Overview
L1 Cell Adhesion Molecule (L1CAM) is a transmembrane glycoprotein belonging to the immunoglobulin superfamily. First identified in neural tissues, it consists of six immunoglobulin-like domains, five fibronectin type III repeats, and intracellular phosphorylation sites. The molecule mediates cell-cell and cell-matrix interactions through homophilic (L1-L1) and heterophilic binding partners like integrins and neuropilin-1. Genetic mutations in L1CAM cause CRASH syndrome (Corpus Callosum Hypoplasia, Retardation, Adducted thumbs, Spastic paraplegia, and Hydrocephalus), underscoring its developmental importance. Beyond neurology, L1CAM overexpression correlates with tumor progression in various cancers, making it a therapeutic target and diagnostic marker.
Physical and Chemical Properties
As a glycoprotein, L1CAM's molecular weight varies (200-220 kDa) due to N-linked glycosylation. The extracellular domain (≈1,100 amino acids) confers binding specificity, while the cytoplasmic tail interacts with ankyrin and cytoskeletal proteins. The protein is stable at pH 7-8 but degrades under reducing conditions or prolonged room-temperature exposure. Commercial preparations typically contain L1CAM in phosphate-buffered saline (PBS) or Tris buffers with stabilizers like bovine serum albumin (BSA). For research, recombinant forms (human/mouse) are produced in HEK293 or CHO cells, with endotoxin levels <1 EU/μg. Analytical methods include Western blot (under non-reducing conditions), ELISA, and surface plasmon resonance for binding assays.
Main Applications
In neuroscience, L1CAM facilitates axon guidance during development and promotes neuronal survival. Researchers use it to coat culture surfaces for enhanced neurite outgrowth in primary neuron studies. Knockout models demonstrate its role in corticospinal tract formation and synaptic plasticity. Oncology studies exploit L1CAM's role in epithelial-mesenchymal transition (EMT), where its overexpression in cancers (e.g., ovarian, colorectal) predicts metastasis. Therapeutic antibodies against L1CAM are in preclinical trials. Additionally, L1CAM-functionalized biomaterials show promise in spinal cord injury repair by directing axonal regeneration across lesion sites.
Safety and Storage
L1CAM itself poses minimal biological hazard (Biosafety Level 1), but associated experimental systems (e.g., viral transduction) may require higher containment. Avoid inhalation of lyophilized powder and direct skin contact, as repeated exposure may induce sensitization. For storage, aliquot liquid forms to prevent freeze-thaw damage. Lyophilized protein is stable for 2-3 years at -20°C; reconstituted solutions retain activity for 1 month at 4°C with protease inhibitors. Verify activity via cell adhesion assays if stored long-term. Shipping typically requires dry ice for long-distance transport.
B2B Procurement Guide
When sourcing L1CAM, prioritize vendors providing Certificates of Analysis (CoA) detailing purity (SDS-PAGE/Coomassie), endotoxin levels, and functional validation data (e.g., neurite outgrowth promotion). Recombinant tags (Fc, His) affect applications—tag removal may be necessary for structural studies. Bulk purchases (10+ mg) often reduce unit costs by 30-40%. Consider GMP-grade for clinical applications ($1,000+/mg). For cell culture, carrier-free versions prevent serum protein interference. Emerging suppliers offer mutant variants (e.g., R184Q for adhesion studies) or species-specific isoforms (chick, zebrafish) for comparative biology.
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