纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | B4GALT3 |
Uniprot No | O60512 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 32-393aa |
氨基酸序列 | RSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERS PLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPH RAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVRE ALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYP QYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPT SVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLAREL GPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPL STANHTALRGSHVDHHHHHH |
预测分子量 | 42 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B4GALT3重组蛋白的3篇参考文献及简要摘要:
---
1. **文献名称**: *B4GALT3 regulates SNAIL1/2 expression through glycosylation of TGFβ receptors and promotes epithelial-mesenchymal transition in cancer*
**作者**: Li Y, et al.
**摘要**: 本研究揭示了重组人B4GALT3蛋白通过介导TGFβ受体糖基化,激活下游SMAD通路,上调SNAIL转录因子表达,从而促进癌细胞上皮-间质转化(EMT)和转移的分子机制。
---
2. **文献名称**: *Recombinant B4GALT3 enhances β1 integrin stability and promotes melanoma cell adhesion*
**作者**: Zhang H, et al.
**摘要**: 通过体外表达纯化的B4GALT3重组蛋白,研究发现其能够修饰β1整合素的N-糖链结构,增强整合素-细胞外基质结合能力,进而促进黑色素瘤细胞黏附和迁移。
---
3. **文献名称**: *Structural and functional analysis of human B4GALT3 using recombinant enzyme expressed in HEK293 cells*
**作者**: Wang X, et al.
**摘要**: 该研究利用HEK293细胞系统成功表达并纯化功能性B4GALT3重组蛋白,通过酶活实验和晶体学分析,阐明了其底物特异性及在合成多乳糖胺链中的关键作用。
---
(注:以上为模拟文献,实际应用中需通过PubMed/Google Scholar等平台以关键词"B4GALT3 recombinant"检索真实文献。)
B4GALT3 (β-1.4-galactosyltransferase 3) is a member of the β-1.4-galactosyltransferase family, enzymes that catalyze the transfer of galactose from UDP-galactose to N-acetylglucosamine residues in glycoproteins and glycolipids. This post-translational modification, termed glycosylation, is critical for modulating protein stability, cellular recognition, and intercellular communication. B4GALT3 is localized to the Golgi apparatus and is ubiquitously expressed, though its activity varies across tissues. It plays roles in synthesizing lactose in mammary glands, forming poly-N-acetyllactosamine chains, and contributing to the structural diversity of cell surface glycans. Dysregulation of B4GALT3 has been linked to developmental disorders, immune dysfunction, and cancer progression, where altered glycosylation patterns influence metastasis and drug resistance.
Recombinant B4GALT3 protein is produced using heterologous expression systems (e.g., E. coli, mammalian cells) to enable functional studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate substrate specificity, kinetic properties, and interactions with inhibitors or therapeutic agents. Purification typically involves affinity tags (e.g., His-tag) for high yield and purity. Studies leveraging recombinant B4GALT3 have advanced our understanding of glycan biosynthesis pathways, cell adhesion mechanisms, and disease-associated glycosylation anomalies. Additionally, it serves as a tool for developing glycan-based diagnostics and therapies, including antibody engineering to optimize Fc-mediated immune responses. Despite its functional overlap with other β-1.4-galactosyltransferases, B4GALT3’s unique substrate preferences and tissue-specific roles underscore its importance in both basic research and biomedical applications.
×