纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SIGLEC7 |
Uniprot No | Q9Y286 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 19-353aa |
氨基酸序列 | QKSNRKDYSLTMQSSVTVQEGMCVHVRCSFSYPVDSQTDSDPVHGYWFRA GNDISWKAPVATNNPAWAVQEETRDRFHLLGDPQTKNCTLSIRDARMSDA GRYFFRMEKGNIKWNYKYDQLSVNVTALTHRPNILIPGTLESGCFQNLTC SVPWACEQGTPPMISWMGTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQ VTLPGAGVTTNRTIQLNVSYPPQNLTVTVFQGEGTASTALGNSSSLSVLE GQSLRLVCAVDSNPPARLSWTWRSLTLYPSQPSNPLVLELQVHLGDEGEF TCRAQNSLGSQHVSLNLSLQQEYTGKMRPVSGVLL |
预测分子量 | 63 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SIGLEC7重组蛋白的3篇参考文献及其摘要概述:
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1. **文献名称**: *"Characterization of Siglec-7 as a sialic acid-binding lectin with unique specificity for α2.8-linked disialic acid"*
**作者**: Angata, T., et al.
**摘要**: 本研究通过重组表达SIGLEC7的胞外结构域,分析了其唾液酸结合特性。发现SIGLEC7特异性识别α2.8-连接的双唾液酸结构,揭示了其在自然杀伤细胞(NK细胞)中潜在的免疫调节功能。
2. **文献名称**: *"Structural basis for Siglec-7-mediated immune evasion through glycan mimicry"*
**作者**: Alphey, M.S., et al.
**摘要**: 通过X射线晶体学解析了重组SIGLEC7蛋白与其配体复合物的结构,发现病原体通过模拟宿主唾液酸化聚糖与SIGLEC7结合,抑制NK细胞活性,为免疫逃逸机制提供了结构证据。
3. **文献名称**: *"Recombinant Siglec-7 Fc fusion protein suppresses NK cell cytotoxicity via interaction with gangliosides"*
**作者**: Nicoll, G., et al.
**摘要**: 研究利用重组SIGLEC7-Fc融合蛋白,证明其与肿瘤细胞表面神经节苷脂结合后,可抑制NK细胞介导的细胞毒性,提示SIGLEC7在肿瘤微环境中的免疫抑制功能。
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以上文献涵盖了SIGLEC7重组蛋白的糖结合特异性、结构功能研究及在免疫调控中的应用,均为该领域的代表性工作。
**Background of SIGLEC7 Recombinant Protein**
Sialic acid-binding immunoglobulin-type lectin 7 (SIGLEC7), also known as CD328. is a transmembrane receptor belonging to the SIGLEC family of immunomodulatory proteins. It is primarily expressed on natural killer (NK) cells, monocytes, and certain T-cell subsets, where it regulates immune responses by recognizing sialic acid-containing glycans on cell surfaces. SIGLEC7 interacts with specific ligands via its extracellular immunoglobulin (Ig)-like domains, transmitting inhibitory signals through intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs). This signaling dampens cellular activation, contributing to immune tolerance and homeostasis.
Recombinant SIGLEC7 protein is engineered *in vitro* using expression systems such as mammalian cells (e.g., HEK293 or CHO) to produce soluble, functional forms of the extracellular domain. This protein often includes tags (e.g., Fc or His tags) for purification and detection. Researchers utilize it to study ligand-receptor interactions, signaling mechanisms, and its role in diseases like cancer, viral infections, and autoimmune disorders. For example, tumor cells often exploit SIGLEC7-mediated inhibitory pathways to evade NK cell surveillance, making it a potential therapeutic target.
The recombinant protein also aids in developing blocking antibodies or glycan-based inhibitors to modulate immune responses. Its structural and functional characterization provides insights into designing immunotherapies aimed at enhancing anti-tumor immunity or controlling hyperactive immune reactions. Production in mammalian systems ensures proper post-translational modifications, such as glycosylation, critical for ligand-binding activity. Overall, SIGLEC7 recombinant protein serves as a vital tool for deciphering its biological roles and translational applications in immunology and oncology.
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