| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GALNTL6 |
| Uniprot No | Q49A17 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-601aa |
| 氨基酸序列 | SLYKDKHLVKSAEPGEQQTFPLGLGDGQFYSWTDGLRRKDWHDYESIQKEAMRSRKGEHGKPYPLTEEDHDDSAYRENGFNIFVSNNIALERSLPDIRHANCKHKMYLERLPNTSIIIPFHNEGWTSLLRTIHSIINRTPGSLIAEIILVDDFSEREHLKDKLEEYMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIPLNHKTIVCPMIDVIDHNHFGYEAQAGDAMRGAFDWEMYYKRIPIPPELQRADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGEMFDVPCSRVGHIYRKYVPYKVPSGTSLARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQKELRKQLKCKDFKWFMAAVAWDVPKYYPPVEPPPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSERTWSHEQLFTFGWREDIRPGEPLHTRKFCFDAISHNSPVTLYDCHGMKGNQLWGYRKDRTLFHPVSNSCMDCNHAEKKIFMARCDPLSETQQWIFEHINMTVLEKFNHHANS |
| 预测分子量 | 70.7 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GALNTL6重组蛋白的3篇参考文献示例(注：文献信息为模拟生成，仅供参考)：
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1. **文献名称**: *Expression and enzymatic characterization of recombinant human GALNTL6 in mammalian cells*
**作者**: Zhang Y, Wang L, Chen X
**摘要**: 本研究在HEK293细胞中成功表达了重组人源GALNTL6蛋白，并证实其具有N-乙酰半乳糖胺转移酶活性，能够特异性催化黏蛋白样底物的糖基化修饰，为研究其在糖蛋白合成中的功能提供基础。
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2. **文献名称**: *GALNTL6 promotes cancer cell invasion via modifying integrin α5 glycosylation in vitro*
**作者**: Li H, Tanaka K, Suzuki T
**摘要**: 通过重组GALNTL6蛋白的体外实验，发现其通过调控整合素α5的O-糖基化修饰增强癌细胞迁移能力，提示GALNTL6可能在肿瘤转移中发挥关键作用。
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3. **文献名称**: *Structural analysis of GALNTL6 reveals conserved motifs in GalNAc-T family*
**作者**: Müller R, Jensen PH, Clausen H
**摘要**: 利用重组GALNTL6蛋白的晶体结构解析，揭示了其催化结构域中保守的糖基转移酶特征，并发现其底物结合口袋的独特构象可能影响底物选择性。
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**备注**：以上文献为示例性质，实际研究中请通过PubMed或Web of Science等平台以“GALNTL6 recombinant protein”为关键词检索最新文献。如需具体文章协助，可提供更详细的研究方向(如疾病关联、结构或应用场景)。
**Background of GALNTL6 Recombinant Protein**
GALNTL6 (polypeptide N-acetylgalactosaminyltransferase-like protein 6) is a member of the GALNT family, which catalyzes the initial step of mucin-type O-glycosylation by transferring N-acetylgalactosamine (GalNAc) to serine or threonine residues on target proteins. This post-translational modification is critical for regulating protein stability, cellular localization, and interactions. While GALNTL6 shares structural homology with other GALNT enzymes, its catalytic activity remains under investigation, with studies suggesting it may function as a regulatory or pseudoenzyme influencing glycosylation patterns indirectly.
The recombinant GALNTL6 protein is typically produced using heterologous expression systems (e.g., mammalian cells, insect cells, or *E. coli*), enabling controlled studies of its biochemical properties and interactions. Researchers employ techniques like affinity chromatography and tag-based purification (e.g., His-tag) to obtain high-purity protein. Its recombinant form facilitates *in vitro* assays to explore substrate specificity, enzymatic kinetics, and potential roles in diseases.
Emerging evidence links GALNTL6 dysregulation to pathologies, including cancers and neurological disorders. For example, aberrant expression has been observed in tumor tissues, implicating it in cancer progression via altered cell adhesion or signaling. Additionally, genome-wide association studies (GWAS) suggest GALNTL6 variants may influence cardiovascular and metabolic traits.
Current research focuses on clarifying GALNTL6’s functional mechanisms, substrates, and therapeutic potential. The availability of recombinant GALNTL6 accelerates drug discovery and biomarker studies, particularly in glycosylation-related diseases. Further characterization of this protein may uncover novel pathways in cellular regulation and disease pathogenesis.
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