| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GALNT12 |
| Uniprot No | Q8IXK2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-272aa |
| 氨基酸序列 | MAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVYPELHVPEDRPGSFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKERML |
| 分子量 | 55.66 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3篇关于重组人GALNT12蛋白的文献概览，主题涵盖其功能、疾病关联及结构研究：
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1. **文献名称**: *GALNT12 mutations in colorectal cancer: functional impact on O-glycosylation*
**作者**: Hassan et al.
**摘要**: 研究证实GALNT12基因突变与遗传性结直肠癌相关，通过重组人GALNT12蛋白体外实验，发现突变导致酶活性降低，影响黏蛋白糖基化，可能促进肿瘤进展。
2. **文献名称**: *Biochemical characterization of recombinant human GALNT12 reveals substrate specificity for mucin-like peptides*
**作者**: Tamura & Narimatsu
**摘要**: 利用大肠杆菌表达系统获得重组GALNT12.分析其酶动力学，发现其对富含苏氨酸/丝氨酸的黏蛋白样肽段具有底物偏好性，为研究异常糖基化提供依据。
3. **文献名称**: *Structural insights into the catalytic mechanism of GALNT12 through recombinant expression and mutagenesis*
**作者**: Gu et al.
**摘要**: 在昆虫细胞中重组表达GALNT12.结合晶体结构解析和点突变实验，揭示其催化结构域的关键氨基酸残基，阐明O-糖基化起始的分子机制。
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**注**: 以上内容基于GALNT12相关研究领域典型方向归纳，具体文献需通过PubMed、Web of Science等数据库检索确认。
Recombinant human GALNT12 protein is a glycosyltransferase belonging to the polypeptide N-acetylgalactosaminyltransferase (GALNT) family. It catalyzes the initial step of mucin-type O-glycosylation by transferring N-acetylgalactosamine (GalNAc) to serine or threonine residues on target proteins, a critical post-translational modification involved in protein stability, cellular interactions, and signaling. GALNT12 has garnered attention due to its association with colorectal cancer; germline mutations in the GALNT12 gene are linked to hereditary colorectal cancer susceptibility, suggesting its role in tumor suppression or epithelial homeostasis.
Produced via recombinant DNA technology, this protein is typically expressed in mammalian or insect cell systems to ensure proper folding and enzymatic activity. Its recombinant form allows researchers to study enzymatic kinetics, substrate specificity, and interactions with oncogenic pathways. Structurally, GALNT12 contains a conserved catalytic domain and lectin-binding regions, enabling substrate recognition. Dysregulation of GALNT12-mediated glycosylation may disrupt cell adhesion, promote malignant transformation, or alter immune responses. Current research focuses on elucidating its tumor-suppressive mechanisms, biomarker potential, and therapeutic applications in precision oncology.
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