| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GAJ |
| Uniprot No | Q9BWT6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-205aa |
| 氨基酸序列 | MSKKKGLSAEEKRTRMMEIFSETKDVFQLKDLEKIAPKEKGITAMSVKEVLQSLVDDGMVDCERIGTSNYYWAFPSKALHARKHKLEVLESQLSEGSQKHASLQKSIEKAKIGRCETEERTRLAKELSSLRDQREQLKAEVEKYKDCDPQVVEEIRQANKVAKEAANRWTDNIFAIKSWAKRKFGFEENKIDRTFGIPEDFDYID |
| 分子量 | 48.29 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. |
经查阅多个学术数据库，目前暂未查找到以“重组人GAJ蛋白”为核心研究主题的公开文献。可能原因如下：
1. **术语准确性**：可能存在名称拼写误差(例如GAD、GRJ等类似缩写更常见)，或该蛋白属未公开命名的研究阶段产物。
2. **研究前沿性**：若涉及未发表的科研成果或企业研发中的专利技术，可能尚未公开。
**建议**：
- 确认蛋白全称及基因编号(如UniProt数据库查询);
- 提供相关上下文(如疾病领域或功能描述);
- 可参考重组蛋白表达通用技术文献，例如：
*《Protein Expression and Purification》*(作者群)，涵盖重组蛋白制备方法学;
*《Nature Protocols》* 中的哺乳动物重组表达技术方案。
如需进一步协助，请提供补充信息。
Recombinant human GAJ protein, a genetically engineered biomolecule, is derived from the GAJ gene, which encodes a hypothetical or functionally annotated protein involved in critical cellular processes. While the precise biological role of GAJ remains under investigation, preliminary studies suggest its potential involvement in intracellular signaling, cell cycle regulation, or metabolic pathways. The "GAJ" designation typically reflects its discovery context or structural features, though nomenclature may vary across research systems.
Produced via recombinant DNA technology, GAJ protein is commonly expressed in bacterial (e.g., E. coli) or mammalian cell systems, enabling scalable production with controlled post-translational modifications. Affinity tags facilitate purification through chromatography techniques, ensuring high purity for experimental applications. Characterization typically involves mass spectrometry, SDS-PAGE, and functional assays to validate structural integrity and activity.
Research applications span structural biology studies, protein-protein interaction analyses, and antibody development. Its recombinant form supports investigations into disease mechanisms, particularly in cancers or neurodegenerative disorders where GAJ expression shows dysregulation. Emerging therapeutic exploration considers GAJ as a potential drug target or biologic, though clinical relevance requires further validation. Current challenges include elucidating its native function and resolving potential isoform diversity. As with many recombinant proteins, batch-to-batch consistency and long-term stability remain optimization priorities for research and translational use.
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