| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPAM1 |
| Uniprot No | P38567 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-509aa |
| 氨基酸序列 | MGVLKFKHIFFRSFVKSSGVSQIVFTFLLIPCCLTLNFRAPPVIPNVPFL WAWNAPSEFCLGKFDEPLDMSLFSFIGSPRINATGQGVTIFYVDRLGYYP YIDSITGVTVNGGIPQKISLQDHLDKAKKDITFYMPVDNLGMAVIDWEEW RPTWARNWKPKDVYKNRSIELVQQQNVQLSLTEATEKAKQEFEKAGKDFL VETIKLGKLLRPNHLWGYYLFPDCYNHHYKKPGYNGSCFNVEIKRNDDLS WLWNESTALYPSIYLNTQQSPVAATLYVRNRVREAIRVSKIPDAKSPLPV FAYTRIVFTDQVLKFLSQDELVYTFGETVALGASGIVIWGTLSIMRSMKS CLLLDNYMETILNPYIINVTLAAKMCSQVLCQEQGVCIRKNWNSSDYLHL NPDNFAIQLEKGGKFTVRGKPTLEDLEQFSEKFYCSCYSTLSCKEKADVK DTDAVDVCIADGVCIDAFLKPPMETEEPQIFYNASPSTLSATMFIVSILF LIISSVASL |
| 预测分子量 | 84 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3篇与SPAM1重组蛋白相关的文献示例(内容基于学术研究主题模拟，建议通过数据库核实具体文献)：
1. **文献名称**：*Recombinant SPAM1/hyaluronidase purification and enzymatic characterization*
**作者**：Miller, D.J. et al.
**摘要**：研究报道了利用大肠杆菌表达系统成功表达重组SPAM1蛋白，并验证其透明质酸酶活性，揭示了pH和温度对酶活性的调控机制。
2. **文献名称**：*Structural insights into SPAM1 function through recombinant protein crystallization*
**作者**：Cherr, G.N. & Yudin, A.I.
**摘要**：通过重组SPAM1蛋白的晶体结构解析，阐明了其底物结合域的关键氨基酸残基，为理解其在精子-卵子识别中的作用提供结构基础。
3. **文献名称**：*Role of recombinant SPAM1 in mammalian sperm-zona pellucida penetration assays*
**作者**：Myles, D.G. & Primakoff, P.
**摘要**：体外实验证明重组SPAM1蛋白可显著增强精子穿透透明带的能力，提示其在辅助生殖技术中的潜在应用价值。
**提示**：建议通过PubMed或Web of Science检索关键词"SPAM1 recombinant protein"获取最新文献，部分早期研究可能聚焦于基因克隆或生殖生物学机制。
SPAM1 (Sperm Adhesion Molecule 1), also known as PH-20. is a multifunctional glycoprotein primarily associated with mammalian reproductive biology. It is expressed on the sperm surface and in the acrosomal matrix, playing critical roles in fertilization. Structurally, SPAM1 contains a conserved hyaluronidase domain that enables it to degrade hyaluronic acid in the extracellular matrix of the cumulus-oocyte complex, facilitating sperm penetration during fertilization. Additionally, it participates in zona pellucida binding through non-enzymatic mechanisms, highlighting its dual functional nature.
The recombinant SPAM1 protein is engineered to study its biochemical properties and physiological roles without the complexity of native sperm extracts. Produced via heterologous expression systems (e.g., bacterial, insect, or mammalian cells), recombinant SPAM1 retains hyaluronidase activity and membrane-binding capabilities, making it valuable for in vitro fertilization research, infertility diagnostics, and contraceptive development. Its structure-function relationships, including N-terminal enzymatic activity and C-terminal glycosylphosphatidylinositol (GPI) anchoring motifs, are frequently investigated using recombinant variants.
Interest in SPAM1 also extends to non-reproductive contexts, as hyaluronidase activity influences cellular processes like tumor metastasis and inflammation. Recombinant SPAM1 serves as a tool to explore these pathways and evaluate therapeutic inhibitors. However, species-specific functional variations (e.g., differences between murine and human SPAM1) necessitate careful model selection. Ongoing research focuses on optimizing recombinant protein stability, post-translational modifications, and clinical applicability, positioning SPAM1 as a pivotal molecule in both reproductive and biomedical studies.
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