| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ST6GAL1 |
| Uniprot No | P15907 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-406aa |
| 氨基酸序列 | KEKKKGSYYDSFKLQTKEFQVLKSLGKLAMGSDSQSVSSSSTQDPHRGRQ TLGSLRGLAKAKPEASFQVWNKDSSSKNLIPRLQKIWKNYLSMNKYKVSY KGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGYLPKESIRT KAGPWGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTK TTIRLMNSQLVTTEKRFLKDSLYNEGILIVWDPSVYHSDIPKWYQNPDYN FFNNYKTYRKLHPNQPFYILKPQMPWELWDILQEISPEEIQPNPPSSGML GIIIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFFDSACTMGAYHPLLYEK NLVKHLNQGTDEDIYLLGKATLPGFRTIHCVDHHHHHH |
| 预测分子量 | 45 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ST6GAL1重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
---
1. **文献名称**: *"Recombinant Human ST6GAL1: Expression in HEK293 Cells and Functional Characterization in Glycosylation Modulation"*
**作者**: Smith A, et al.
**摘要**: 本研究报道了人源ST6GAL1在HEK293细胞中的重组表达与纯化，通过质谱验证其酶活性，证明其能够特异性催化α2.6-唾液酸在N-糖链末端的添加，并揭示了其在调节EGFR糖基化中的作用。
2. **文献名称**: *"Structural Insights into ST6GAL1 Catalytic Mechanism via Recombinant Protein Crystallography"*
**作者**: Chen L, et al.
**摘要**: 通过重组ST6GAL1蛋白的晶体结构解析，揭示了其底物结合域的关键氨基酸残基及催化活性位点，为开发靶向ST6GAL1的糖基化抑制剂提供了结构基础。
3. **文献名称**: *"ST6GAL1 Recombinant Protein Enhances Cancer Cell Invasiveness via Sialylation of Integrins"*
**作者**: Tanaka K, et al.
**摘要**: 利用重组ST6GAL1处理结肠癌细胞，发现其通过增加整合素β1的α2.6-唾液酸化水平，促进肿瘤细胞迁移和侵袭，提示ST6GAL1在癌症转移中的潜在作用。
4. **文献名称**: *"High-Yield Production of Active ST6GAL1 in Baculovirus-Insect Cell System for Glycoengineering Applications"*
**作者**: Müller J, et al.
**摘要**: 开发了一种基于杆状病毒-昆虫细胞系统的高效ST6GAL1重组蛋白生产方法，优化后的蛋白产量和活性适用于工业化糖蛋白工程，如抗体唾液酸化修饰。
---
如需真实文献，建议通过PubMed或Web of Science检索关键词(如ST6GAL1 recombinant protein/sialyltransferase)获取最新研究。
ST6GAL1 (ST6 beta-galactoside alpha-2.6-sialyltransferase 1) is a key enzyme in protein glycosylation, catalyzing the transfer of sialic acid residues to terminal galactose moieties on glycoproteins and glycolipids via α-2.6-linkages. This post-translational modification, known as sialylation, critically influences molecular recognition processes, including cell-cell communication, immune regulation, and pathogen-host interactions. The enzyme is predominantly localized in the Golgi apparatus and plays a vital role in shaping the glycan landscape of secreted and membrane-bound proteins.
Recombinant ST6GAL1 proteins are engineered through heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to study its biological functions and therapeutic potential. These purified proteins typically retain the catalytic domain (amino acids 45-403) responsible for substrate recognition and enzymatic activity, often fused with affinity tags like His-tag for simplified purification. Researchers utilize recombinant ST6GAL1 to investigate sialylation's impact on disease mechanisms, particularly in cancer metastasis (where hypersialylation promotes immune evasion), chronic inflammation, and neurodegenerative disorders.
Pharmaceutically, recombinant ST6GAL1 supports the production of sialylated therapeutic glycoproteins, such as monoclonal antibodies, where terminal sialylation enhances serum half-life and anti-inflammatory properties. Its applications extend to diagnostic development for glycan-based biomarkers and glycoengineering of cell surfaces for improved therapeutic cell therapies. Current research focuses on modulating ST6GAL1 activity to address pathological sialylation imbalances, positioning this recombinant enzyme as both a biological tool and a potential therapeutic target.
×
