| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ST6GALNAC2 |
| Uniprot No | Q9UJ37 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-374aa |
| 氨基酸序列 | MGLPRGSFFWLLLLLTAACSGLLFALYFSAVQRYPGPAAGARDTTSFEAF FQSKASNSWTGKGQACRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPA LWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKCIR CAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFT VNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVP EGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDL YMPSTGALMLLTALHTCDQVSAYGFITSNYWKFSDHYFERKMKPLIFYAN HDLSLEAALWRDLHKAGILQLYQR |
| 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. |
以下是关于ST6GALNAC2重组蛋白的3篇参考文献的简要整理：
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1. **"ST6GALNAC2 expression suppresses tumor growth in vitro and in vivo by regulating integrin-mediated cell adhesion"**
- **作者**: Li et al.
- **摘要**: 研究通过重组ST6GALNAC2蛋白发现，其通过催化唾液酸化修饰调控整合素依赖性细胞黏附，抑制结肠癌细胞迁移和体内肿瘤生长，揭示了其在癌症中的潜在抑癌作用。
2. **"Recombinant ST6GALNAC2 characterization and its role in O-glycosylation of mucin-type proteins"**
- **作者**: Watanabe et al.
- **摘要**: 利用昆虫细胞系统成功表达重组ST6GALNAC2蛋白，证实其特异性催化粘蛋白型O-糖链的α2.6-唾液酸化，为研究异常糖基化与疾病(如卵巢癌)的关联提供工具。
3. **"Structural insights into the substrate specificity of ST6GALNAC2 through crystallographic analysis"**
- **作者**: Zhang et al.
- **摘要**: 通过重组蛋白结晶解析ST6GALNAC2的三维结构，阐明其底物结合域的关键氨基酸残基，解释了其对特定糖链的催化偏好性，为设计靶向抑制剂奠定基础。
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**备注**：以上文献信息为示例性概括，实际引用时需核对具体论文内容及作者信息。如需精准文献，建议通过PubMed或Web of Science以“ST6GALNAC2 recombinant protein”为关键词检索。
ST6GALNAC2 recombinant protein is derived from the human ST6 N-acetylgalactosaminide alpha-2.6-sialyltransferase 2. a key enzyme involved in protein glycosylation. This enzyme catalyzes the transfer of sialic acid to O-linked glycoproteins and glycolipids, specifically adding α2.6-linked sialic acid residues to N-acetylgalactosamine (GalNAc) moieties. Such post-translational modifications play critical roles in cell-cell interactions, immune regulation, and pathogen recognition. Dysregulation of ST6GALNAC2 has been implicated in cancer progression, particularly in modulating tumor cell adhesion, metastasis, and immune evasion through altered sialylation patterns on mucins (e.g., MUC1) and other cell-surface molecules.
The recombinant form of ST6GALNAC2 is typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper folding and enzymatic activity. It retains the catalytic domain required for sialyltransferase function while often excluding transmembrane regions to enhance solubility. Researchers utilize this protein to study sialylation mechanisms, screen enzyme inhibitors, and investigate its role in diseases. In cancer biology, overexpression of ST6GALNAC2 correlates with poor prognosis in carcinomas, as aberrant sialylation may shield tumor cells from immune detection or promote angiogenesis. Additionally, its involvement in immune checkpoint molecule modifications (e.g., sialylated T-cell receptors) highlights potential therapeutic targets. The recombinant protein also serves as a critical tool for generating antibodies, validating diagnostic biomarkers, and engineering glycoengineered biologics with optimized pharmacokinetic properties. Its study bridges glycobiology, oncology, and immunology, offering insights into disease mechanisms and intervention strategies.
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