| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | LRIG1 |
| Uniprot No | P70193 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-794aa |
| 氨基酸序列 | MARPGPGVLG APRLAPRLLL WLLLLLLQWP ESAGAQAGPR APCAAACTCA GDSLDCSGRG LATLPRDLPS WTRSLNLSYN RLSEIDSAAF EDLTNLQEVY LNSNELTAIP SLGAASIGVV SLFLQHNKIL SVDGSQLKSY LSLEVLDLSS NNITEIRSSC FPNGLRIREL NLASNRISIL ESGAFDGLSR SLLTLRLSKN RITQLPVKAF KLPRLTQLDL NRNRIRLIEG LTFQGLDSLE VLRLQRNNIS RLTDGAFWGL SKMHVLHLEY NSLVEVNSGS LYGLTALHQL HLSNNSISRI QRDGWSFCQK LHELILSFNN LTRLDEESLA ELSSLSILRL SHNAISHIAE GAFKGLKSLR VLDLDHNEIS GTIEDTSGAF TGLDNLSKLT LFGNKIKSVA KRAFSGLESL EHLNLGENAI RSVQFDAFAK MKNLKELYIS SESFLCDCQL KWLPPWLMGR MLQAFVTATC AHPESLKGQS IFSVLPDSFV CDDFPKPQII TQPETTMAVV GKDIRFTCSA ASSSSSPMTF AWKKDNEVLA NADMENFAHV RAQDGEVMEY TTILHLRHVT FGHEGRYQCI ITNHFGSTYS HKARLTVNVL PSFTKIPHDI AIRTGTTARL ECAATGHPNP QIAWQKDGGT DFPAARERRM HVMPDDDVFF ITDVKIDDMG VYSCTAQNSA GSVSANATLT VLETPSLAVP LEDRVVTVGE TVAFQCKATG SPTPRITWLK GGRPLSLTER HHFTPGNQLL VVQNVMIDDA GRYTCEMSNP LGTERAHSQL SILPTPGCRK DGTT |
| 预测分子量 | 85 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LRIG1重组蛋白的3篇代表性文献(信息基于公开研究总结，非真实文献，仅作示例参考)：
1. **文献名称**：*LRIG1 extracellular domain shedding by ADAM proteases promotes LRIG1 inhibition of EGFR signaling*
**作者**：Gur et al.
**摘要**：研究揭示了ADAM蛋白酶介导的LRIG1重组蛋白胞外域脱落机制，证明可溶性LRIG1片段通过抑制EGFR二聚化负调控肿瘤细胞增殖。
2. **文献名称**：*Recombinant LRIG1 ectodomain suppresses growth of oral squamous cell carcinoma by blocking ErbB signaling*
**作者**：Wang et al.
**摘要**：体外实验表明，重组LRIG1胞外域蛋白通过结合ErbB受体(如EGFR和HER2)，抑制下游MAPK/AKT通路，减少头颈鳞癌细胞侵袭。
3. **文献名称**：*Structural basis of LRIG1-EGFR interaction for targeted cancer therapy*
**作者**：Zhang et al.
**摘要**：通过X射线晶体学解析重组LRIG1与EGFR复合物结构，揭示其结合界面，为基于LRIG1的EGFR靶向药物设计提供依据。
如需具体文献，建议在PubMed或Web of Science中检索关键词“LRIG1 recombinant”或“soluble LRIG1”获取最新研究。
LRIG1 (Leucine-rich repeats and immunoglobulin-like domains protein 1) is a transmembrane protein belonging to the LRIG family, which includes LRIG1. LRIG2. and LRIG3. It is characterized by leucine-rich repeats (LRRs) in its extracellular domain and an immunoglobin-like (Ig-like) domain, which mediate protein-protein interactions. LRIG1 functions as a negative regulator of receptor tyrosine kinases (RTKs), particularly the epidermal growth factor receptor (EGFR/ERBB) family, by promoting receptor ubiquitination and degradation through interactions with E3 ubiquitin ligases. This regulatory role positions LRIG1 as a potential tumor suppressor, with its downregulation or loss of expression linked to cancer progression, poor prognosis, and therapeutic resistance in various malignancies, including glioblastoma, breast cancer, and squamous cell carcinoma.
Recombinant LRIG1 protein, produced via expression systems such as mammalian cells, *E. coli*, or insect cells, retains functional domains critical for binding RTKs and modulating downstream signaling. Its production often involves codon optimization, affinity tag fusion (e.g., Fc or His tags), and purification via chromatography to ensure stability and bioactivity. Research applications include *in vitro* studies to dissect RTK signaling mechanisms, screen for therapeutic agents, or develop LRIG1-based biologics. Additionally, recombinant LRIG1 has shown promise in preclinical models for inhibiting oncogenic signaling and enhancing the efficacy of targeted therapies. Beyond cancer, LRIG1 is implicated in stem cell regulation and tissue homeostasis, expanding its relevance to regenerative medicine. Despite its therapeutic potential, challenges remain in optimizing delivery methods and understanding context-dependent interactions within diverse cellular environments.
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