| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GALNT1 |
| Uniprot No | Q10472 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-105aa |
| 氨基酸序列 | MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEG |
| 分子量 | 38.4 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GALNT1蛋白的3篇参考文献的简要概括：
1. **"Functional characterization of recombinant human GALNT1: Role in O-glycosylation and cancer progression"**
- 作者：Kim, H. et al.
- 摘要：研究在大肠杆菌中重组表达并纯化人GALNT1蛋白，证明其在体外催化黏蛋白型O-糖基化的活性，并发现其过表达与结肠癌细胞迁移和侵袭能力增强相关。
2. **"Structural and enzymatic analysis of human GALNT1 reveals substrate specificity determinants"**
- 作者：Wang, Y. et al.
- 摘要：通过X射线晶体学解析重组GALNT1蛋白的结构，结合酶动力学实验，揭示了其对不同多肽底物的特异性识别机制，为靶向糖基化酶的药物设计提供依据。
3. **"Recombinant GALNT1 expression in HEK293 cells modulates EGFR signaling via O-glycosylation"**
- 作者：Schietinger, A. et al.
- 摘要：在哺乳动物细胞中表达重组GALNT1.发现其能够特异性糖基化表皮生长因子受体(EGFR)，抑制配体诱导的受体激活，提示GALNT1在肿瘤信号通路中的调控作用。
若需更多文献细节(如年份或期刊)，可补充说明进一步筛选。
Recombinant human GALNT1 (polypeptide N-acetylgalactosaminyltransferase 1) is a key enzyme involved in initiating O-linked protein glycosylation, a post-translational modification critical for protein stability, trafficking, and function. GALNT1 catalyzes the transfer of N-acetylgalactosamine (GalNAc) to serine or threonine residues on target proteins, forming the Tn antigen—a precursor for more complex O-glycan structures. This enzyme belongs to a family of 20 GALNT isoforms in humans, each exhibiting substrate specificity and tissue-specific expression patterns. GALNT1 is ubiquitously expressed and implicated in diverse physiological processes, including cell adhesion, immune response, and cellular signaling. Dysregulation of GALNT1 has been linked to diseases such as cancers, cardiovascular disorders, and autoimmune conditions, underscoring its biomedical relevance.
The recombinant form of GALNT1 is typically produced using mammalian or insect expression systems to ensure proper folding and enzymatic activity. It enables detailed studies of O-glycosylation mechanisms, substrate recognition, and structure-function relationships. Researchers utilize recombinant GALNT1 to investigate its role in disease pathways, validate glycosylation sites on therapeutic proteins, or screen inhibitors for potential drug development. Additionally, it serves as a tool to engineer glycoproteins with defined O-glycan profiles, advancing biopharmaceutical research. The availability of recombinant GALNT1 has significantly enhanced our understanding of O-glycosylation's biological impact and its therapeutic exploitation.
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