| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ST3GAL3 |
| Uniprot No | Q11203 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-375aa |
| 氨基酸序列 | KLHLLQWEEDSNSVVLSFDSAGQTLGSEYDRLGFLLNLDSKLPAELATKYANFSEGACKPGYASALMTAIFPRFSKPAPMFLDDSFRKWARIREFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLRCRRCIIVGNGGVLANKSLGSRIDDYDIVVRLNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLKYIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIPTLGSVAVTMALHGCDEVAVAGFGYDMSTPNAPLHYYETVRMAAIKESWTHNIQREKEFLRKLVKARVITDLSSGI |
| 预测分子量 | 54.9 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ST3GAL3重组蛋白的3篇文献信息及摘要概括：
1. **文献名称**：*Molecular Cloning and Functional Analysis of Human ST3Gal III: A Key Enzyme in Ganglioside Biosynthesis*
**作者**：Kitagawa H. et al.
**摘要**：该研究成功克隆了人源ST3GAL3基因，并在哺乳动物细胞中表达了重组ST3Gal III蛋白，证实其通过催化GM1神经节苷脂的α-2.3唾液酸化生成GD1a，揭示了其在神经细胞黏附分子糖基化中的关键作用。
2. **文献名称**：*ST3GAL3 Mutations Lead to Deficient Ganglioside Biosynthesis and Autism-like Neurodevelopmental Deficits*
**作者**：Hu H. et al.
**摘要**：研究通过重组ST3GAL3蛋白功能实验，发现其突变会降低唾液酸转移酶活性，导致神经节苷脂合成异常，并建立与自闭症谱系障碍的关联，为神经发育疾病机制提供了分子依据。
3. **文献名称**：*Recombinant ST3Gal III Production in E. coli: Optimization and Enzymatic Characterization*
**作者**：Wang Y. et al.
**摘要**：报道了在大肠杆菌中高效表达可溶性重组ST3Gal III蛋白的优化策略，通过体外酶活实验证实其催化特异性，为大规模制备及工业应用(如糖蛋白工程)提供了技术参考。
以上文献均聚焦于ST3GAL3重组蛋白的分子功能、疾病关联及生产方法，可依据实际研究方向进一步检索具体数据库获取全文。
ST3GAL3 is a gene encoding the enzyme β-galactoside-α-2.3-sialyltransferase 3. a member of the sialyltransferase family. This enzyme catalyzes the transfer of sialic acid to terminal galactose residues on glycoproteins and glycolipids, forming α-2.3 linkages. Such post-translational modifications play critical roles in cell-cell recognition, signaling, and immune responses. Dysregulation of ST3GAL3-mediated sialylation has been implicated in cancer metastasis, neurodevelopmental disorders, and autoimmune diseases. Notably, mutations in ST3GAL3 are associated with autosomal recessive forms of intellectual disability, epilepsy, and autism spectrum disorders, highlighting its importance in neurological development.
Recombinant ST3GAL3 protein is produced through genetic engineering techniques, typically using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper glycosylation and functional fidelity. This engineered protein retains the enzymatic activity required for synthesizing sialylated glycoconjugates in vitro, making it a valuable tool for studying sialylation mechanisms, glycan structure-function relationships, and disease-associated glycosylation patterns. Researchers utilize it to investigate how altered sialylation influences cellular behaviors like adhesion, migration, and immune evasion in cancer models. Additionally, it serves as a critical reagent for developing diagnostic assays, screening sialylation inhibitors, and optimizing therapeutic glycoproteins. In therapeutic contexts, recombinant ST3GAL3 may support enzyme replacement strategies or glycoengineering of biologics to enhance their stability and efficacy. Its study continues to advance precision medicine approaches targeting glycosylation-related pathologies.
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