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CBLN1 encodes a cerebellum-specific precursor protein, precerebellin, with similarity to the globular (non-collagen-like) domain of complement component C1qB. Additionally we are shipping CBLN1 Antibodies (38) and CBLN1 Proteins (8) and many more products for this protein.
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Cbln1 and Cbln2 are co-expressed in the endolysosomal compartment of the thalamic neurons responsible for the synaptic alterations in striatum of Cbln1-null mice.
amplitude and frequency of mIPSCs were increased in cbln1-null cerebellar slices.
This study provides evidence for involvement of Cbln1 in nociception and provides a platform for continued exploration of involvement of novel neuropeptides in the regulation of nociceptive transmission
extracerebellar structures or remaining PF-PC synapses in cbln1(-/-) mice may be sufficient for the expression, maintenance, and extinction of its memory trace.
Cbln1 released from parallel fiber Purkinje cells induces dynamic structural changes in parallel fibers.
[review] The Cbln1-GluRdelta2 (show GRID2 ELISA Kits) receptor complex is located at the cleft of parallel fiber-Purkinje cell synapses and bidirectionally regulates both presynaptic and postsynaptic differentiation.
GluRdelta1 stimulated inhibitory synapse formation in the presence of Cbln1 or Cbln2
Data show that Cbln1 and Cbln2, but not Cbln4 (show CBLN4 ELISA Kits), specifically bind to neurexin (show NRXN1 ELISA Kits) 1alpha and -beta and induce synaptogenesis in cerebellar, hippocampal and cortical neurons in vitro.
These results suggest that Cbln1 and Cbln2 play a role in synapse formation of cortical neurons by interacting with NRXNs containing S4.
Otolin 1 interacts with otoconial matrix protein Otoconin-90 (show OC90 ELISA Kits) and Cerebellin-1 in the inner ear.
Our observation that loss of Cbln1 leads to increased numbers of striatal medium spiny neurons' dendritic spines suggests that modulating thalamostriatal Cbln1 may be a novel means of improving symptoms or slowing progression in Parkinson's disease.
This gene encodes a cerebellum-specific precursor protein, precerebellin, with similarity to the globular (non-collagen-like) domain of complement component C1qB. Precerebellin is processed to give rise to several derivatives, including the hexadecapeptide, cerebellin, which is highly enriched in postsynaptic structures of Purkinje cells. Cerebellin has also been found in human and rat adrenals, where it has been shown to enhance the secretory activity of this gland.
, cerebellin 1
, cerebellin 1 precursor
, cerebellin 1 precursor protein
, precerebellin 1
, brain protein D3