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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLURP2 |
| Uniprot No | P0DP57 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-97aa |
| 氨基酸序列 | IWCHQCTGFGGCSHGSRCLRDSTHCVTTATRVLSNTEDLPLVTKMCHIGCPDIPSLGLGPYVSIACCQTSLCNHD |
| 预测分子量 | 10.0 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SLURP2重组蛋白的3篇代表性文献概览(注：部分文献信息为模拟示例，实际文献需通过学术数据库验证)：
1. **文献名称**：*"Recombinant SLURP2 modulates keratinocyte differentiation via nicotinic acetylcholine receptors"*
**作者**：A. Galat et al.
**摘要**：研究报道了重组SLURP2蛋白通过结合α3-nAChR受体调控表皮角质细胞分化，揭示了其在皮肤屏障功能中的作用，为治疗银屑病等皮肤疾病提供潜在靶点。
2. **文献名称**：*"Structural and functional characterization of human SLURP2 as a novel immune modulator"*
**作者**：K. Takeda et al.
**摘要**：通过X射线晶体学解析了重组SLURP2的三维结构，发现其通过抑制TLR4信号通路减轻炎症反应，提示其在自身免疫性疾病中的治疗潜力。
3. **文献名称**：*"SLURP2 recombinant protein suppresses tumor growth by blocking EGFR signaling in oral squamous cell carcinoma"*
**作者**：M. Tanaka et al.
**摘要**：体外及小鼠模型实验表明，重组SLURP2能竞争性抑制EGFR磷酸化，显著抑制口腔鳞癌增殖，提出其作为新型抗癌生物制剂的可能。
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**说明**：以上文献内容为领域知识综合模拟，实际研究中建议通过PubMed、Web of Science等平台以“SLURP2 recombinant protein”为关键词检索最新实验论文。
SLURP-2 (Secreted Ly6/uPAR-Related Protein 2) is a member of the Ly6/uPAR protein family, a group of conserved cysteine-rich proteins involved in cell signaling, immune regulation, and receptor modulation. Encoded by the *LYPD2* gene in humans, SLURP-2 is a 10–12 kDa glycoprotein primarily expressed in epithelial tissues, including the skin, oral mucosa, and gastrointestinal tract. It shares structural homology with snake venom α-neurotoxins and binds to nicotinic acetylcholine receptors (nAChRs), particularly the α3-subunit-containing subtypes, influencing cellular processes such as differentiation, apoptosis, and inflammation.
Structurally, SLURP-2 contains a characteristic Ly6/uPAR domain stabilized by five disulfide bonds formed by 10 conserved cysteine residues. Recombinant SLURP-2 is typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems to ensure proper folding and post-translational modifications. Its recombinant form enables studies on molecular interactions, signaling pathways, and therapeutic potential.
Functionally, SLURP-2 regulates epidermal homeostasis by modulating keratinocyte proliferation and differentiation. Dysregulation of SLURP-2 is linked to inflammatory skin disorders (e.g., psoriasis), oral squamous cell carcinoma, and autoimmune conditions. It also exhibits anti-inflammatory properties by suppressing pro-inflammatory cytokine release and interacting with immune cells. Recent studies suggest its role in cancer progression, where it may either promote or inhibit tumor growth depending on context.
Research on recombinant SLURP-2 focuses on its therapeutic potential in treating inflammatory diseases, wound healing, and cancer. However, its dual roles in pathophysiology and complex receptor interactions necessitate further mechanistic studies. Advances in structural biology and targeted drug design are expected to clarify its therapeutic applications and biomarker utility in precision medicine.
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