| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | B4GALT2 |
| Uniprot No | O60909 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-372aa |
| 氨基酸序列 | MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASSSSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLERVQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYVINQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDIRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITVDIGRPPSWPPRG |
| 分子量 | 41 kDa |
| 蛋白标签 | His tag N-Terminus |
| 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. |
以下是关于重组人β-1.4半乳糖基转移酶2(B4GALT2)的参考文献示例：
1. **"Functional characterization of human β-1.4-galactosyltransferase 2 (B4GALT2) in glycoprotein biosynthesis"**
- 作者：Smith A et al.
- 摘要：研究通过体外重组表达B4GALT2.验证其在N-连接糖链合成中的催化活性，发现其特异性地将半乳糖转移至GlcNAc残基，并揭示其对底物的选择性。
2. **"B4GALT2 overexpression promotes cancer cell adhesion via enhanced glycosylation of integrin β1"**
- 作者：Chen L et al.
- 摘要：探讨B4GALT2在肿瘤转移中的作用，证明其通过调节整合素β1的糖基化促进细胞间黏附，重组酶的表达水平与癌细胞侵袭性呈正相关。
3. **"Structural insights into the catalytic mechanism of B4GALT2 using X-ray crystallography"**
- 作者：Yamamoto K et al.
- 摘要：首次解析B4GALT2的晶体结构，阐明其底物结合域及锰离子依赖性催化机制，为开发特异性抑制剂提供结构基础。
4. **"Recombinant B4GALT2 production in mammalian cells: implications for industrial glycoprotein engineering"**
- 作者：Zhang R et al.
- 摘要：优化B4GALT2在CHO细胞中的重组表达系统，证明其在抗体半乳糖化修饰中的应用潜力，显著提高治疗性蛋白的稳定性与效价。
(注：以上文献为示例，实际文献需通过学术数据库查询。)
B4GALT2. a member of the β-1.4-galactosyltransferase (B4GALT) family, is a key enzyme in glycosylation processes. It catalyzes the transfer of galactose from UDP-galactose to terminal N-acetylglucosamine residues via a β-1.4 linkage, contributing to the synthesis of glycoconjugates like N-linked glycoproteins, glycolipids, and proteoglycans. Located primarily in the Golgi apparatus, B4GALT2 is encoded by the B4GALT2 gene on human chromosome 4q28.2. Its enzymatic activity is critical for forming lactose in mammary glands and shaping glycoprotein structures involved in cell adhesion, signaling, and immune recognition.
Recombinant B4GALT2. produced through heterologous expression systems (e.g., mammalian or insect cells), retains catalytic activity and is widely used to study glycan biosynthesis mechanisms. Dysregulation of B4GALT2 has been linked to congenital disorders of glycosylation (CDGs), cancer metastasis, and neurological diseases. For instance, altered B4GALT2 expression may influence tumor cell invasiveness by modifying cell-surface glycans that mediate interactions with extracellular matrices. Structural studies reveal conserved motifs in its catalytic domain and a transmembrane region anchoring it to Golgi membranes. Research on recombinant B4GALT2 supports applications in glycobiology, including glycoengineering of therapeutic proteins to optimize pharmacokinetics or reduce immunogenicity. Additionally, it serves as a tool for synthesizing defined glycan structures to investigate carbohydrate-mediated biological processes.
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