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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 Kits (22) and CBLN1 Proteins (7) and many more products for this protein.
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Human Polyclonal CBLN1 Primary Antibody for IHC (fro), WB - ABIN2472947
Urade, Oberdick, Molinar-Rode, Morgan: Precerebellin is a cerebellum-specific protein with similarity to the globular domain of complement C1q B chain. in Proceedings of the National Academy of Sciences of the United States of America 1991
Show all 3 Pubmed References
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.
Results show that Cbln1, Cbln2, and Cbln4 (show CBLN4 Antibodies) are abundantly expressed in nearly all brain regions, but exhibit strikingly different expression patterns and developmental dynamics. Using newly generated knockin reporter mice for Cbln2 and Cbln4 (show CBLN4 Antibodies), we find that Cbln2 and Cbln4 (show CBLN4 Antibodies) are not universally expressed in all neurons, but only in specific subsets of neurons.
results suggest that gene and seizure interactions in ventral tegmental area glutamatergic neurons impair sociability by downregulating Cbln1, a key node in the expanding protein interaction network of autism genes
Despites its well known role in motor coordination and motor learning, whether and how the cerebellum is involved in cognitive functions remains less clear. Cerebellin 1 (Cbln1) is highly expressed in the cerebellum and serves as an essential synaptic organizer. Although genes encoding Cbln1 and its receptor are associated with many psychiatric disorders, it remains unknown whether such cognitive impairments are caused by
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 Antibodies) 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 Antibodies), specifically bind to neurexin (show NRXN1 Antibodies) 1alpha and -beta and induce synaptogenesis in cerebellar, hippocampal and cortical neurons in vitro.
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