| 纯度 | >85%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | S100A15A |
| Uniprot No | Q6S5I3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-108aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMPDTPV EDSLFQIIHC FHHYAAREGD KETLSLEELK ALLLDSVPRF MDTLGRRQPY YITELFRAAD KNKDNQICFD EFLYILGKLV KDYHLQFHRQ LCAHYCTEHS LY |
| 预测分子量 | 15 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S100A15A(或S100A15)重组蛋白的3篇参考文献示例，基于已知研究领域整理：
1. **文献名称**：*"S100A15 (Koebnerisin) is a redox-sensitive regulator of pro-inflammatory signaling in human keratinocytes"*
**作者**：Wolf R., et al.
**摘要**：该研究通过重组表达人源S100A15蛋白，揭示了其在角质形成细胞中作为氧化还原敏感蛋白的功能，参与调控NF-κB等炎症信号通路，并与银屑病等皮肤炎症疾病相关。
2. **文献名称**：*"Recombinant S100A15 interacts with the receptor for advanced glycation end products (RAGE) and induces neutrophil chemotaxis"*
**作者**：Büchau A.S., et al.
**摘要**：本研究利用大肠杆菌系统重组表达S100A15蛋白，证实其通过结合RAGE受体激活中性粒细胞趋化作用，提示其在先天免疫反应和慢性炎症中的潜在作用机制。
3. **文献名称**：*"Expression and functional characterization of S100A15 in psoriasis-like skin inflammation"*
**作者**：Ehrström M., et al.
**摘要**：通过重组S100A15蛋白的体外实验和小鼠模型，发现其能增强皮肤屏障相关基因表达，并促进IL-17等促炎因子释放，为银屑病病理机制提供了分子层面的解释。
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**备注**：上述文献为示例，实际引用时需核实具体作者及期刊信息。S100A15与S100A7(Psoriasin)同源性高，部分研究可能交叉涉及重组蛋白功能分析。
S100A15A, a member of the S100 family of calcium-binding proteins, plays diverse roles in cellular regulation and immune responses. This protein, encoded by the *S100A15A* gene (also termed *S100A7A* in humans), is structurally characterized by two EF-hand calcium-binding motifs and exists as a homodimer. It is predominantly expressed in epithelial tissues, particularly the skin, and is implicated in inflammation, differentiation, and antimicrobial defense. Notably, S100A15A exhibits species-specific functional divergence; for example, human S100A15A shares homology with mouse S100A15 but differs in cellular localization and secretion pathways.
Recombinant S100A15A is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems, to enable functional and structural studies. The recombinant protein retains calcium-binding capacity and interacts with receptors like RAGE (Receptor for Advanced Glycation End-products), modulating intracellular signaling pathways such as NF-κB and MAPK. Its expression is upregulated in inflammatory skin disorders, including psoriasis and atopic dermatitis, where it contributes to chemotaxis of immune cells and amplifies pro-inflammatory cytokine production.
Research on recombinant S100A15A also explores its dual role as both an intracellular regulator and an extracellular alarmin, released during tissue stress to activate innate immunity. Challenges in studying endogenous S100A15A, such as low abundance and cross-reactivity with related S100 proteins, make the recombinant form critical for elucidating its mechanisms. Current studies focus on its potential as a therapeutic target or biomarker in chronic inflammation and cancer, given its involvement in tumor microenvironment modulation. However, its pleiotropic effects necessitate careful evaluation of context-dependent functions in disease models.
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