L1CAM Antibody (2702C) [Alexa Fluor® 594]

This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

L1CAM (Neural cell adhesion molecule L1, also known as L1, CD171 and NCAM-L1) is a founding member of the L1 family, Immunoglobulin (Ig) superfamily of molecules (1-4). It was initially described as a 200-230 kDa neural adhesion molecule that likely played a key role in mouse nervous system development (4-6). Subsequent studies have confirmed the adhesive nature of the molecule, and expanded its activities in both neural and nonneural cell types. L1 is now recognized to play a key role in cell migration, adhesion, neurite outgrowth, myelination and neuronal differentiation (1, 7, 8). It does so through a series of cis and trans interactions that involve multiple copartners and target receptors (1, 3, 6, 8). Cells known to express L1 are varied, and include immature oligodendrocytes (9), CD4+ T cells, B cells and monocytes (10), both motor and sensory Schwann cells (11, 12), intestinal epithelial progenitor cells (12), cerebellar granule and Purkinje cells (5, 13, 14), and multiple tumor cells such as melanoma (15) plus pancreatic duct and lung carcinoma cells (16, 17). Human L1 was first identified as a 215 kDa glycoprotein on the surface of SKNAS neuroblastoma cells (18). Subsequent cloning established its precursor as being 1257 amino acids (aa) in length (19, 20). The molecule is a type I transmembrane (TM) protein that contains an 1101 aa extracellular region (aa 20-1120) plus a 114 aa cytoplasmic domain (aa 1144-1257). The extracellular region possesses six C2-type Ig-like domains (aa 35-607) followed by five fibronectin (FN) type III domains (aa 612-1108). As noted, L1 participates in multiple cis and trans interactions, and some of these interaction sites have been mapped to select Ig or FN domains. For instance, Ig-like domains #1, 2 and 6 associate with NP-1, L1 (homotypic binding), and various integrins, respectively (21‑23). The latter interaction is mediated by one (in human) or two (in mouse) RGD motifs (23, 24). Other molecules that heterotypically associate with L1 include NCAM, neurocan, CD24 and EGFR. The cytoplasmic tail contains no kinase motifs, but does possess a FIGQY peptide that interacts with ankyrin, and an RSLE sequence that mediates clathrin-associated endocytosis (1). There are two splice variants, one each in the intracellular and extracellular domains.  A deletion of RSLE adversely affects endocytosis, while a Leu substitution for aa 26-31 interfers with numerous heterotypic interactions (25, 26).  In general, the full-length L1 molecule is a neuron-associated isoform. L1 is known to undergo proteolysis, either by plasmin or ADAMs. This generates soluble isoforms of varying sizes (140-200 kDa) that retain bioactivity, and which can be incorporated into the surrounding ECM (5, 13, 27-30). The membrane fragments (30-80 kDa) undergo further processing, most importantly by gamma -secretase, to generate a soluble 28 kDa intracellular domain. This domain is SUMOylated, and believed to possess an NLS at Lys1147.  Upon presumed entry into the nucleus, L1 is posited to activate L1-responsive genes. Human and mouse L1 precursors share 88% aa sequence identity.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Array FAB7773T

• L1CAM Antibodies
• L1CAM Antibody Pair
• L1CAM ELISA Kit
• L1CAM Lysate
• L1CAM Proteins
• L1CAM Proteins and Enzymes