病毒DNA复制发挥宿主防御功能，为抗病毒治疗提供新靶点。
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3. **Title**: *Dysregulated FAM111A Recombinant Protease Activity in Fibrosis Pathogenesis*
**Authors**: Chen X., Wang H., Ito M.
**摘要**: 通过重组蛋白活性筛选，发现FAM111A具有金属蛋白酶特性，并在肺纤维化模型中异常激活。抑制其活性可减少胶原沉积，提示FAM111A可能成为纤维化疾病的新型治疗靶标。
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注：以上文献为模拟内容，实际研究中建议通过PubMed或Web of Science检索关键词“FAM111A recombinant protein”获取真实文献。
**Background of FAM111A Recombinant Protein**
FAM111A (family with sequence similarity 111 member A) is a nuclear protein encoded by the *FAM111A* gene, located on human chromosome 11q12.1. It contains a conserved trypsin-like cysteine/serine peptidase domain, though its enzymatic activity remains debated. Structurally, FAM111A features a C-terminal domain critical for interactions with proliferating cell nuclear antigen (PCNA), a key player in DNA replication and repair. This interaction suggests its involvement in DNA damage response pathways or replication stress management.
Functionally, FAM111A has been implicated in restricting the replication of certain viruses, such as vaccinia virus, by targeting viral DNA polymerase processivity factors. Mutations in *FAM111A* are linked to hereditary fibrosing poikiloderma (HFP), a rare autosomal dominant disorder characterized by skin abnormalities, tendon contractures, and pulmonary fibrosis. These pathogenic variants (e.g., p.Arg569His) likely confer gain-of-function or dominant-negative effects, disrupting normal protein function. Notably, dysregulated FAM111A expression is also observed in cancers, including pancreatic ductal adenocarcinoma, where it may promote tumor progression through unclear mechanisms.
Recombinant FAM111A protein, typically produced in bacterial or mammalian expression systems, enables biochemical and structural studies to dissect its molecular roles. Researchers utilize it to analyze interactions (e.g., with PCNA or viral proteins), assess enzymatic activity, and model disease-associated mutations. Such studies aim to clarify FAM111A's contribution to genomic stability, antiviral defense, and disease pathogenesis, potentially informing therapeutic strategies for HFP or cancers. Despite progress, its precise physiological substrates and regulatory mechanisms remain under investigation, highlighting the need for further functional characterization.
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