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This gene encodes one of the major intermediate filament proteins of mature astrocytes. It is used as a marker to distinguish astrocytes from other glial cells during development. Mutations in this gene cause Alexander disease, a rare disorder of astrocytes in the central nervous system. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Oct 2008]

This gene encodes one of the major intermediate filament proteins of mature astrocytes. It is used as a marker to distinguish astrocytes from other glial cells during development. Mutations in this gene cause Alexander disease, a rare disorder of astrocytes in the central nervous system. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Oct 2008]

Neuroligins are a family of plasma membrane proteins that possess an N-terminal hydrophobic domain, a large esterase homology domain, a single transmembrane region, a short cytoplasmic domain, and an EF-hand binding domain (1,2). Members of the neuroligin family include Neuroligin 1, Neuroligin 2 and Neuroligin 3. Neuroligins are expressed in excitatory neuronal synaptic clefts. Neuroligins play a role in the formation and remodeling of CNS synapses by binding to b-neurexins, a family of neu

CKAP4 is a substrate of DHHC2, a putative tumor suppressor. CK MNF116 and CKAP4 were useful in identifying squamous cell carcinomas with single cell infiltration. These results suggest a role for CKAP4 in tumor.

AviTag, a peptide allowing biotinylation by the enzyme BirA and so the protein can be isolated by streptavidin (GLNDIFEAQKIEWHE)

FcRN present in the intestinal epithelium of neonatal mice and rats mediates the selective uptake of immunoglobulin G (IgG) in mothers' milk, thereby helping newborn animals to acquire passive immunity. FcRn (also designated FCGRT, Brambell receptor, FcRn å chain, IgG Gc receptor and neonatal Fc-receptor) is comprised of a heavy chain and ∫-2-Microglobulin. FcRn heavy chain shows approximately 35% amino acid identity to an MHC class I molecule. FcRN localizes in endosomes of vascular