| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | B3GNT5 |
| Uniprot No | Q9BYG0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-378aa |
| 氨基酸序列 | MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVNDTLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQLNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWANTYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVSYEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDHVFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKIILLCKISYVDTYPCRAAFI |
| 分子量 | 67.32 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 冻干粉 |
| 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3篇关于B3GNT5的参考文献示例(人工虚构示例供参考，实际文献需检索数据库)：
1. **"B3GNT5-mediated glycosylation drives breast cancer metastasis by enhancing stem-like properties"**
- **作者**: Lee, S. et al.
- **摘要**: 本研究揭示B3GNT5通过合成多聚乳糖胺结构促进乳腺癌细胞表面整合素糖基化，增强干细胞特性和肺转移。
2. **"Structural insights into the catalytic mechanism of B3GNT5 in poly-N-acetyllactosamine synthesis"**
- **作者**: Zhang, Y. et al.
- **摘要**: 报道B3GNT5的晶体结构，阐明其底物结合位点及催化域，揭示其在糖链延伸中的酶活调控机制。
3. **"B3GNT5 regulates immune suppression via Treg cell glycosylation in colorectal cancer"**
- **作者**: Wang, H. et al.
- **摘要**: 发现肿瘤微环境中B3GNT5通过调节调节性T细胞(Treg)糖基化增强其免疫抑制功能，促进结直肠癌进展。
4. **"B3GNT5 knockout suppresses glioblastoma invasion by modulating EGFR glycosylation"**
- **作者**: Nakamura, K. et al.
- **摘要**: 证实B3GNT5缺失通过抑制EGFR糖基化降低胶质母细胞瘤细胞侵袭性和MAPK信号通路激活。
(注：以上内容根据公开研究背景虚构，真实文献需通过PubMed/Google Scholar检索确认。)
**Background of Recombinant Human N-Acetylglucosaminyltransferase 5 (B3GNT5)**
B3GNT5. a member of the β-1.3-N-acetylglucosaminyltransferase family, catalyzes the transfer of N-acetylglucosamine (GlcNAc) to galactose-containing glycans via β1.3-linkages, forming poly-N-acetyllactosamine chains. These chains are critical structural components of glycoproteins and glycolipids, influencing cell-cell interactions, immune responses, and signal transduction. The enzyme is ubiquitously expressed, with notable roles in embryonic development, inflammation, and cancer.
B3GNT5 is encoded by the *B3GNT5* gene (also termed *B3GNT7*) in humans and is localized to the Golgi apparatus. Its activity contributes to the biosynthesis of Lewis antigens and selectin ligands, which mediate leukocyte trafficking and tumor metastasis. Dysregulation of B3GNT5 has been implicated in pathological conditions, including colorectal cancer, glioblastoma, and chronic inflammatory diseases, where it often correlates with poor prognosis.
Recombinant B3GNT5 is produced using heterologous expression systems (e.g., mammalian or insect cells) to study its enzymatic kinetics, substrate specificity, and inhibitor screening. Its recombinant form enables detailed exploration of glycosylation mechanisms and therapeutic targeting in glycan-mediated disorders. Recent studies also highlight its potential in glycoengineering for biologics production. As glycosylation gains prominence in precision medicine, recombinant B3GNT5 serves as a vital tool for decoding glycan functions and developing glycan-based therapeutics.
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