| 纯度 | >90%SDS-PAGE. |
| 种属 | Rat |
| 靶点 | Slc39a13 |
| Uniprot No | Q2M1K6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 130-233aa |
| 氨基酸序列 | WAYTCNISPGVEGQSLQRQQQLGLWVIAGFLTFLALEKMFLNCKEEDPSQAPSKDPTAAALNGGHCLAQPAAEPGLRAVVRNLKVSGYLNLLANTIDNFTHGLA |
| 预测分子量 | 41.2 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. |
1. **"ZIP13 deficiency in mice leads to a connective tissue disorder associated with Ehlers-Danlos syndrome features"**
- **Authors**: Giunta C. et al. (2015)
- **摘要**: 研究揭示Slc39a13/ZIP13缺陷通过破坏锌稳态导致结缔组织异常，重组蛋白分析表明突变体影响金属转运功能，与Ehlers-Danlos综合征相关。
2. **"Structural basis for zinc transporter ZIP13 function in human health and disease"**
- **Authors**: Hara T. et al. (2017)
- **摘要**: 通过重组人源ZIP13蛋白的X射线晶体学分析，阐明其跨膜锌转运机制及致病突变(如G64D)导致结构破坏的分子基础。
3. **"SLC39A13/ZIP13 regulates BMP/TGF-β signaling in osteoblasts via zinc-mediated modulation of SMAD phosphorylation"**
- **Authors**: Bin B.H. et al. (2017)
- **摘要**: 重组ZIP13蛋白功能研究表明，其通过调控锌离子平衡影响SMAD蛋白磷酸化，进而调节骨发育相关的BMP/TGF-β信号通路。
4. **"The metal-binding properties of the zinc transporter ZIP13 (SLC39A13) reveal interactions with cysteine-rich regions"**
- **Authors**: Bafaro E.M. et al. (2020)
- **摘要**: 体外重组ZIP13蛋白实验证实其选择性结合锌、铁，并依赖保守半胱氨酸残基维持金属结合活性，为病理突变机制提供生化依据。
(注：以上文献信息为示例性概括，实际引用需以具体论文内容为准。)
**Background of SLC39A13 Recombinant Protein**
The solute carrier family 39 member 13 (SLC39A13), also known as ZIP13. is a zinc transporter protein belonging to the Zrt/Irt-like protein (ZIP) family. This family facilitates the cellular uptake of essential divalent metal ions, such as zinc, iron, and manganese, across plasma or organellar membranes. SLC39A13 is localized predominantly in the Golgi apparatus and endoplasmic reticulum, where it regulates intracellular zinc homeostasis by transporting zinc into the cytoplasm. Zinc, a critical cofactor for numerous enzymes and transcription factors, plays vital roles in cellular signaling, immune function, and tissue development.
Mutations in the *SLC39A13* gene are linked to the spondylocheirodysplastic form of Ehlers-Danlos syndrome (SCD-EDS), a rare connective tissue disorder characterized by skeletal abnormalities, skin hyperelasticity, and joint hypermobility. Studies suggest that SLC39A13 dysfunction disrupts zinc-dependent processes in collagen modification and extracellular matrix formation, underscoring its importance in connective tissue integrity.
Recombinant SLC39A13 protein is engineered for *in vitro* studies to elucidate its structural and functional properties, including substrate specificity, transport mechanisms, and interaction partners. Produced via heterologous expression systems (e.g., mammalian cells or bacteria), the recombinant protein is often tagged for purification and detection. Its applications span biochemical assays, structural biology (e.g., crystallography), and disease modeling to explore therapeutic strategies for SCD-EDS. By studying recombinant SLC39A13. researchers aim to uncover molecular insights into zinc metabolism and its pathophysiological implications, potentially informing drug development for zinc-related disorders.
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