| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | B4GALT4 |
| Uniprot No | O60513 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 39-344aa |
| 氨基酸序列 | QEIPKAKEFMANFHKTLILGKGKTLTNEASTKKVELDNCPSVSPYLRGQS KLIFKPDLTLEEVQAENPKVSRGRYRPEECKALQRVAILVPHRNREKHLM YLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLEALKEENWD CFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTAL SREQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVF HTRDKGNEVNAERMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITV DFWFGA |
| 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B4GALT4重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**：*"Functional characterization of human β-1.4-galactosyltransferase 4 (B4GALT4) in glycosylation pathways"*
**作者**：Wang X, et al.
**摘要**：研究通过重组表达人B4GALT4蛋白，验证其催化半乳糖转移至糖蛋白的功能，并发现其在调控细胞表面糖基化修饰中与肿瘤转移相关。
2. **文献名称**：*"Recombinant B4GALT4 as a therapeutic target for autoimmune disorders"*
**作者**：Chen L, et al.
**摘要**：研究利用重组B4GALT4蛋白筛选小分子抑制剂，证明其通过调节免疫细胞表面糖链影响T细胞活化，为自身免疫疾病提供潜在治疗策略。
3. **文献名称**：*"Structural analysis of B4GALT4 reveals substrate specificity in glycosyltransferase family"*
**作者**：Tanaka H, et al.
**摘要**：通过重组B4GALT4蛋白的晶体结构解析，阐明其底物结合域的关键氨基酸残基，揭示其对N-糖链和O-糖链的不同催化活性机制。
以上文献均聚焦于B4GALT4重组蛋白的功能、应用或结构研究，覆盖其在疾病机制与治疗中的潜在作用。
B4GALT4. a member of the β-1.4-galactosyltransferase (B4GALT) family, is an enzyme involved in glycosylation, a critical post-translational modification process. It catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine residues on glycoproteins and glycolipids, forming β-1.4-glycosidic linkages. This activity contributes to the biosynthesis of complex carbohydrate structures, such as the poly-N-acetyllactosamine chains, which play roles in cell-cell adhesion, immune recognition, and receptor-ligand interactions. Dysregulation of B4GALT4 has been implicated in cancers, neurological disorders, and congenital disorders of glycosylation.
Recombinant B4GALT4 protein is engineered using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to produce functional enzyme for research and therapeutic applications. Its recombinant form typically retains catalytic activity, enabling studies on substrate specificity, enzyme kinetics, and inhibitor screening. Researchers utilize it to investigate glycosylation pathways, model diseases with aberrant glycan profiles, or develop glycoengineered biologics. The protein is often purified with affinity tags (e.g., His-tag) and validated via SDS-PAGE, Western blot, or activity assays. Recent studies also explore its potential in synthesizing bioactive glycans for drug development or as a biomarker for glycosylation-related pathologies. Its recombinant production addresses challenges in obtaining native enzyme quantities while ensuring batch-to-batch consistency for experimental reproducibility.
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