| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOC155060 |
| Uniprot No | 0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-281aa |
| 活性数据 | MAEAAPARDPETDKHTEDQSPSTPLPQPAAEKNSYLYSTEITLWTVVAAIQALEKKVDSCLTRLLTLEGRTGTAEKKLADCEKTAVEFGNQLEGKWAVLGTLLQEYGLLQRRLENVENLLRNRNFWILRLPPGSKGEAPKVPVTFDDVAVYFSELEWGKLEDWQKELYKHVMRGNYETLVSLDYAISKPDILTRIERGEEPCLDRWGQEKGNEVEVGRPRMMGTGLPPYPEHLTSPLSPAQEELKEGQAPKQQQDSEARVAPAGPEAGLALRTDLQGEAQI |
| 分子量 | 57.8 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. |
以下是关于重组人LOC155060蛋白的示例文献(注：LOC155060为NCBI临时基因编号，相关研究较少，以下内容为模拟示例)：
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1. **文献名称**：重组人LOC155060蛋白的表达纯化及其抗炎功能研究
**作者**：Zhang L, et al.
**摘要**：本研究通过大肠杆菌系统成功表达重组人LOC155060蛋白，并优化纯化工艺。功能实验表明，该蛋白可通过抑制NF-κB通路显著减轻巨噬细胞炎症反应，提示其在炎症性疾病中的潜在应用价值。
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2. **文献名称**：LOC155060蛋白在肿瘤细胞凋亡中的作用机制
**作者**：Wang Y, et al.
**摘要**：研究利用HEK293细胞表达重组LOC155060蛋白，发现其可通过激活Caspase-3通路诱导结直肠癌细胞凋亡，并揭示其在肿瘤微环境中与p53蛋白的相互作用。
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3. **文献名称**：LOC155060蛋白的结构解析及其酶活性分析
**作者**：Chen R, et al.
**摘要**：通过X射线晶体学解析LOC155060蛋白的三维结构，确认其属于丝氨酸水解酶家族。酶活实验表明，重组蛋白对特定脂质底物具有水解活性，提示其可能参与脂代谢调控。
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**说明**：
- 实际研究中，"LOC155060"可能尚未有正式命名或公开功能数据，建议通过NCBI Gene或UniProt确认最新注释。
- 检索时可尝试关联其染色体定位(如**chrX:123456**)或同源基因，或使用临时编号结合关键词(如"recombinant LOC155060")在PubMed/Google Scholar筛选。
Recombinant human LOC155060 protein is a genetically engineered form of a protein encoded by the LOC155060 gene, which remains relatively understudied in current literature. The LOC155060 gene, located on human chromosome X (Xq28), is annotated to encode a protein of unknown function, though bioinformatics analyses suggest potential roles in cellular signaling or metabolic regulation. Structural predictions indicate it may contain conserved domains associated with protein-protein interactions, such as coiled-coil motifs or phosphorylation sites, but experimental validation is limited.
Interest in recombinant LOC155060 stems from its differential expression patterns observed in certain cancers and neurological disorders, hinting at pathological or therapeutic relevance. Recombinant production typically involves cloning the gene into expression vectors (e.g., E. coli, HEK293. or yeast systems) to enable large-scale purification via affinity tags (e.g., His-tag). This allows functional studies, including antibody development, interactome mapping, and screening for binding partners or inhibitors. Despite progress in production methods, the protein's precise biological mechanisms, physiological substrates, and disease connections remain unresolved, driving ongoing research to elucidate its molecular and therapeutic potential.
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