| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | b3GNT3 |
| Uniprot No | Q9Y2A9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-372aa |
| 氨基酸序列 | MKYLRHRRPNATLILAIGAFTLLLFSLLVSPPTCKVQEQPPAIPEALAWPTPPTRPAPAPCHANTSMVTHPDFATQPQHVQNFLLYRHCRHFPLLQDVPPSKCAQPVFLLLVIKSSPSNYVRRELLRRTWGRERKVRGLQLRLLFLVGTASNPHEARKVNRLLELEAQTHGDILQWDFHDSFFNLTLKQVLFLQWQETRCANASFVLNGDDDVFAHTDNMVFYLQDHDPGRHLFVGQLIQNVGPIRAFWSKYYVPEVVTQNERYPPYCGGGGFLLSRFTAAALRRAAHVLDIFPIDDVFLGMCLELEGLKPASHSGIRTSGVRAPSQRLSSFDPCFYRDLLLVHRFLPYEMLLMWDALNQPNLTCGNQTQIY |
| 预测分子量 | 42,5 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b3GNT3重组蛋白的参考文献示例(内容为虚构示例，仅供格式参考)：
1. **《β3Gn-T3重组蛋白促进肿瘤细胞迁移的机制研究》**
作者：Zhang L. et al.
摘要：通过体外表达b3GNT3重组蛋白，研究发现其通过调控粘附分子糖基化修饰增强结肠癌细胞迁移能力，提示其在肿瘤转移中的关键作用。
2. **《重组b3GNT3酶法合成Lewis抗原的体外功能验证》**
作者：Chen Y. et al.
摘要：利用昆虫细胞系统表达b3GNT3重组蛋白，证实其催化特定糖链结构(如Lewis抗原)的生物合成，为糖工程研究提供工具酶。
3. **《b3GNT3重组蛋白对T细胞活化的抑制作用》**
作者：Liu X. et al.
摘要：研究发现b3GNT3重组蛋白可修饰免疫细胞表面糖蛋白，抑制T细胞受体信号通路，为自身免疫疾病治疗提供潜在靶点。
4. **《高效可溶性b3GNT3重组蛋白表达与纯化策略》**
作者：Wang Q. et al.
摘要：优化原核表达系统，获得高纯度b3GNT3重组蛋白，并验证其酶活性，为后续结构解析及药物筛选奠定基础。
(注：以上文献为模拟内容，实际文献需通过PubMed/Google Scholar等平台检索关键词“b3GNT3 recombinant”或“β3Gn-T3 expression”获取。)
**Background of b3GNT3 Recombinant Protein**
β-1.3-N-acetylglucosaminyltransferase 3 (b3GNT3), a member of the glycosyltransferase family, plays a critical role in synthesizing poly-N-acetyllactosamine chains by catalyzing the transfer of N-acetylglucosamine (GlcNAc) to galactose residues via β1-3 linkages. These carbohydrate structures are essential for cell-cell interactions, immune responses, and signal transduction. Dysregulation of b3GNT3 has been implicated in cancer progression, particularly in promoting metastasis and modulating tumor cell adhesion.
Structurally, b3GNT3 contains a conserved catalytic domain and transmembrane region, typical of Golgi-resident glycosyltransferases. Its enzymatic activity influences the formation of cell surface glycans, such as Lewis antigens, which are associated with malignant phenotypes. Overexpression of b3GNT3 has been observed in multiple cancers, including gastric, colorectal, and hepatocellular carcinomas, often correlating with poor prognosis. Mechanistically, it enhances invasiveness by altering integrin-mediated signaling or activating pro-metastatic pathways like Wnt/β-catenin.
Recombinant b3GNT3 protein is produced using heterologous expression systems (e.g., *E. coli*, mammalian cells) for functional studies. Purified recombinant proteins enable researchers to investigate substrate specificity, enzyme kinetics, and interactions with inhibitors or antibodies. Such studies are pivotal for developing glycan-targeted diagnostics or therapies. For instance, inhibiting b3GNT3 activity may suppress metastasis, while its glycan products could serve as biomarkers.
Overall, b3GNT3 recombinant protein serves as a vital tool for dissecting glycan biosynthesis mechanisms and exploring therapeutic strategies in cancer and glycosylation-related disorders.
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