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We identified 9 novel CNTNAP1 variants in 6 families: three missense variants, four nonsense variants, one frameshift variant and one splice site variant. Significant polyhydramnios occurred in 6/7 pregnancies
E. coli exploits Caspr1 as a host receptor for penetration of the blood-brain barrier, resulting in meningitis
In two brothers with severe congenital hypotonia and foot deformities, we identified compound heterozygous variants in CNTNAP1, reporting the first causative missense variant, p.(Cys323Arg). Motor nerve conductions were markedly decreased.
CNTNAP1 mutations were found to induce characteristic ultrastructural lesions of the paranodal region.
report a consanguineous Arab family from Qatar with three children having an early lethal form of arthrogryposis multiplex congenita and a novel frameshift mutation in CNTNAP1
Mutations in CNTNAP1 and ADCY6 are responsible for severe arthrogryposis multiplex congenita with axoglial defects
VDAC1 and CNTNAP1 associate with gamma-secretase in detergent-resistant membranes and affect amyloid precursor protein processing.
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
These data suggest that NgR1 may regulate axo-myelin ultrastructure through Caspr-mediated adhesion, regulating the electrophysiological signature of myelinated axons of central nervous system.
In Caspr1 mutants, there was a reduction in conductive properties of peripheral myelinated fibers and neuromuscular junction disintegration.
Caspr as a novel key regulator that controls the temporal specification of cell fate in radial glial cells of the developing cerebral cortex through Notch signaling
Simultaneous deletion of Caspr and Caspr2 disrupts the internodal organization of Kv1.2.
Caspr co-localizes and interacts with APP. Amyloid-beta (Abeta) 40 and Abeta42 generation were also reduced in HEK-APP cells by Caspr overexpression.
Caspr labeling was observed through much of the retina, including horizontal, bipolar, amacrine, and ganglion cells.
Clustering of Caspr at initial contact sites between OL processes and the axon requires glial expression of NF155 but not of contactin. Expression of membrane proteins along the axolemma is determined by the type of the contacting glial cells.
These results suggest that Caspr serves as a "transmembrane scaffold" that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon.
F3/contactin and caspr/paranodin traffic to the cell surface via a non-conventional pathway
Nogo-A interacts in trans with axonal Caspr at CNS paranodes, an interaction that may have a role in modulating axon-glial junction architecture and possibly K(+)-channel localization during development.
the Caspr/Cont complex is essential for the formation of axoglial SJ
Caspr protein is required for recruitment and retention of KCNQ4 at calyceal synapses in vestibular hair cells.
The Caspr gene has been identified in the neurological mutant shambling (shm) mouse and shown to encode the contactin-associated protein, which is a major component of the paranodal junction in myelinated nerves.
These results show a critical role for NCP1 in the delineation of specific axonal domains and the axon-glia interactions required for normal saltatory conduction.
Both NCP1 and CGT mutants develop large swellings accompanied by cytoskeletal disorganization and degeneration in the axons of cerebellar Purkinje neurons.
The gene product was initially identified as a 190-kD protein associated with the contactin-PTPRZ1 complex. The 1,384-amino acid protein, also designated p190 or CASPR for 'contactin-associated protein,' includes an extracellular domain with several putative protein-protein interaction domains, a putative transmembrane domain, and a 74-amino acid cytoplasmic domain. Northern blot analysis showed that the gene is transcribed predominantly in brain as a transcript of 6.2 kb, with weak expression in several other tissues tested. The architecture of its extracellular domain is similar to that of neurexins, and this protein may be the signaling subunit of contactin, enabling recruitment and activation of intracellular signaling pathways in neurons.
contactin associated protein 1
, contactin-associated protein 1-like
, contactin-associated protein 1
, neurexin 4
, neurexin IV
, neurexin 4 (contactin associated protein)