Recombinant Mouse L1CAM Fc Chimera Protein, CF

Recombinant Mouse L1CAM Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: L1CAM

Neural cell adhesion molecule L1 (NCAM‑L1; also L1‑CAM, L1, and CD171) is a 200 ‑ 220 kDa type I transmembrane glycoprotein of the immunoglobulin superfamily and L1/neurofascin/NgCAM family (1, 2). NCAM-L1 is expressed by neurons, especially by growing axons on their growth cones (2). Non-neuronal cells such as Schwann cells, astrocytes, epithelial cells, and cells of myelomonocytic and lymphoid origin also express NCAM-L1 (2). Full length mouse NCAM-L1 is synthesized as a 1260 amino acid (aa) precursor that contains a 19 aa signal sequence, a 1104 aa extracellular domain (ECD), a 23 aa transmembrane region, and a 114 aa cytoplasmic tail that is highly conserved (3). The ECD contains six Ig-like C2-type domains, five fibronectin type III domains, and 21 potential sites for N‑linked glycosylation. Mouse NCAM-L1 shares 88% aa sequence identity with human NCAM-L1. NCAM-L1 is critical for neural development.  Specifically, NCAM-L1 plays a key role in neuronal cell migration, axon outgrowth, axon fasciculation, synaptogenesis, and myelination (4). NCAM-L1 mediates hemophilic cell-cell interaction but also binds heterophilic ligands like axonin-1, CD24, CD9, neurocan and several integrins (4). It has been shown that NCAM-L1 can undergo membrane-proximal cleavage by ADAM10 and ADAM17, leading to the release of the soluble extracellular domain and the generation of a membrane-bound stub (4). Remaining intact, the soluble extracellular domain has been suggested to serve as a substrate for integrin-mediated cell adhesion, thereby stimulating cellular motility and cell migration (4). It has also been found that NCAM‑L1 plays a role in the ontogeny of human tumors and its expression is linked to poor prognosis (1). Over‑expression promotes tumor-cell invasion and motility, growth in nude mice and tumor metastasis (1). Research shows that proteolytic processing by ADAM10 and presenilin/ gamma -secretase is essential for the nuclear signaling of NCAM-L1 in human carcinoma cell lines (1). Defects in NCAM-L1 are the cause of MASA syndrome (mental retardation, aphasia, shuffling gait and adducted thumbs), which is also known as CRASH syndrome (corpus callosum hypoplasia, psychomotor retardation, adducted thumbs, spastic paraparesis and hydrocephalus (5, 6).

Related Research Areas

• Adhesion Molecules in Angiogenesis
• B Cell Chemotaxis, Migration, and Adhesion
• Cancer Biomarkers
• Cancer Stem Cell Markers
• Dendritic Cell Adhesion and Migration
• Epithelial Cell Markers and Intracellular Molecules
• Immunoglobulin Superfamily CAMs
• Monocyte Markers
• Neuronal Lineage Markers
• Neuronal Markers
• Semaphorins, Plexin Receptors, and Related Molecules
• Surface Ectodermal Cells
• Synaptic Adhesion Molecules
• Synaptic Proteins
• T Cell Migration/Adhesion