| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNTN |
| Uniprot No | A6NMZ2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-147aa |
| 氨基酸序列 | GSSHHHHHHSSGLVPRGSHMGGCMHSTQDKSLHLEGDPNPSAAPTSTCAP RKMPKRISISKQLASVKALRKCSDLEKAIATTALIFRNSSDSDGKLEKAI AKDLLQTQFRNFAEGQETKPKYREILSELDEHTENKLDFEDFMILLLSIT VMSDLLQNIRNVKIMK |
| 预测分子量 | 19 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. |
以下是关于SNTN重组蛋白的3篇参考文献示例(注：以下内容为模拟虚构，实际文献需通过学术数据库检索确认)：
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1. **文献名称**: *"Recombinant SNTN Protein Promotes Tumor Cell Invasion via Actin Remodeling"*
**作者**: Li, X.; Zhang, Y.; Wang, H.
**摘要**: 本研究通过大肠杆菌系统表达了SNTN重组蛋白，并证明其通过调控肌动蛋白动态变化促进肿瘤细胞侵袭，为SNTN在癌症转移中的作用提供了机制依据。
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2. **文献名称**: *"Structural Characterization of SNTN and Its Role in Cilia Function"*
**作者**: Smith, J.R.; Patel, K.; Brown, T.
**摘要**: 利用X射线晶体学解析了SNTN重组蛋白的三维结构，发现其与纤毛内转运蛋白相互作用，提示SNTN可能在纤毛组装和信号转导中发挥关键作用。
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3. **文献名称**: *"High-Yield Purification of Recombinant SNTN and Its Application in Drug Screening"*
**作者**: Chen, L.; Gupta, S.; Kim, M.
**摘要**: 开发了一种高效纯化SNTN重组蛋白的方法，并基于此建立了高通量药物筛选平台，筛选出多个潜在调控SNTN活性的小分子化合物。
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如需实际文献，建议在PubMed或Google Scholar中搜索关键词“SNTN recombinant protein”或结合具体研究领域细化检索。
**Background of SNTN Recombinant Protein**
SNTN (Sputacin) is a protein encoded by the *SNTN* gene, primarily recognized for its role in sperm development and function. Initially identified as a component of the fibrous sheath in sperm flagella, SNTN is critical for maintaining structural integrity and motility of sperm, with potential implications in male fertility. Studies suggest its involvement in cytoskeletal organization and ciliary functions, linking it to broader cellular processes beyond reproduction, such as ciliopathies or respiratory tract disorders.
The recombinant form of SNTN is produced using genetic engineering techniques, typically via expression systems like *E. coli*, yeast, or mammalian cell cultures. Recombinant SNTN retains the functional domains of the native protein, including its N-terminal transmembrane region and C-terminal coiled-coil domains, which are essential for protein-protein interactions and structural stability. This engineered protein enables researchers to study SNTN’s biochemical properties, interactions, and mechanisms in controlled settings.
Interest in SNTN recombinant protein spans basic and applied research. In reproductive biology, it serves as a tool to investigate sperm maturation defects or infertility pathways. Beyond reproduction, SNTN’s association with cilia function has spurred exploration into diseases like primary ciliary dyskinesia (PCD) or chronic respiratory conditions. Additionally, recombinant SNTN may aid in developing diagnostic biomarkers or therapeutic strategies targeting cilia-related disorders.
Despite progress, challenges remain in fully elucidating SNTN’s multifunctional roles and optimizing recombinant production for clinical applications. Ongoing research focuses on structural analysis, interaction mapping, and validating its therapeutic potential, positioning SNTN as a protein of growing significance in both reproductive health and ciliopathy research.
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