| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LRIG3 |
| Uniprot No | Q6UXM1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1119aa |
| 氨基酸序列 | MSAPSLRARAAGLGLLLCAVLGRAGRSDSGGRGELGQPSGVAAERPCPTTCRCLGDLLDCSRKRLARLPEPLPSWVARLDLSHNRLSFIKASSMSHLQSLREVKLNNNELETIPNLGPVSANITLLSLAGNRIVEILPEHLKEFQSLETLDLSSNNISELQTAFPALQLKYLYLNSNRVTSMEPGYFDNLANTLLVLKLNRNRISAIPPKMFKLPQLQHLELNRNKIKNVDGLTFQGLGALKSLKMQRNGVTKLMDGAFWGLSNMEILQLDHNNLTEITKGWLYGLLMLQELHLSQNAINRISPDAWEFCQKLSELDLTFNHLSRLDDSSFLGLSLLNTLHIGNNRVSYIADCAFRGLSSLKTLDLKNNEISWTIEDMNGAFSGLDKLRRLILQGNRIRSITKKAFTGLDALEHLDLSDNAIMSLQGNAFSQMKKLQQLHLNTSSLLCDCQLKWLPQWVAENNFQSFVNASCAHPQLLKGRSIFAVSPDGFVCDDFPKPQITVQPETQSAIKGSNLSFICSAASSSDSPMTFAWKKDNELLHDAEMENYAHLRAQGGEVMEYTTILRLREVEFASEGKYQCVISNHFGSSYSVKAKLTVNMLPSFTKTPMDLTIRAGAMARLECAAVGHPAPQIAWQKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDIGVYSCTAQNSAGSISANATLTVLETPSFLRPLLDRTVTKGETAVLQCIAGGSPPPKLNWTKDDSPLVVTERHFFAAGNQLLIIVDSDVSDAGKYTCEMSNTLGTERGNVRLSVIPTPTCDSPQMTAPSLDDDGWATVGVVIIAVVCCVVGTSLVWVVIIYHTRRRNEDCSITNTDETNLPADIPSYLSSQGTLADRQDGYVSSESGSHHQFVTSSGAGFFLPQHDSSGTCHIDNSSEADVEAATDLFLCPFLGSTGPMYLKGNVYGSDPFETYHTGCSPDPRTVLMDHYEPSYIKKKECYPCSHPSEESCERSFSNISWPSHVRKLLNTSYSHNEGPGMKNLCLNKSSLDFSANPEPASVASSNSFMGTFGKALRRPHLDAYSSFGQPSDCQPRAFYLKAHSSPDLDSGSEEDGKERTDFQEENHICTFKQTLENYRTPNFQSYDLDT |
| 预测分子量 | 123 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LRIG3重组蛋白的3篇参考文献及简要摘要概括：
1. **文献名称**：*LRIG3 modulates proliferation, apoptosis, and invasion in glioblastoma cells by regulating the EGFR/AKT signaling pathway*
**作者**：Zhang Y, et al.
**摘要**：该研究通过重组LRIG3蛋白实验，发现其过表达可抑制胶质母细胞瘤细胞的增殖和侵袭能力，并通过调控EGFR/AKT信号通路诱导细胞凋亡，提示LRIG3可能作为肿瘤治疗的潜在靶点。
2. **文献名称**：*Recombinant LRIG3 extracellular domain inhibits angiogenesis by antagonizing VEGF/VEGFR2 signaling*
**作者**：Wang L, et al.
**摘要**：研究利用重组LRIG3胞外域蛋白，证明其通过结合VEGF受体(VEGFR2)阻断血管内皮生长因子(VEGF)信号传导，抑制体内外血管生成，为抗血管生成治疗提供了新策略。
3. **文献名称**：*Structural and functional characterization of LRIG3 reveals its role in neuronal development*
**作者**：Chen H, et al.
**摘要**：通过重组LRIG3蛋白的结构解析和体外实验，发现LRIG3通过调控神经突触相关蛋白(如ErbB受体)的活性，促进神经元轴突生长和突触形成，揭示其在神经系统发育中的关键作用。
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**备注**：以上文献为示例性内容，实际文献需通过PubMed或专业数据库检索确认。若需具体论文，建议以关键词“LRIG3 recombinant protein”或“LRIG3 function”在学术平台(如NCBI、ScienceDirect)查询近年研究。
LRIG3 (Leucine-rich Repeats and Immunoglobulin-like Domains 3) is a member of the LRIG protein family, which includes LRIG1. LRIG2. and LRIG3. These transmembrane glycoproteins are characterized by leucine-rich repeats (LRRs) in their extracellular domains and immunoglobulin-like (Ig-like) folds, which facilitate protein-protein interactions. LRIG3 is primarily involved in regulating receptor tyrosine kinase (RTK) signaling pathways, such as EGFR and MET, through direct binding or modulation of receptor trafficking and degradation. It acts as a tumor suppressor in certain cancers, with studies linking its altered expression to glioblastoma, melanoma, and other malignancies.
Recombinant LRIG3 protein is engineered for research applications, typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications. This engineered protein retains functional domains critical for interaction with RTKs and downstream signaling components. Researchers utilize recombinant LRIG3 to investigate its role in cellular processes like proliferation, differentiation, and apoptosis, particularly in cancer biology and neural development contexts. Its inhibitory effects on oncogenic RTK pathways have sparked interest in therapeutic development, including potential use as a biomarker or targeted therapy component. However, the precise molecular mechanisms of LRIG3 remain less characterized compared to LRIG1. highlighting the need for further study. Current applications extend to in vitro binding assays, structural studies, and functional screens to identify novel interaction partners or signaling networks influenced by LRIG3 activity.
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