纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | LY9 |
Uniprot No | Q9HBG7 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 48-454aa |
氨基酸序列 | KDSAPTVVSGILGGSVTLPLNISVDTEIENVIWIGPKNALAFA RPKENVTIMVKSYLGRLDIT KWSYSLCISN LTLNDAGSYK AQINQRNFEVTTEEEFTLFVYEQLQEPQVTMKSVKVSENFSCNITLMCSV KGAEKSVLYSWTPREPHASESNGGSILTVSRTPCDPDLPYICTAQNPVSQ RSSLPVHVGQFCTDPGASRGGTTGETVVGVLGEPVTLPLALPACRDTEKV VWLFNTSIISKEREEAATADPLIKSRDPYKNRVWVSSQDCSLKISQLKIE DAGPYHAYVCSEASSVTSMTHVTLLIYRRLRKPKITWSLRHSEDGICRIS LTCSVEDGGN TVMYTWTPLQKEAVVSQGES HLNVSWRSSE NHPNLTCTAS NPVSRSSHQFLSENICSGPERNTK |
预测分子量 | 39 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LY9重组蛋白的虚构参考文献示例,基于合理推测的研究方向整理:
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1. **标题**:*Structural Characterization of Recombinant LY9 Extracellular Domain and Its Interaction with SLAMF6*
**作者**:Smith, J.R. et al.
**期刊**:*Journal of Biological Chemistry* (2018)
**摘要**:本研究通过X射线晶体学解析了LY9重组蛋白胞外域的三维结构,揭示了其独特的Ig样结构域排列。实验证实LY9与SLAMF6蛋白通过特定表位结合,为理解其在T/B细胞免疫突触中的作用提供了结构基础。
2. **标题**:*LY9 Recombinant Protein Modulates B Cell Activation via Synergistic Signaling with CD19*
**作者**:Zhang, L. et al.
**期刊**:*Immunity* (2020)
**摘要**:利用LY9重组蛋白和基因敲除小鼠模型,研究发现LY9与CD19共定位于B细胞表面,协同增强PI3K-Akt信号通路,促进B细胞增殖及抗体分泌,提示其在适应性免疫中的调控作用。
3. **标题**:*Targeting LY9 with Recombinant Fusion Protein Attenuates Autoimmunity in Lupus-Prone Mice*
**作者**:Patel, S. et al.
**期刊**:*Nature Communications* (2021)
**摘要**:通过构建LY9-Fc重组融合蛋白,研究团队证明其可阻断LY9与配体的病理相互作用,显著降低MRL/lpr小鼠模型的肾脏炎症和自身抗体水平,为治疗系统性红斑狼疮提供了新策略。
4. **标题**:*LY9 Recombinant Protein as a Biomarker for Lymphoma Progression*
**作者**:Kim, Y. et al.
**期刊**:*Blood* (2022)
**摘要**:分析弥漫大B细胞淋巴瘤患者样本发现,LY9重组蛋白的高表达与肿瘤侵袭性正相关。体外实验显示LY9通过ERK通路促进细胞迁移,提示其作为预后标志物和治疗靶点的潜力。
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注:上述文献为虚构示例,实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。
**Background of LY9 Recombinant Protein**
LY9 (also known as SLAMF3 or CD229) is a member of the signaling lymphocytic activation molecule (SLAM) family, a group of cell-surface receptors involved in modulating immune responses. These proteins play critical roles in immune cell communication, particularly in T-cell and B-cell activation, adhesion, and homeostasis. LY9 is expressed predominantly on lymphocytes, including T cells, B cells, and dendritic cells, and interacts with specific ligands to regulate both activating and inhibitory signals in immune pathways.
Structurally, LY9 features an extracellular region with two immunoglobulin-like domains (V and C2 types), a transmembrane domain, and a cytoplasmic tail containing immunoreceptor tyrosine-based switch motifs (ITSMs). These motifs recruit adaptor proteins like SAP (SLAM-associated protein), facilitating downstream signaling. LY9’s dual role in immune regulation—enhancing lymphocyte activation while also contributing to immune tolerance—has made it a focus in studies of autoimmune diseases, immunodeficiency disorders, and cancer immunotherapy.
Recombinant LY9 protein is engineered *in vitro* using expression systems (e.g., mammalian cells or *E. coli*) to produce soluble, functional forms of the protein for research and therapeutic development. It retains the ligand-binding capability of native LY9. enabling studies on receptor-ligand interactions, immune synapse formation, and signaling mechanisms. In drug discovery, recombinant LY9 serves as a tool for screening antibodies or small molecules targeting LY9-mediated pathways. Recent studies explore its potential as a biomarker or therapeutic target, particularly in contexts like lupus or lymphoproliferative diseases.
Efforts to optimize LY9 recombinant protein focus on purity, stability, and post-translational modifications to mimic native functionality, ensuring relevance in both basic research and clinical applications.
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