| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LIME1 |
| Uniprot No | Q9H400 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-295aa |
| 氨基酸序列 | MGLPVSWAPPALWVLGCCALLLSLWALCTACRRPEDAVAPRKRARRQRARLQGSATAAEASLLRRTHLCSLSKSDTRLHELHRGPRSSRALRPASMDLLRPHWLEVSRDITGPQAAPSAFPHQELPRALPAAAATAGCAGLEATYSNVGLAALPGVSLAASPVVAEYARVQKRKGTHRSPQEPQQGKTEVTPAAQVDVLYSRVCKPKRRDPGPTTDPLDPKGQGAILALAGDLAYQTLPLRALDVDSGPLENVYESIRELGDPAGRSSTCGAGTPPASSCPSLGRGWRPLPASLP |
| 预测分子量 | 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LIME1重组蛋白的3篇模拟参考文献(实际文献可能需根据具体研究补充)：
1. **文献名称**：*LIME1: A Novel Transmembrane Adaptor Protein in T Cell Signaling*
**作者**：Brückner S. et al.
**摘要**：研究首次报道了LIME1作为T细胞中的跨膜接头蛋白，通过重组蛋白技术证实其与Csk激酶相互作用，并参与调控T细胞受体下游的磷酸化信号通路。
2. **文献名称**：*Structural and Functional Analysis of Recombinant LIME1 in B Cell Activation*
**作者**：Müller P., et al.
**摘要**：通过表达LIME1重组蛋白，揭示了其胞内结构域中酪氨酸磷酸化位点的功能，证明LIME1在B细胞活化中通过招募SHP-1磷酸酶负向调控信号传导。
3. **文献名称**：*Recombinant LIME1 Protein Binds to Lipid Rafts and Modulates Immune Synapse Formation*
**作者**：Lee H., Kim T.
**摘要**：利用重组LIME1蛋白进行体外结合实验，发现其通过N端结构域靶向脂筏区域，并影响免疫突触的稳定性，为LIME1在抗原呈递中的作用提供证据。
注：以上为示例性内容，实际文献需通过PubMed/Google Scholar检索确认。
LIME1 (Lck-interacting transmembrane adapter 1) is a transmembrane signaling protein primarily expressed in immune cells, notably T lymphocytes and B cells. It belongs to the family of adapter proteins that lack intrinsic enzymatic activity but facilitate signal transduction by recruiting and organizing signaling molecules. Discovered in the early 2000s, LIME1 gained attention for its role in T-cell receptor (TCR)-mediated signaling. Structurally, it contains an extracellular immunoglobulin-like domain, a single transmembrane helix, and a cytoplasmic tail with multiple tyrosine phosphorylation sites. These sites interact with Src homology 2 (SH2) domain-containing proteins, including the Src-family kinase Lck, which is critical for TCR activation.
LIME1 is implicated in modulating immune cell activation and downstream signaling pathways. Upon TCR engagement, LIME1 undergoes phosphorylation, enabling its interaction with signaling molecules like Grb2 and phospholipase C-γ1 (PLC-γ1), thereby influencing calcium mobilization, cytokine production, and cell proliferation. Studies suggest its involvement in both positive and negative regulatory mechanisms, depending on cellular context and phosphorylation status. Dysregulation of LIME1 has been loosely associated with autoimmune disorders and lymphoproliferative diseases, though its exact pathophysiological role remains under investigation.
Recombinant LIME1 protein is engineered for in vitro studies to dissect its molecular interactions, structure-function relationships, and role in immune signaling cascades. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it serves as a tool for binding assays, kinase activity studies, and antibody development. Research leveraging recombinant LIME1 has advanced understanding of immune receptor signaling complexity, offering potential insights into therapeutic targets for immune-related pathologies. Its study continues to bridge gaps in adapter protein biology and signal transduction networks.
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