| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | b3GALT5 |
| Uniprot No | P59052 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-145aa |
| 氨基酸序列 | MRRLRHREVR GPVLGHTATG GPQNGTSGCT TAPQQRPPPG TQGMLEQYLN RGGQKSHGLC WLLCFVSQGQ NQDVISAELW CRIHVQAHWG CWQNSAVWGC RNEVLVSLLA VGQGLPSASG GRLPSLVHGP SHPDSQHPRE VPLAL |
| 预测分子量 | 15,7 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3篇关于b3GALT5重组蛋白的关键文献摘要信息：
1. **文献名称**: "β3GalT5 regulates lysosomal functions and glioma cell radiosensitivity via CTSD-mediated autophagy"
**作者**: Li X et al. (2022)
**摘要**: 研究发现重组b3GALT5蛋白通过调控CTSD依赖性自噬通路影响胶质瘤细胞溶酶体功能，并揭示其通过改变糖基化修饰增强肿瘤细胞对放疗的敏感性。
2. **文献名称**: "Structural basis of β1.3-galactosyltransferase 5 substrate specificity"
**作者**: Wang Q et al. (2019)
**摘要**: 解析了重组b3GALT5蛋白的晶体结构，阐明其催化结构域中关键氨基酸残基(如Asp211)对底物UDP-galactose的特异性结合机制，为设计糖基化酶抑制剂提供依据。
3. **文献名称**: "β3GALT5 knockout in HEK293 cells alters N-glycan profiles and EGFR signaling"
**作者**: Zhang Y et al. (2020)
**摘要**: 利用重组b3GALT5蛋白进行功能补偿实验，证明该酶通过介导多聚乳糖胺链合成调控EGFR糖基化修饰，进而影响受体二聚化及下游MAPK信号通路激活。
注：以上文献信息为示例性内容，实际文献需通过PubMed或Web of Science等平台检索确认。如需具体文献链接或DOI号，建议补充检索条件进一步查询。
b3GALT5 (β-1.3-galactosyltransferase 5) is a key enzyme in glycobiology, belonging to the glycosyltransferase family. It catalyzes the transfer of galactose from UDP-galactose to acceptor substrates via β-1.3-linkages, playing a critical role in synthesizing glycoconjugates like glycoproteins and glycolipids. This enzyme is particularly involved in forming poly-N-acetyllactosamine (poly-LacNAc) chains, which serve as scaffolds for functional glycan epitopes involved in cell adhesion, immune recognition, and signaling. Dysregulation of b3GALT5 has been linked to cancer progression, autoimmune disorders, and congenital disorders of glycosylation (CDGs), highlighting its biological and clinical relevance.
Recombinant b3GALT5 protein is engineered using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to enable large-scale production for functional studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate substrate specificity, kinetic properties, and interactions with other glycosylation enzymes. This tool has advanced research on glycan biosynthesis pathways and the role of specific glycostructures in diseases. For example, studies show that b3GALT5 overexpression in certain cancers promotes metastasis by modifying cell surface glycans to enhance invasiveness or immune evasion. Conversely, reduced activity may impair neural development, as seen in some CDGs.
In therapeutic contexts, recombinant b3GALT5 aids in glycoengineering biologics, such as optimizing antibody glycosylation to improve therapeutic efficacy. It also serves as a target for inhibitors in cancer therapy. Despite progress, challenges remain in fully elucidating its regulatory mechanisms and tissue-specific functions, driving ongoing research into its structural biology and disease associations.
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