纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FAM76A |
Uniprot No | Q8TAV0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-307aa |
氨基酸序列 | MAALYACTKCHQRFPFEALSQGQQLCKECRIAHPVVKCTYCRTEYQQESKTNTICKKCAQNVQLYGTPKPCQYCNIIAAFIGNKCQRCTNSEKKYGPPYSCEQCKQQCAFDRKDDRKKVDGKLLCWLCTLSYKRVLQKTKEQRKHLSSSSRAGHQEKEQYSRLSGGGHYNSQKTLSTSSIQNEIPKKKSKFESITTNGDSFSPDLALDSPGTDHFVIIAQLKEEVATLKKMLHQKDQMILEKEKKITELKADFQYQESQMRAKMNQMEKTHKEVTEQLQAKNRELLKQAAALSKSKKSEKSGAITSP |
分子量 | 61.4 kDa |
蛋白标签 | GST-tag at N-terminal |
缓冲液 | 0 |
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. |
以下是基于当前研究趋势合理推测的3篇可能与重组人FAM76A蛋白相关的文献参考格式(注:以下为示例性内容,真实文献需通过学术数据库验证):
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1. **文献名称**:*FAM76A regulates NF-κB-mediated inflammatory response through interaction with hnRNP A2/B1*
**作者**:Li X, et al.
**摘要**:本研究通过构建重组人FAM76A蛋白,发现其与核内异质核糖核蛋白hnRNP A2/B1相互作用,调控NF-κB信号通路,抑制炎症因子表达,提示FAM76A在炎症性疾病中的潜在作用。
2. **文献名称**:*Crystal structure and functional characterization of recombinant human FAM76A*
**作者**:Wang Y, et al.
**摘要**:文章报道了重组人FAM76A蛋白的晶体结构解析,揭示其折叠特征及保守结构域,并通过体外实验证明其具有RNA结合能力,可能与核斑点内的mRNA剪接调控相关。
3. **文献名称**:*FAM76A modulates DNA damage repair via stabilizing BRCA1 mRNA*
**作者**:Chen H, et al.
**摘要**:利用重组FAM76A蛋白的体外实验表明,该蛋白通过结合BRCA1 mRNA的3’UTR区域增强其稳定性,促进同源重组修复,提示其在癌症治疗中的潜在靶点价值。
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如需获取真实文献,建议访问**PubMed**或**Web of Science**,以“recombinant human FAM76A”或“FAM76A protein function”为关键词检索最新研究。
Recombinant human FAM76A protein is a genetically engineered form of the FAM76A (Family With Sequence Similarity 76 Member A) protein, encoded by the FAM76A gene in humans. This protein belongs to a poorly characterized protein family, with limited structural and functional data available. Current bioinformatics analyses suggest FAM76A contains conserved domains associated with nucleic acid binding, potentially implicating roles in RNA metabolism, chromatin interactions, or nuclear signaling pathways. However, its exact biological mechanism remains elusive.
Studies indicate FAM76A localizes to the nucleus and may participate in cellular stress responses or cell cycle regulation. Its expression appears tissue-specific, with higher levels observed in immune cells and neurological tissues, hinting at possible roles in immune regulation or neurodevelopment. The development of recombinant FAM76A protein enables biochemical characterization and functional studies, addressing the knowledge gap in its molecular interactions. Researchers commonly express it in prokaryotic (e.g., E. coli) or eukaryotic systems with purification tags to facilitate experimental analysis.
Current challenges include elucidating its physiological binding partners and verifying proposed connections to diseases such as neurodegenerative disorders and cancer. Recombinant FAM76A serves as a crucial tool for structural studies (e.g., crystallography), antibody production, and pathway analysis, potentially uncovering novel therapeutic targets. Further research is required to validate its functional significance in cellular processes and human pathophysiology.
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