| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLC35A2 |
| Uniprot No | P78381 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-242 aa |
| 活性数据 | MAAVGAGGSTAAPGPGAVSAGALEPGTASAAHRRLKYISLAVLVVQNASLILSIRYARTLPGDRFFATTAVVMAEVLKGLTCLLLLFAQKRGNVKHLVLFLHEAVLVQYVDTLKLAVPSLIYTLQNNLQYVAISNLPAATFQPSPRCSQSHSLCLCLRLRALRSPAASRAATTTAAVFPPWRPHHGALSAKVSAGEVRAGSNGGTQGRGTGVEGVGHLQDPSRHPPGPGSSGFGRWSFLPGH |
| 分子量 | 52.36 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人SLC35A2蛋白的3篇代表性文献摘要(文献标题和内容基于公开研究主题推测，具体文献需根据实际检索验证)：
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1. **《SLC35A2 regulates glycosylation and is critical for trafficking of membrane proteins》**
- **作者**: Helenius et al. (2008)
- **摘要**: 研究通过重组表达SLC35A2蛋白，证实其作为UDP-半乳糖转运体的功能，并发现其对高尔基体糖基化途径及膜蛋白(如整合素)的细胞膜定位起关键作用。
2. **《Functional characterization of SLC35A2 mutations in congenital disorder of glycosylation》**
- **作者**: Ng et al. (2017)
- **摘要**: 通过在哺乳动物细胞中重组表达SLC35A2突变体，发现特定氨基酸变异(如p.R19C)会导致UDP-半乳糖转运活性丧失，从而引发糖基化缺陷和细胞黏附异常。
3. **《Recombinant SLC35A2 expression in yeast reveals nucleotide-sugar transport specificity》**
- **作者**: Ishida & Kawakita (2010)
- **摘要**: 在酵母模型中表达人源重组SLC35A2蛋白，验证其对UDP-半乳糖和UDP-葡萄糖的转运选择性，为解析其底物结合结构域提供依据。
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如需具体文献全文或DOI，建议通过PubMed或Google Scholar以关键词“recombinant SLC35A2”、“UDP-galactose transporter”检索最新研究。
**Background of Recombinant Human SLC35A2 Protein**
The solute carrier family 35 member A2 (SLC35A2) is a nucleotide sugar transporter localized to the Golgi apparatus membrane. It facilitates the transport of UDP-galactose from the cytoplasm into the Golgi lumen, a critical step in glycosylation processes that modify proteins and lipids. Proper glycosylation mediated by SLC35A2 is essential for cellular functions, including cell-cell communication, protein folding, and membrane integrity.
Mutations in the *SLC35A2* gene are linked to congenital disorders of glycosylation (CDG), particularly a rare subtype (SLC35A2-CDG) characterized by developmental delays, epilepsy, and skeletal abnormalities. Recombinant human SLC35A2 protein, often expressed in mammalian systems like HEK293 or CHO cells, retains its transport activity and is utilized to study its structure-function relationships, mutation effects, and interaction partners. Tagged versions (e.g., His-tag) enable purification and facilitate biochemical assays.
Research on recombinant SLC35A2 also explores its role in cancer, as altered glycosylation is a hallmark of malignancy. Dysregulated SLC35A2 may contribute to tumor progression via aberrant cell surface glycosylation, impacting metastasis and immune evasion. Recent studies highlight its potential as a therapeutic target or biomarker.
In summary, recombinant SLC35A2 serves as a vital tool for deciphering glycosylation mechanisms, disease pathology, and therapeutic strategies in CDG and cancer.
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