| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | b3GALT1 |
| Uniprot No | Q9Y5Z6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-326aa |
| 氨基酸序列 | MASKVSCLYVLTVVCWASALWYLSITRPTSSYTGSKPFSHLTVARKNFTFGNIRTRPINPHSFEFLINEPNKCEKNIPFLVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSKAKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGGPIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVAELIYKTSLHTRLLHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQISPEEMHRIWNDMSSKKHLRC |
| 预测分子量 | 37,9 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b3GALT1重组蛋白的3篇参考文献示例(文献信息为模拟示例，非真实发表论文)：
1. **文献名称**: "Expression and Functional Characterization of Recombinant Human β3GalT1 in Glycosylation Pathway Analysis"
**作者**: Smith A, et al.
**摘要**: 该研究通过哺乳动物表达系统成功表达并纯化了具有酶活性的重组b3GALT1蛋白，证实其在体外催化糖基转移反应的功能，为研究糖蛋白合成机制提供了工具。
2. **文献名称**: "Structural Insights into β3GalT1 Substrate Specificity via Recombinant Protein Crystallography"
**作者**: Lee J, et al.
**摘要**: 利用重组b3GALT1蛋白的晶体结构解析，揭示了该酶底物结合域的关键氨基酸残基，阐明了其底物选择性的分子机制。
3. **文献名称**: "Role of Recombinant β3GalT1 in Modulating Collagen Glycosylation in Connective Tissue Disorders"
**作者**: Chen R, et al.
**摘要**: 通过体外实验证明重组b3GALT1蛋白可修复因基因突变导致的胶原糖基化缺陷，为相关结缔组织疾病的治疗提供了潜在策略。
(注：以上文献为模拟内容，实际引用时请以真实发表的学术论文为准。)
**Background of b3GALT1 Recombinant Protein**
β-1.3-galactosyltransferase 1 (b3GALT1) is a member of the glycosyltransferase family, which catalyzes the transfer of galactose to acceptor substrates in a β-1.3 linkage. This enzyme plays a critical role in the biosynthesis of glycoconjugates, including glycoproteins and glycolipids, which are essential for cell-cell communication, immune recognition, and extracellular matrix organization. Specifically, b3GALT1 is involved in synthesizing the core 1 O-glycan structure (Galβ1-3GalNAc-) on mucin-type glycoproteins, a modification vital for protein stability, trafficking, and ligand interactions.
The gene encoding b3GALT1 is located on human chromosome 2q24.3 and is highly conserved across vertebrates. Dysregulation or mutations in b3GALT1 have been linked to congenital disorders, including a subtype of muscular dystrophy (MDDGA9) and platelet-type bleeding disorders, highlighting its physiological importance. Additionally, altered b3GALT1 expression is observed in cancers, suggesting roles in tumor progression and metastasis.
Recombinant b3GALT1 protein is produced using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to enable functional and structural studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate substrate specificity, kinetic parameters, and inhibitor screening. Purified b3GALT1 is also used to synthesize defined glycan structures for glycoengineering applications, such as developing glycoprotein therapeutics with optimized pharmacokinetic properties.
In drug discovery, b3GALT1 serves as a potential target for modulating glycosylation in diseases. Structural insights from recombinant protein studies aid in designing small molecules or biologics to regulate its activity. Furthermore, recombinant b3GALT1 is employed in diagnostic assays to detect autoantibodies in autoimmune conditions or characterize glycan-binding proteins.
Overall, b3GALT1 recombinant protein is a valuable tool for advancing glycobiology research, therapeutic development, and understanding glycosylation-related pathologies.
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