| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELSPBP1 |
| Uniprot No | Q96BH3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-223aa |
| 氨基酸序列 | MTRWSSYLLGWTTFLLYSYESSGGMHEECVFPFTYKGSVYFTCTHIHSLSPWCATRAVYNGQWKYCQSEDYPRCIFPFIYRGKAYNSCISQGSFLGSLWCSVTSVFDEKQQWKFCETNEYGGNSLRKPCIFPSIYRNNVVSDCMEDESNKLWCPTTENMDKDGKWSFCADTRISALVPGFPCHFPFNYKNKNYFNCTNKGSKENLVWCATSYNYDQDHTWVYC |
| 分子量 | 50.27 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ELSPBP1蛋白的参考文献示例(虚构内容，仅供参考)：
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1. **标题**: *重组人ELSPBP1蛋白的克隆表达及其与生殖功能的关联*
**作者**: Smith J, et al.
**摘要**: 本研究通过大肠杆菌表达系统成功制备了重组人ELSPBP1蛋白，并验证其在精子成熟过程中与脂质转运的关键作用。Western blot分析显示，该蛋白在人类附睾液中的高表达水平。
2. **标题**: *ELSPBP1的晶体结构揭示其脂质结合域的独特构象*
**作者**: Wang L, et al.
**摘要**: 首次解析了重组ELSPBP1蛋白的晶体结构，揭示了其N端脂质结合域的三维构象。研究通过体外结合实验证实其与花生四烯酸的特异性互作，提示其在炎症调控中的潜在功能。
3. **标题**: *重组ELSPBP1在肿瘤细胞迁移中的功能研究*
**作者**: Garcia R, et al.
**摘要**: 通过体外细胞实验发现，重组ELSPBP1可显著抑制乳腺癌细胞的迁移能力。机制研究表明，该蛋白通过调控Integrin信号通路发挥抗转移作用。
4. **标题**: *ELSPBP1基因缺失模型及其对雄性生育力的影响*
**作者**: Tanaka K, et al.
**摘要**: 利用重组ELSPBP1蛋白制备抗体，构建基因敲除小鼠模型。实验表明，ELSPBP1缺失导致精子活力下降，证实其对男性生育力的必要性。
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**说明**：上述文献为模拟示例，实际研究中可能需通过PubMed或Web of Science等平台检索真实文献(如确存在ELSPBP1蛋白)。若搜索无果，建议检查拼写(如是否为“HEL-S-1”或类似蛋白别名)，或关注其同源家族蛋白(如脂质结合蛋白家族)的相关研究。
**Recombinant human ELSPBP1 (Epididymal Luminal Secretory Protein Binding Protein 1)** is a protein of interest in reproductive biology and cancer research. Primarily expressed in the epididymis, ELSPBP1 is implicated in sperm maturation and function by binding to luminal secretory proteins, potentially influencing sperm capacitation or motility. Its role extends beyond reproduction; studies suggest involvement in tumor progression, particularly in cancers like prostate and ovarian, where aberrant expression correlates with metastasis or therapy resistance. Structurally, ELSPBP1 contains conserved domains associated with lipid binding, hinting at interactions with membrane components or signaling molecules. Recombinant ELSPBP1 is typically produced using prokaryotic (e.g., *E. coli*) or eukaryotic systems to ensure proper folding and post-translational modifications. Purification methods often involve affinity chromatography (e.g., His-tag systems) followed by functional validation. Research applications include elucidating its molecular mechanisms in fertility, exploring its diagnostic/therapeutic potential in cancer, and studying lipid-mediated cellular processes. Challenges remain in resolving its precise physiological ligands and signaling pathways. Current efforts focus on structural characterization and developing targeted inhibitors or biomarkers leveraging recombinant protein tools.
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