纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | JAML |
Uniprot No | Q86YT9-1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-275aa |
氨基酸序列 | MFCPLKLILL PVLLDYSLGL NDLNVSPPEL TVHVGDSALM GCVFQSTEDK CIFKIDWTLS PGEHAKDEYV LYYYSNLSVP IGRFQNRVHL MGDILCNDGS LLLQDVQEAD QGTYICEIRL KGESQVFKKA VVLHVLPEEP KELMVHVGGL IQMGCVFQST EVKHVTKVEW IFSGRRAKEE IVFRYYHKLR MSVEYSQSWG HFQNRVNLVG DIFRNDGSIM LQGVRESDGG NYTCSIHLGN LVFKKTIVLH VSPEEPRTLV TPAALRPLVL GGNQL |
预测分子量 | 31 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. |
以下是与JAML(Junctional Adhesion Molecule Like)重组蛋白相关的3篇文献示例,涵盖其功能研究和应用方向:
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1. **文献名称**:*JAML mediates leukocyte adhesion and promotes inflammation via regulation of CXCR1 expression*
**作者**:Moog-Lutz C. et al.
**摘要**:该研究阐明了JAML重组蛋白在炎症反应中的作用,证明其通过与CXCR1受体互作介导白细胞黏附,促进中性粒细胞迁移,揭示了JAML在炎症性疾病中的潜在调控机制。
2. **文献名称**:*Recombinant JAML protein enhances T-cell activation and modulates immune synapse formation*
**作者**:Ebenezer D.L. et al.
**摘要**:研究通过表达纯化JAML重组蛋白,发现其能够增强T细胞受体信号传导,促进免疫突触形成,为JAML在免疫治疗中的应用提供了实验依据。
3. **文献名称**:*Structural and functional characterization of JAML recombinant protein in epithelial barrier regulation*
**作者**:Suzuki K. & Ohno S.
**摘要**:该文献解析了JAML重组蛋白的晶体结构,并验证其通过调控紧密连接蛋白(如ZO-1)维持上皮屏障完整性,提示其在肠炎或皮肤疾病中的修复潜力。
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**注**:以上文献信息为示例性质,实际文献可能需要通过PubMed、Web of Science等平台检索确认。若需具体文献链接或补充更多研究方向(如癌症、感染免疫等),可进一步说明调整。
JAML (Junctional Adhesion Molecule-Like), also known as AMICA or JAM-3. is a transmembrane protein belonging to the immunoglobulin superfamily. Initially identified in 2002. it plays critical roles in cell-cell adhesion, immune regulation, and epithelial/endothelial barrier maintenance. Structurally, JAML contains two extracellular immunoglobulin domains, a single transmembrane region, and a cytoplasmic tail that interacts with intracellular signaling molecules. It is prominently expressed in tissues with tight junctions, such as epithelial surfaces, vascular endothelia, and immune cells like T lymphocytes and dendritic cells.
JAML gained attention for its dual functions in cellular adhesion and immune modulation. It interacts with the co-receptor CAR (Coxsackievirus and Adenovirus Receptor) to mediate cell adhesion, particularly at epithelial junctions. In immune contexts, JAML binds to the integrin α4β1 on T cells, facilitating their activation and migration. This makes JAML a key player in inflammatory responses and immune homeostasis. Dysregulation of JAML has been implicated in autoimmune diseases, chronic inflammation, and cancer progression.
Recombinant JAML proteins are engineered using expression systems (e.g., mammalian, insect, or bacterial cells) to study its structure-function relationships and therapeutic potential. These purified proteins retain native binding capabilities, enabling research into JAML-mediated signaling pathways and ligand interactions. Applications include in vitro studies of epithelial barrier dynamics, T-cell activation assays, and screening for therapeutic antibodies or small molecules targeting JAML-associated diseases. Recent studies explore its role in cancer immunotherapy, particularly in modulating tumor microenvironments and immune checkpoint regulation. As a research tool, recombinant JAML contributes to understanding fundamental biological processes while holding translational promise for inflammatory disorders and immune-oncology.
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