|Detection of Mouse CHL‑1/L1CAM‑2 by Western Blot. Western blot shows lysates of mouse brain stem tissue. PVDF membrane was probed with 0.25 µg/mL of Goat Anti-Mouse CHL‑1/L1CAM‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2147) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for CHL‑1/L1CAM‑2 at approximately 200 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Detection of Mouse CHL‑1/L1CAM‑2 by Simple WesternTM. Simple Western lane view shows lysates of mouse brain (cortex) tissue and mouse brain stem tissue, loaded at 0.2 mg/mL. A specific band was detected for CHL‑1/L1CAM‑2 at approximately 196-201 kDa (as indicated) using 2.5 µg/mL of Goat Anti-Mouse CHL‑1/L1CAM‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2147) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the |
12-230 kDa separation system.
Close homolog of L1 (CHL-1), also known as cell adhesion L1-like (CALL) and L1 cell adhesion molecule 2 (L1CAM-2), belongs to the L1 subfamily of immunoglobulin (Ig) superfamily cell adhesion molecules, which also includes L1, neurofascin and NgCAM-related cell adhesion molecule (NrCAM) (1‑3). These molecules are type I transmembrane proteins that have 6 Ig-like domains and 4‑5 fibronectin type III-like (FNIII) domains in their extracellular regions. They also share a highly conserved cytoplasmic region of approximately 110 amino acid (aa) residues containing an ankyrin-binding site. CHL-1 is expressed as a highly glycosylated 185 kDa transmembrane protein by subpopulations of neurons and glia of the central and peripheral nervous system (4, 5). Ectodomain shedding via the metalloprotease-disintegrin ADAM8 releases 165 kDa and 125 kDa soluble CHL-1 fragments, which can diffuse away to function at distant sites (6). CHL-1 is not capable of homotypic interactions, but an extracellular binding partner of CHL-1 has not been identified (4). Human CHL1 has been mapped to chromosome 3p26 and is a candidate gene for 3p- syndrome characterized by mental impairment (7). A missense CHL1 polymorphism associated increased risk of schizophrenia, has also been reported (8). The functional importance of CHL-1 in the nervous system is also evident in CHL-1 deficient mice, which display behavioral abnormalities and show misguided axons within the hippocampus and olfactory tract (9). Enhanced ectodomain-shedding of CHL-1 is also observed in Wobbler mice, the neurodegenerative mutant mice (6). In vitro, soluble or substrate-coated CHL-1 promotes neurite outgrowth and neuronal survival of both cerebellar and hippocampal neurons. Cell surface CHL-1 interacts with integrins in cis to potentiate integrin-dependent cell migration toward extracellular matrix proteins (10). For this enhanced cell motility, CHL-1 linkage to the actin cytoskeleton via interaction between ankyrin and the CHL-1 cytoplasmic region is required.
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Western Blot: Mouse CHL‑1/L1CAM‑2 Antibody [AF2147]
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