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The product of NYX belongs to the small leucine-rich proteoglycan (SLRP) family of proteins. Additionally we are shipping Nyctalopin Antibodies (28) and Nyctalopin Kits (1) and many more products for this protein.
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Nyctalopin is essential for synaptic transmission in the cone dominated zebrafish retina.
Two Novel NYX Gene Mutations in the Chinese Families with X-linked Congenital Stationary Night Blindness were described.
Four potential pathogenic variations in the NYX gene were found in four families with high myopia with or without CSNB1.
Loss of ERG (show ERG Proteins) amplitude and apparent ON-pathway dysfunction at high temporal frequencies distinguish this patient with a Trp237Ter NYX mutation from those with other previously reported NYX mutations.
A mutation was identified in NYX in 20 male patients with Congenital Stationary Night Blindness 1.
The results expand the mutation spectrum of NYX, CACNA1F (show CACNA1F Proteins) and GRM6 (show GRM6 Proteins). They also suggest that NYX mutations are a common cause of congenital stationary night blindness (CSNB (show CSN2 Proteins)).
A proteomic search for proteins associated with nyctalopin in the retina identified TRPM1 (show TRPM1 Proteins) as the binding partner and nyctalopin additionally interacts with mGluR6 (show GRM6 Proteins) receptor.
Phenotypic expression of the complete type of X-linked congenital stationary night blindness in patients with different mutations in the NYX gene.
Seven in-frame deletion, splicing, missense, nonsense, and frameshift mutations were identified segregating with X-linked congenital stationary night blindness in the NYX gene.
Human and mouse nyctalopin are membrane-bound extracellular proteins and are functionally conserved.
The results implicated a specific on-pathway signaling deficiency in CSNB1-NYX males with no evidence of off-pathway involvement. Likewise, rapid-on/off ramping stimuli also indicated that the functional deficit was localized to the on pathway.
murine nyctalopin is anchored to the plasma membrane by a single transmembrane domain, such that the leucin-rich repeat domain is located in the extracellular space.
The results of this study suggested that the nyctalopin is acting as an accessory TRP (show TYRP1 Proteins) channel subunit critical for proper channel localization to the synapse.
The nob phenotype is caused by an 85-bp deletion in the mouse nyx gene, which encodes the nyctalopin protein.
These data suggest an important function of the Nyx protein in the inner retina and provide evidence that CSNB1 is based on a defect in the inner retinal circuitry.
Absence of nyctalopin does not disrupt the expression pattern of other proteins known to be required for synaptic transmission.
No differences in nob mice and carriers suggesting equal susceptibility to light-induced photoreceptor degeneration.
The product of this gene belongs to the small leucine-rich proteoglycan (SLRP) family of proteins. Defects in this gene are the cause of congenital stationary night blindness type 1 (CSNB1), also called X-linked congenital stationary night blindness (XLCSNB). CSNB1 is a rare inherited retinal disorder characterized by impaired scotopic vision, myopia, hyperopia, nystagmus and reduced visual acuity. The role of other SLRP proteins suggests that mutations in this gene disrupt developing retinal interconnections involving the ON-bipolar cells, leading to the visual losses seen in patients with complete CSNB.
, leucine-rich repeat protein
, no b wave