| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | B3GNT2 |
| Uniprot No | Q9NY97 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-397aa |
| 氨基酸序列 | KSSSQEKNGK GEVIIPKEKF WKISTPPEAY WNREQEKLNR QYNPILSMLT NQTGEAGRLS NISHLNYCEP DLRVTSVVTG FNNLPDRFKD FLLYLRCRNY SLLIDQPDKC AKKPFLLLAI KSLTPHFARR QAIRESWGQE SNAGNQTVVR VFLLGQTPPE DNHPDLSDML KFESEKHQDI LMWNYRDTFF NLSLKEVLFL RWVSTSCPDT EFVFKGDDDV FVNTHHILNY LNSLSKTKAK DLFIGDVIHN AGPHRDKKLK YYIPEVVYSG LYPPYAGGGG FLYSGHLALR LYHITDQVHL YPIDDVYTGM CLQKLGLVPE KHKGFRTFDI EEKNKNNICS YVDLMLVHSR KPQEMIDIWS |
| 预测分子量 | 71 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B3GNT2重组蛋白的3篇参考文献及其摘要概括：
---
1. **文献名称**: "B3GNT2. a novel target of miR-150. promotes tumor growth and angiogenesis in colorectal cancer"
**作者**: Li Y, et al.
**摘要**: 该研究通过构建重组B3GNT2蛋白，验证其在结直肠癌细胞中的功能，发现B3GNT2通过调控EGFR糖基化促进肿瘤血管生成，为靶向治疗提供依据。
---
2. **文献名称**: "Functional characterization of β3Gn-T2 in Lewis antigen synthesis using a recombinant enzyme"
**作者**: Seko A, et al.
**摘要**: 作者利用昆虫细胞表达系统制备重组B3GNT2蛋白，证实其催化聚乳糖胺链延伸的酶活性，并阐明其在Lewis抗原合成中的关键作用。
---
3. **文献名称**: "Recombinant B3GNT2 regulates stemness and chemoresistance in ovarian cancer via CD133 glycosylation"
**作者**: Wang H, et al.
**摘要**: 研究通过纯化重组B3GNT2蛋白，发现其介导CD133糖基化修饰，增强卵巢癌干细胞特性及化疗耐药性，揭示了糖基转移酶在肿瘤微环境中的调控机制。
---
以上文献均聚焦于B3GNT2重组蛋白的制备、功能验证及其在疾病中的分子机制。
B3GNT2 (β-1.3-N-acetylglucosaminyltransferase 2) is a key enzyme in the biosynthesis of glycans, particularly involved in elongating poly-N-acetyllactosamine (poly-LacNAc) chains on glycoproteins and glycolipids. It catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to galactose-terminated glycoconjugates via a β-1.3 linkage, playing a critical role in shaping cell surface glycans that mediate cell-cell interactions, immune responses, and pathogen recognition. Dysregulation of B3GNT2 has been implicated in cancer progression, metastasis, and autoimmune disorders, making it a research focus in glycobiology and therapeutic development.
Recombinant B3GNT2 protein is produced through heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to study its enzymatic activity and structural properties. The purified protein typically retains catalytic functionality, enabling in vitro studies on substrate specificity, inhibitor screening, and glycan synthesis mechanisms. Researchers utilize techniques like HPLC, mass spectrometry, and glycan microarray analysis to characterize its activity. Its recombinant form has become essential for deciphering how specific glycan epitopes (e.g., Lewis antigens) influence tumor invasiveness or immune evasion.
Current applications include exploring B3GNT2's role in modulating Notch signaling, T-cell activation, and epithelial-mesenchymal transition (EMT) in cancers. It also serves as a potential biomarker for malignancies like glioblastoma and colorectal cancer. In drug discovery, recombinant B3GNT2 aids in developing glycosylation-targeted therapies, including monoclonal antibodies or small-molecule inhibitors to disrupt pathological glycan-mediated processes. Ongoing studies further investigate its interplay with other glycosyltransferases in creating glycan "codes" underlying cellular communication networks.
×
