| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GCNT1 |
| Uniprot No | Q02742 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-428aa |
| 氨基酸序列 | MLRTLLRRRLFSYPTKYYFMVLVLSLITFSVLRIHQKPEFVSVRHLELAGENPSSDINCTKVLQGDVNEIQKVKLEILTVKFKKRPRWTPDDYINMTSDCSSFIKRRKYIVEPLSKEEAEFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDTKSEDSYLAAVMGIASCFSNVFVASRLESVVYASWSRVQADLNCMKDLYAMSANWKYLINLCGMDFPIKTNLEIVRKLKLLMGENNLETERMPSHKEERWKKRYEVVNGKLTNTGTVKMLPPLETPLFSGSAYFVVSREYVGYVLQNEKIQKLMEWAQDTYSPDEYLWATIQRIPEVPGSLPASHKYDLSDMQAVARFVKWQYFEGDVSKGAPYPPCDGVHVRSVCIFGAGDLNWMLRKHHLFANKFDVDVDLFAIQCLDEHLRHKALETLKH |
| 分子量 | 76.2 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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GCNT1蛋白的3篇参考文献示例(注：示例内容基于领域典型研究方向构建，实际文献需通过数据库核实)：
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1. **文献名称**：*Cloning and Functional Characterization of Recombinant Human GCNT1 in Glycosylation Modification*
**作者**：Smith A. et al.
**摘要**：报道了在HEK293细胞中重组表达人GCNT1蛋白的方法，证明其能够催化O-糖链分支合成，并发现其活性依赖Mn²⁺离子，为研究糖基化异常疾病提供工具。
2. **文献名称**：*Structural Insights into the Catalytic Mechanism of GCNT1 Through Cryo-EM Analysis*
**作者**：Zhang L. et al.
**摘要**：通过冷冻电镜解析了重组人GCNT1蛋白的三维结构，揭示了其底物结合口袋的关键氨基酸残基，解释了其在肿瘤相关糖抗原(如T抗原)合成中的特异性。
3. **文献名称**：*GCNT1 Overexpression Promotes Colorectal Cancer Metastasis via CD44 Glycosylation*
**作者**：Wang Y. et al.
**摘要**：利用重组GCNT1蛋白验证其在结肠癌细胞中通过修饰CD44的糖链结构增强肿瘤细胞的侵袭能力，提示其作为转移性癌症治疗靶点的潜力。
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如需真实文献，建议通过PubMed或Web of Science检索关键词 **"recombinant human GCNT1"** 或 **"GCNT1 glycosyltransferase"**。该蛋白研究多集中在糖生物学、肿瘤转移及自身免疫疾病领域。
GCNT1 (Glucosaminyl (N-Acetyl) Transferase 1) is a critical glycosyltransferase involved in the synthesis of mucin-type O-glycans. It catalyzes the formation of the core 2 O-glycan structure by transferring N-acetylglucosamine (GlcNAc) to GalNAc-O-Ser/Thr, a key branching step that diversifies O-glycan functions. This enzyme plays a pivotal role in cell adhesion, immune response, and protein stability, with dysregulation linked to diseases like cancer metastasis, immunodeficiency, and congenital disorders of glycosylation (CDG).
Recombinant human GCNT1 protein is produced using heterologous expression systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications. Its recombinant form enables studies on O-glycosylation mechanisms, structure-function relationships, and therapeutic targeting. Researchers use it to investigate pathological glycophenotypes in cancers (e.g., leukemia, colorectal cancer) where altered GCNT1 expression affects tumor progression and immune evasion. It also serves as a tool for screening glycosylation-modulating drugs or engineering glycoproteins with tailored carbohydrate motifs. Notably, GCNT1’s tissue-specific isoforms (e.g., in lymphocytes or mucous epithelia) highlight its functional versatility, driving interest in isoform-specific biomedical applications. Current challenges include elucidating its regulatory networks and translating findings into therapies for glycosylation-related disorders.
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