纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | L1CAM |
Uniprot No | P32004-3 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 20-1115aa |
氨基酸序列 | IQIPEELMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGV HFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAM SHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNS KILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEP IDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTI KWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHA YYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVE ELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQL PAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERF FPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGP RSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDG RLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLH LLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTS TTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGE GNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLV VSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEIL NSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVP ANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEAL HLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPE LRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNIS ATAGENYSVVSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSS YTQWDLQPDTDYEIHLFKERMFRHQMAVKTNGTGRVRLPPAGFATELEHH HHHH |
预测分子量 | 124 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L1CAM重组蛋白的参考文献及其摘要概括:
1. **文献名称**:*"Recombinant L1-CAM enhances axonal regeneration and functional recovery after spinal cord injury"*
**作者**:Chen et al.
**摘要**:研究通过在大鼠脊髓损伤模型中表达重组L1CAM蛋白,发现其显著促进轴突再生和运动功能恢复,机制涉及激活神经元内Src/ERK信号通路。
2. **文献名称**:*"Purification and functional characterization of soluble L1CAM extracellular domain in tumor cell adhesion"*
**作者**:Silletti et al.
**摘要**:报道了从HEK293细胞中纯化可溶性L1CAM胞外域重组蛋白的方法,并证明其通过整合素相互作用增强肿瘤细胞黏附与迁移,提示其在癌症转移中的潜在作用。
3. **文献名称**:*"Structural basis of L1CAM homophilic interaction and Alzheimer's disease-related mutations"*
**作者**:Schäfer et al.
**摘要**:通过X射线晶体学解析了重组人源L1CAM胞外域的结构,揭示了其同源结合界面的关键氨基酸,并发现阿尔茨海默病相关突变会破坏其介导的细胞间粘附。
*注:以上文献信息为基于公开研究的概括性描述,实际引用时建议通过学术数据库核对原文细节。*
L1CAM (L1 cell adhesion molecule) is a transmembrane glycoprotein belonging to the immunoglobulin (Ig) superfamily, first identified for its critical role in neural development. It consists of six Ig-like domains, five fibronectin type III (FnIII) repeats, a transmembrane region, and a cytoplasmic tail. L1CAM mediates cell-cell and cell-matrix interactions through homophilic and heterophilic binding, influencing axon guidance, neuronal migration, and synaptic plasticity. Its functions extend beyond the nervous system, contributing to cancer progression, angiogenesis, and immune regulation.
Dysregulation of L1CAM is linked to neurological disorders (e.g., CRASH syndrome) and multiple cancers, where it promotes metastasis, chemoresistance, and stemness. These pathological associations have driven interest in recombinant L1CAM proteins for research and therapeutic development. Recombinant L1CAM is typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, though bacterial or insect cell systems are occasionally used for specific applications. The protein can be engineered as full-length or truncated variants (e.g., extracellular domain-only forms) to study structure-function relationships.
Applications include in vitro binding assays, cell migration studies, and animal models to investigate L1CAM's role in disease mechanisms. It also serves as a tool for antibody validation, drug screening, and biomarker discovery. Notably, recombinant L1CAM has been utilized to develop blocking antibodies and peptide inhibitors targeting its extracellular domains, particularly the Ig1 and Ig2 regions critical for homophilic interactions. Recent work explores its potential in regenerative medicine, leveraging its neurite-outgrowth-promoting properties. Despite progress, challenges remain in mimicking native conformational states and understanding isoform-specific effects, driving ongoing optimization of recombinant production platforms.
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