| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | B4GALT1 |
| Uniprot No | P15291-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 44-398aa |
| 氨基酸序列 | GRDLSRLPQL VGVSTPLQGG SNSAAAIGQS SGELRTGGAR PPPPLGASSQ PRPGGDSSPV VDSGPGPASN LTSVPVPHTT ALSLPACPEE SPLLVGPMLI EFNMPVDLEL VAKQNPNVKM GGRYAPRDCV SPHKVAIIIP FRNRQEHLKY WLYYLHPVLQ RQQLDYGIYV INQAGDTIFN RAKLLNVGFQ EALKDYDYTC FVFSDVDLIP MNDHNAYRCF SQPRHISVAM DKFGFSLPYV QYFGGVSALS KQQFLTINGF PNNYWGWGGE DDDIFNRLVF RGMSISRPNA VVGRCRMIRH SRDKKNEPNP QRFDRIAHTK ETMLSDGLNS LTYQVLDVQR YPLYTQITVD IGTPS |
| 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B4GALT1重组蛋白的模拟参考文献示例(内容为虚构，仅供参考)：
1. **《Expression and Characterization of Recombinant Human B4GALT1 in Mammalian Cells》**
作者：Zhang Y, et al.
摘要：研究利用HEK293细胞成功表达并纯化B4GALT1重组蛋白，证实其具有β-1.4-半乳糖基转移酶活性，并优化了糖基化反应条件。
2. **《Structural Insights into B4GALT1 Substrate Specificity via Mutagenesis Analysis》**
作者：Kumar S, et al.
摘要：通过定点突变和晶体结构解析，揭示了B4GALT1催化结构域的关键氨基酸残基，阐明了其底物选择性的分子机制。
3. **《B4GALT1 Overexpression Promotes Cancer Cell Adhesion in Metastatic Tumors》**
作者：Chen L, et al.
摘要：发现B4GALT1重组蛋白在癌细胞中高表达可增强整合素介导的细胞黏附，可能与肿瘤转移相关，为癌症治疗提供新靶点。
4. **《Development of a High-Throughput Assay for B4GALT1 Enzyme Activity Screening》**
作者：Wang H, et al.
摘要：建立基于荧光标记底物的B4GALT1酶活检测方法，用于快速筛选抑制剂，应用于阿尔茨海默病相关糖蛋白异常研究。
**注**：以上为示例性内容，实际文献需通过PubMed、Google Scholar等平台检索关键词“B4GALT1 recombinant protein”获取。
B4GALT1 (β-1.4-galactosyltransferase 1) is a key enzyme in glycobiology, catalyzing the transfer of galactose from UDP-galactose to terminal N-acetylglucosamine residues in glycoproteins and glycolipids. This reaction is critical for the biosynthesis of complex carbohydrate structures, including the lactosamine disaccharide unit (Galβ1-4GlcNAc), a fundamental component of N-linked and O-linked glycans. As a member of the glycosyltransferase family, B4GALT1 localizes to the Golgi apparatus and plays essential roles in cell-cell interactions, immune responses, and protein folding quality control. Its activity influences biological processes such as embryonic development, neural function, and cancer metastasis.
The recombinant B4GALT1 protein is typically produced using heterologous expression systems (e.g., mammalian cells, insect cells, or Escherichia coli) to enable controlled studies of its enzymatic properties and structure-function relationships. Unlike native forms, recombinant versions often lack transmembrane domains or are fused with solubility-enhancing tags (e.g., His-tag, GST) for purification convenience. These engineered proteins retain catalytic activity while offering improved stability for in vitro applications.
Research applications include elucidating glycan biosynthesis pathways, developing glycoengineering tools for therapeutic proteins, and screening inhibitors for drug discovery. Dysregulation of B4GALT1 has been linked to congenital disorders of glycosylation (CDGs), certain cancers, and autoimmune diseases, making its recombinant form valuable for mechanistic studies and diagnostic assay development. Recent structural studies using recombinant B4GALT1 have revealed insights into substrate binding specificity, aiding the design of glycan-targeted therapies. Its recombinant expression also supports biotechnological production of humanized glycoproteins with enhanced therapeutic efficacy.
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