纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SIAL2 |
Uniprot No | Q9Y3R4 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-380aa |
氨基酸序列 | MASLPVLQKE SVFQSGAHAY RIPALLYLPG QQSLLAFAEQ RASKKDEHAE LIVLRRGDYD APTHQVQWQA QEVVAQARLD GHRSMNPCPL YDAQTGTLFL FFIAIPGQVT EQQQLQTRAN VTRLCQVTST DHGRTWSSPR DLTDAAIGPA YREWSTFAVG PGHCLQLHDR ARSLVVPAYA YRKLHPIQRP IPSAFCFLSH DHGRTWARGH FVAQDTLECQ VAEVETGEQR VVTLNARSHL RARVQAQSTN DGLDFQESQL VKKLVEPPPQ GCQGSVISFP SPRSGPGSPA QWLLYTHPTH SWQRADLGAY LNPRPPAPEA WSEPVLLAKG SCAYSDLQSM GTGPDGSPLF GCLYEANDYE EIVFLMFTLK QAFPAEYLPQ |
预测分子量 | 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. |
1. **文献名称**: "Production and functional characterization of recombinant Siglec-2 (CD22) for glycan-binding studies"
**作者**: Smith A, et al.
**摘要**: 研究报道了人源Siglec-2(SIAL2)重组蛋白在大肠杆菌中的表达与纯化,验证了其唾液酸结合活性,并用于探究其在B细胞信号通路中的作用。
2. **文献名称**: "Structural analysis of Sial2 adhesion protein in cancer metastasis"
**作者**: Chen L, et al.
**摘要**: 通过昆虫细胞系统表达重组SIAL2蛋白,结合X射线晶体学解析其结构,揭示了该蛋白通过唾液酸介导的肿瘤细胞黏附机制。
3. **文献名称**: "Recombinant SIAL2 as a potential biomarker for autoimmune diseases"
**作者**: Kim J, et al.
**摘要**: 利用哺乳动物细胞表达的重组SIAL2蛋白,发现其与血清中自身抗体的特异性结合,为红斑狼疮等疾病的诊断提供了新靶点。
4. **文献名称**: "High-yield purification of SIAL2 fusion protein for therapeutic antibody screening"
**作者**: Wang Y, et al.
**摘要**: 优化了CHO细胞中重组SIAL2-Fc融合蛋白的纯化工艺,并验证其在单克隆抗体药物筛选中的应用潜力。
注:上述文献为示例性内容,实际引用需根据具体研究领域检索真实文献(如PubMed/Google Scholar)。
SIAL2. also known as Siglec-2 or CD22. is a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family, primarily expressed on the surface of B cells. It plays a critical role in modulating B-cell receptor (BCR) signaling and immune responses by recognizing glycoconjugates containing α2.6-linked sialic acid residues. Structurally, SIAL2 contains an N-terminal V-set immunoglobulin domain responsible for ligand binding, followed by multiple C2-set domains, a transmembrane region, and a cytoplasmic tail with immunoreceptor tyrosine-based inhibitory motifs (ITIMs). These motifs recruit phosphatases like SHP-1 to dampen B-cell activation, ensuring immune tolerance and preventing autoimmunity.
Recombinant SIAL2 proteins are engineered to study its biological functions and therapeutic potential. Typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper glycosylation, these proteins often include the extracellular domain for ligand interaction studies. Purification methods like affinity chromatography yield high-purity products for functional assays, structural analysis (e.g., X-ray crystallography), or antibody development.
Research on recombinant SIAL2 has highlighted its dual role in immunity: it suppresses aberrant B-cell activation but also contributes to pathogenic processes in B-cell malignancies and autoimmune disorders. Therapeutic strategies targeting SIAL2 include monoclonal antibodies to block inhibitory signaling in cancers or enhance its activity to treat autoimmune diseases. Additionally, SIAL2-ligand interactions are explored for drug delivery systems leveraging B-cell specificity. Despite progress, challenges remain in understanding its context-dependent signaling and optimizing clinical applications. Recombinant SIAL2 remains a vital tool for dissecting B-cell biology and developing immunotherapies.
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