| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JAM1 |
| Uniprot No | Q9Y624 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-238aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMLGSVT VHSSEPEVRI PENNPVKLSC AYSGFSSPRV EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT REDTGTYTCM VSEEGGNSYG EVKVKLIVLV PPSKPTVNIP SSATIGNRAV LTCSEQDGSP PSEYTWFKDG IVMPTNPKST RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGV |
| 预测分子量 | 26 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JAM1重组蛋白的3篇示例文献及其摘要概括：
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1. **文献名称**：*Recombinant JAM-1 protein regulates endothelial barrier function through tight junction modulation*
**作者**：Martinez-Estrada OM, et al.
**摘要**：本研究通过表达并纯化重组JAM1蛋白，证明其在体外能增强内皮细胞单层的屏障功能。实验表明JAM1通过调控紧密连接蛋白(如ZO-1)的分布，抑制炎症因子诱导的血管通透性异常。
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2. **文献名称**：*Structural characterization of recombinant JAM1 extracellular domain and its interaction with adenovirus*
**作者**：Bewley MC, et al.
**摘要**：利用重组JAM1胞外域蛋白进行晶体结构解析，揭示了其Ig样结构域的关键构象。进一步实验证实，JAM1作为腺病毒次要受体，其重组蛋白可竞争性抑制病毒与宿主细胞的结合。
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3. **文献名称**：*JAM1 recombinant protein inhibits neutrophil transendothelial migration in sepsis models*
**作者**：Liu L, et al.
**摘要**：在小鼠脓毒症模型中，注射重组JAM1蛋白显著减少中性粒细胞跨内皮迁移，降低组织损伤。机制研究表明，该蛋白通过阻断JAM1与LFA-1的相互作用抑制炎症反应。
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(注：以上为模拟文献，实际引用时需以真实数据库检索结果为准。)
JAM1 (Junctional Adhesion Molecule 1), also known as JAM-A or F11R, is a transmembrane glycoprotein belonging to the immunoglobulin superfamily. Initially identified in endothelial and epithelial cells, it plays a critical role in regulating cell-cell interactions, leukocyte transmigration, and barrier function. Structurally, JAM1 contains two extracellular immunoglobulin-like domains, a single transmembrane region, and a cytoplasmic tail with signaling motifs. Its interaction partners include ligands such as LFA-1 (on leukocytes), other JAM family members, and viruses like reoviruses, which exploit JAM1 as a receptor for cell entry.
Recombinant JAM1 protein is engineered to study these biological processes in vitro or in animal models. Typically produced in expression systems like *E. coli* or mammalian cell lines, recombinant JAM1 retains functional domains to mimic native protein behavior. It is often tagged (e.g., His-tag, Fc-fusion) for purification or detection. Researchers use it to investigate JAM1-mediated signaling pathways (e.g., PI3K/Akt, small GTPases), leukocyte-endothelial interactions in inflammation, or viral pathogenesis. In disease contexts, altered JAM1 expression correlates with cancer metastasis, atherosclerosis, and autoimmune disorders, making its recombinant form valuable for therapeutic target validation. For example, soluble JAM1 can competitively inhibit leukocyte recruitment in experimental models of sepsis or ischemia-reperfusion injury. Its role in maintaining epithelial/endothelial integrity also positions it as a candidate for barrier-stabilizing therapies. Despite its utility, challenges remain in replicating post-translational modifications (e.g., glycosylation) in prokaryotic systems, potentially affecting ligand-binding specificity. Ongoing studies aim to refine recombinant JAM1 production and explore its applications in drug discovery and immunomodulation.
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