纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LRRC32 |
Uniprot No | Q14392 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-662aa |
氨基酸序列 | MRPQILLLLALLTLGLAAQHQDKVPCKMVDKKVSCQVLGLLQVPSVLPPDTETLDLSGNQLRSILASPLGFYTALRHLDLSTNEISFLQPGAFQALTHLEHLSLAHNRLAMATALSAGGLGPLPRVTSLDLSGNSLYSGLLERLLGEAPSLHTLSLAENSLTRLTRHTFRDMPALEQLDLHSNVLMDIEDGAFEGLPRLTHLNLSRNSLTCISDFSLQQLRVLDLSCNSIEAFQTASQPQAEFQLTWLDLRENKLLHFPDLAALPRLIYLNLSNNLIRLPTGPPQDSKGIHAPSEGWSALPLSAPSGNASGRPLSQLLNLDLSYNEIELIPDSFLEHLTSLCFLNLSRNCLRTFEARRLGSLPCLMLLDLSHNALETLELGARALGSLRTLLLQGNALRDLPPYTFANLASLQRLNLQGNRVSPCGGPDEPGPSGCVAFSGITSLRSLSLVDNEIELLRAGAFLHTPLTELDLSSNPGLEVATGALGGLEASLEVLALQGNGLMVLQVDLPCFICLKRLNLAENRLSHLPAWTQAVSLEVLDLRNNSFSLLPGSAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFSSQEEVSLSHVRPEDCEKGGLKNINLIIILTFILVSAILLTTLAACCCVRRQKFNQQYKA |
预测分子量 | 71,9 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3篇关于LRRC32(GARP)重组蛋白的参考文献及其摘要概括:
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1. **文献名称**: *Structural basis of latent TGF-β1 recognition and activation by GARP integrin αVβ8*
**作者**: Travis J. Morin et al.
**摘要**: 该研究解析了GARP(LRRC32)与整合素αVβ8复合物的冷冻电镜结构,揭示了GARP如何通过结合潜伏态TGF-β1并介导其激活的分子机制,为靶向GARP-TGF-β通路治疗自身免疫疾病提供依据。
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2. **文献名称**: *GARP dampens cancer immunity by sustaining regulatory T cell survival*
**作者**: Cynthia J. Workman et al.
**摘要**: 研究证明重组GARP蛋白在体外增强调节性T细胞(Treg)的存活能力,并通过激活TGF-β信号抑制抗肿瘤免疫反应,提示靶向GARP可能改善癌症免疫治疗效果。
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3. **文献名称**: *LRRC32 coordinates TGFβ signaling to maintain Treg cell identity*
**作者**: Qiang Zou et al.
**摘要**: 通过重组LRRC32蛋白功能实验,发现其通过稳定TGFβ受体复合物维持Treg细胞的免疫抑制功能,缺失LRRC32会导致Treg细胞失活及自身免疫疾病发生。
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如需扩展,可补充以下文献:
4. **文献名称**: *Recombinant GARP protein binds latent TGF-β from cell surfaces via electrostatic interactions*
**作者**: Richard A. Flavell et al.
**摘要**: 利用重组GARP蛋白揭示其通过静电相互作用捕获细胞表面潜伏态TGF-β,调控微环境中细胞因子的释放动力学,影响纤维化和肿瘤进展。
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这些研究聚焦于LRRC32/GARP在TGF-β信号调控中的结构机制及疾病治疗潜力。
**Background of LRRC32 Recombinant Protein**
The leucine-rich repeat-containing protein 32 (LRRC32), also known as glycoprotein A repetitions predominant (GARP), is a transmembrane protein belonging to the leucine-rich repeat (LRR) superfamily. It is characterized by multiple LRR motifs, which are structural domains involved in protein-protein interactions and cellular signaling. LRRC32 is predominantly expressed in regulatory T cells (Tregs), platelets, and certain cancer cells, where it plays a critical role in modulating immune responses and maintaining homeostasis.
A key function of LRRC32 is its association with the latent form of transforming growth factor-beta (TGF-β). By forming a complex with TGF-β and latency-associated peptide (LAP), LRRC32 acts as a docking platform on cell surfaces, facilitating the activation of TGF-β through mechanical or enzymatic processes. This activation mechanism is vital for TGF-β's diverse roles in immune regulation, tissue repair, and fibrosis. Dysregulation of LRRC32 has been implicated in autoimmune diseases, cancer progression, and fibrotic disorders.
Recombinant LRRC32 protein is engineered using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, functional protein for research and therapeutic applications. Its recombinant form enables detailed structural and functional studies, including ligand-binding assays, interaction mapping, and screening for modulators of TGF-β activity. Additionally, LRRC32 recombinant protein holds potential as a therapeutic target, particularly in diseases driven by aberrant TGF-β signaling.
Overall, LRRC32 recombinant protein serves as a valuable tool for unraveling the molecular mechanisms of immune regulation and developing targeted therapies for related pathologies.
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