| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Mer |
| Uniprot No | Q12866 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-999aa |
| 氨基酸序列 | MGPAPLPLLLGLFLPALWRRAITEAREEAKPYPLFPGPFPGSLQTDHTPLLSLPHASGYQPALMFSPTQPGRPHTGNVAIPQVTSVESKPLPPLAFKHTVGHIILSEHKGVKFNCSISVPNIYQDTTISWWKDGKELLGAHHAITQFYPDDEVTAIIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYIEVQGLPHFTKQPESMNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEQPEKSPSVLTVPGLTEMAVFSCEAHNDKGLTVSKGVQINIKAIPSPPTEVSIRNSTAHSILISWVPGFDGYSPFRNCSIQVKEADPLSNGSVMIFNTSALPHLYQIKQLQALANYSIGVSCMNEIGWSAVSPWILASTTEGAPSVAPLNVTVFLNESSDNVDIRWMKPPTKQQDGELVGYRISHVWQSAGISKELLEEVGQNGSRARISVQVHNATCTVRIAAVTRGGVGPFSDPVKIFIPAHGWVDYAPSSTPAPGNADPVLIIFGCFCGFILIGLILYISLAIRKRVQETKFGNAFTEEDSELVVNYIAKKSFCRRAIELTLHSLGVSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLDNSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFMKYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPLDRPTFSVLRLQLEKLLESLPDVRNQADVIYVNTQLLESSEGLAQGSTLAPLDLNIDPDSIIASCTPRAAISVVTAEVHDSKPHEGRYILNGGSEEWEDLTSAPSAAVTAEKNSVLPGERLVRNGVSWSHSSMLPLGSSLPDELLFADDSSEGSEVLM |
| 预测分子量 | 110,2 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. |
以下是关于Mer重组蛋白的参考文献示例(注：以下为模拟示例，实际文献需通过学术数据库查询)：
1. **《Recombinant Production and Functional Analysis of the Mer Tyrosine Kinase Ectodomain》**
- **作者：** Smith A, et al.
- **摘要：** 本研究成功表达并纯化人Mer酪氨酸激酶的胞外域重组蛋白，通过体外实验证实其与配体Gas6的结合能力，并分析其结构特征，为靶向Mer的抗体开发奠定基础。
2. **《Mer-Fc Fusion Protein Modulates Inflammation in Sepsis Models》**
- **作者：** Lee J, Brown K.
- **摘要：** 构建Mer-Fc重组融合蛋白，验证其在脓毒症模型中通过调控巨噬细胞信号通路减轻炎症反应的效果，显示其在免疫治疗中的潜在应用价值。
3. **《Structural Insights into Mer Receptor Activation by Cryo-EM》**
- **作者：** Zhang Y, et al.
- **摘要：** 利用冷冻电镜解析Mer重组蛋白的全长结构，揭示其与配体结合后的构象变化，为设计小分子抑制剂提供结构依据。
4. **《Recombinant Mer Enhances Efferocytosis in Cancer-Associated Macrophages》**
- **作者：** Garcia R, et al.
- **摘要：** 研究重组Mer蛋白对肿瘤微环境中巨噬细胞胞葬功能的促进作用，证实其通过Mer信号通路抑制肿瘤进展的机制。
**提示：** 建议通过PubMed、Google Scholar等平台以关键词“Mer recombinant protein”、“MerTK expression”或“MERS-CoV spike protein”检索最新文献。
**Background of Mer Recombinant Protein**
The Mer receptor tyrosine kinase, encoded by the *MERTK* gene, belongs to the TAM family of receptors (Tyro3. Axl, Mer), which play critical roles in cellular homeostasis, immune regulation, and disease pathogenesis. Mer is primarily expressed in immune cells (e.g., macrophages, dendritic cells) and epithelial tissues, where it mediates phagocytosis of apoptotic cells, modulates inflammatory responses, and supports tissue repair. Its activation relies on binding to ligands such as Gas6 and Protein S, triggering downstream signaling pathways like PI3K/Akt and MAPK, which promote cell survival, proliferation, and anti-apoptotic effects.
Dysregulation of Mer signaling is implicated in cancers, autoimmune disorders, and chronic inflammation. Overexpression of Mer in malignancies (e.g., leukemia, solid tumors) contributes to therapy resistance by enhancing tumor cell survival and immune evasion. Conversely, Mer deficiency or inhibition has been linked to autoimmune conditions due to impaired clearance of cellular debris, leading to prolonged inflammation.
Recombinant Mer proteins are engineered in vitro using expression systems (e.g., mammalian, insect cells) to retain functional domains, including the extracellular ligand-binding region and intracellular kinase domain. These proteins serve as vital tools for studying Mer-ligand interactions, screening therapeutic inhibitors (e.g., small molecules, monoclonal antibodies), and developing diagnostic assays. In therapeutic research, Mer-targeted strategies aim to either block oncogenic signaling or enhance Mer activity to resolve inflammation.
Recent advances in structural biology and antibody engineering have further refined the design of Mer recombinant proteins, enabling precise modulation of its signaling pathways. As a result, Mer remains a promising yet complex target for precision medicine, balancing its dual roles in promoting tissue homeostasis and driving disease progression.
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