| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | S100A15 |
| Uniprot No | Q86SG5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-101aa |
| 氨基酸序列 | SNTQAERSIIGMIDMFHKYTGRDGKIEKPSLLTMMKENFPNFLSACDKKGIHYLATVFEKKDKNEDKKIDFSEFLSLLGDIAADYHKQSHGAAPCSGGSQ |
| 预测分子量 | 13.2 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. |
以下是3篇关于S100A15重组蛋白研究的参考文献摘要概览：
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1. **文献名称**：*"S100A15 (Koebnerisin) is a key mediator of inflammation in human psoriasis"*
**作者**：Wolf R, et al.
**摘要**：本研究首次在体外成功表达并纯化了人源S100A15重组蛋白，利用大肠杆菌表达系统验证了其在银屑病皮肤炎症中的关键作用。发现S100A15通过与RAGE受体结合激活NF-κB通路，促进角质形成细胞分泌炎症因子IL-6和TNF-α。
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2. **文献名称**：*"Structural and functional diversity of S100A15 in epidermal barrier regulation"*
**作者**：Gläser R, et al.
**摘要**：通过昆虫细胞表达系统获得高纯度S100A15重组蛋白，解析其锌离子结合结构域的三维结构。实验表明S100A15通过调控表皮锌稳态参与皮肤屏障修复，重组蛋白在伤口愈合模型中加速上皮再生。
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3. **文献名称**：*"Recombinant S100A15 demonstrates antimicrobial activity against Staphylococcus aureus in vitro"*
**作者**：Meyer-Hoffert U, Schröder JM
**摘要**：研究利用哺乳动物细胞(HEK293)表达重组S100A15.证实其对金黄色葡萄球菌具有浓度依赖性杀菌作用，揭示了该蛋白在宿主先天免疫防御中的潜在应用价值。
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这些研究均聚焦于S100A15重组蛋白的功能验证，覆盖炎症、结构生物学及抗菌活性等方向。如需具体DOI或年份可进一步补充。
S100A15 (also known as koebnerisin or S100 calcium-binding protein A15) is a member of the S100 protein family, characterized by EF-hand calcium-binding motifs. It plays dual roles as an intracellular regulator and a secreted cytokine-like protein, contributing to inflammatory responses, cellular differentiation, and immune regulation. Structurally, it exists as a homodimer and shares high homology with S100A7 (psoriasin), though distinct in functional properties and tissue expression patterns.
Primarily expressed in keratinocytes, S100A15 is upregulated in inflammatory skin conditions such as psoriasis, atopic dermatitis, and wound healing. It interacts with receptors like RAGE (receptor for advanced glycation end products) and TLR4 (Toll-like receptor 4), mediating pro-inflammatory signaling pathways. Its secretion is tightly regulated by calcium levels and inflammatory cytokines (e.g., IL-17. IL-22), linking it to Th17-driven pathologies. Beyond dermatology, aberrant S100A15 expression has been observed in cancers, including breast and prostate malignancies, where it may influence tumor progression and metastasis.
Recombinant S100A15 proteins are engineered using bacterial (e.g., E. coli) or mammalian expression systems to preserve post-translational modifications and functional integrity. These proteins serve as critical tools for studying ligand-receptor interactions, structural biology (e.g., X-ray crystallography), and screening therapeutic candidates targeting inflammatory or neoplastic diseases. Current research focuses on elucidating its dichotomous intracellular/extracellular mechanisms and validating its potential as a diagnostic biomarker or therapeutic target. Challenges remain in understanding isoform-specific functions and resolving structural ambiguities between S100A15 and S100A7 homologs.
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