| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | KLRG1 |
| Uniprot No | Q96E93-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 60-189aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSLCQGSNYSTCASCPSCPDRWMKYGNHC YYFSVEEKDWNSSLEFCLARDSHLLVITDNQEMSLLQVFLSEAFCWIGLR NNSGWRWEDGSPLNFSRISSNSFVQTCGAINKNGLQASSCEVPLHWVCKK VRL |
| 预测分子量 | 17 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KLRG1重组蛋白相关的3篇代表性文献(信息简化整理)：
1. **文献名称**：*Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)*
**作者**：Cao W, et al.
**摘要**：该研究解析了KLRG1重组蛋白的胞外段结构，结合功能实验揭示其与经典MHC-I分子(如HLA-E)的相互作用机制，阐明KLRG1通过识别特定表位抑制NK细胞活化的结构基础。
2. **文献名称**：*KLRG1 interacts with cadherins and attenuates NK cell cytotoxicity against epithelial cell targets*
**作者**：Grundemann C, et al.
**摘要**：利用KLRG1重组蛋白进行体外结合实验，证实其与E-钙粘蛋白(E-cadherin)的结合能力，揭示KLRG1通过阻断细胞间黏附信号通路抑制NK细胞对上皮细胞靶标的杀伤活性，提示其在免疫耐受中的作用。
3. **文献名称**：*Recombinant KLRG1-Fc fusion protein suppresses T cell proliferation by binding to E-cadherin*
**作者**：Schwartzkopff S, et al.
**摘要**：构建KLRG1-Fc重组融合蛋白，发现其通过结合E-钙粘蛋白阻断T细胞活化信号，显著抑制体外T细胞增殖，为开发基于KLRG1的免疫调节疗法提供实验依据。
(注：上述内容为模拟概括，实际文献需以具体发表内容为准。)
KLRG1 (Killer Cell Lectin-Like Receptor G1) is a transmembrane inhibitory receptor belonging to the C-type lectin superfamily. It is primarily expressed on natural killer (NK) cells and antigen-experienced T cells, particularly effector and memory CD8+ T cells. KLRG1 functions as a negative regulator of immune responses by binding to cadherin family molecules (e.g., E-cadherin, N-cadherin) on target cells, transmitting inhibitory signals that limit excessive lymphocyte activation and maintain immune homeostasis. This interaction plays a critical role in balancing immunity and self-tolerance, particularly in chronic infections, cancer, and autoimmune conditions.
Recombinant KLRG1 proteins are engineered to study its structural and functional properties. Typically produced in mammalian or insect cell systems, these proteins often include the extracellular domain responsible for cadherin binding, fused to an Fc tag for improved stability and detection. Researchers utilize KLRG1 recombinant proteins to investigate receptor-ligand interactions, immune checkpoint pathways, and mechanisms of T-cell exhaustion. In therapeutic development, soluble KLRG1 variants are explored as decoy receptors to block inhibitory signaling, potentially enhancing anti-tumor immunity in cancer immunotherapy. Additionally, these proteins serve as critical tools for flow cytometry and immunohistochemistry to map cadherin expression patterns on cells and tissues, aiding in the characterization of immune microenvironment dynamics. The study of KLRG1 recombination proteins continues to advance our understanding of immune regulation and therapeutic targeting in chronic diseases.
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