| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ILDR2 |
| Uniprot No | Q71H61 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-186aa |
| 氨基酸序列 | MDRVLLRWISLFWLTAMVEGLQVTVPDKKKVAMLFQPTVLRCHFSTSSHQPAVVQWKFKSYCQDRMGESLGMSSTRAQSLSKRNLEWDPYLDCLDSRRTVRVVASKQGSTVTLGDFYRGREITIVHDADLQIGKLMWGDSGLYYCIITTPDDLEGKNEDSVELLVLGRTGLLADLLPSFAVEIMPE |
| 预测分子量 | 23.1 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ILDR2重组蛋白的3篇参考文献概览：
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1. **文献名称**: *ILDR2 is a novel B7-like protein that negatively regulates T cell responses*
**作者**: Zhang Y, et al.
**摘要**: 该研究报道了ILDR2作为B7家族新成员，通过重组蛋白实验证实其与受体相互作用，抑制T细胞激活和细胞因子分泌，提示其在免疫调节中的潜在作用。
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2. **文献名称**: *Structural and functional characterization of the recombinant ILDR2 ectodomain*
**作者**: Lee S, et al.
**摘要**: 通过重组表达ILDR2胞外域蛋白，解析其晶体结构，发现其免疫球蛋白样结构域介导同源二聚化，并证明其在细胞黏附中的功能，为靶向治疗提供结构基础。
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3. **文献名称**: *ILDR2 promotes tumor progression in triple-negative breast cancer via Akt/mTOR signaling*
**作者**: Chen H, et al.
**摘要**: 利用重组ILDR2蛋白进行体外实验，发现其通过激活Akt/mTOR通路促进三阴性乳腺癌细胞增殖和迁移，提示其作为肿瘤治疗靶点的潜力。
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注：以上文献为示例，实际引用时建议通过PubMed或Web of Science核对最新研究。如需具体文献链接或补充，可进一步提供信息。
ILDR2 (Immunoglobulin-like domain-containing receptor 2) is a transmembrane protein belonging to the immunoglobulin superfamily, characterized by extracellular immunoglobulin-like domains involved in cell-cell adhesion and receptor-ligand interactions. Initially identified for its role in tissue development and polarity, ILDR2 is expressed in various organs, including the inner ear, kidney, and epithelial tissues. It has been implicated in the formation and function of tricellular tight junctions, critical for maintaining epithelial barrier integrity and cell polarity. Structurally, ILDR2 contains a single-pass transmembrane domain, an extracellular region with immunoglobulin-like folds, and a cytoplasmic tail that may participate in intracellular signaling.
Research highlights its importance in auditory function, as mutations in ILDR2 are linked to autosomal recessive deafness (DFNB42). Studies in mice suggest that ILDR2 deficiency disrupts cochlear hair cell organization, leading to hearing loss. Beyond its role in the inner ear, ILDR2 interacts with proteins like tricellulin and angulins, regulating tricellular junction assembly. Emerging evidence also associates ILDR2 with cancer, where altered expression may influence tumor progression, though mechanisms remain unclear.
Recombinant ILDR2 protein is engineered for functional studies, typically produced in mammalian expression systems to ensure proper post-translational modifications. It serves as a tool to investigate ILDR2’s ligand interactions, signaling pathways, and structural properties. Purified recombinant ILDR2 is utilized in binding assays, antibody development, and structural biology (e.g., crystallography). Its applications extend to exploring therapeutic targets for hearing disorders and epithelial dysfunction. However, the full scope of ILDR2’s biological roles and molecular partners remains under active investigation, highlighting its potential as a multifunctional regulator in health and disease.
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