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anti-Human Otoferlin Antibodies:
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Mouse (Murine) Polyclonal Otoferlin Primary Antibody for IHC - ABIN1742371
Vogl, Cooper, Neef, Wojcik, Reim, Reisinger, Brose, Rhee, Moser, Wichmann: Unconventional molecular regulation of synaptic vesicle replenishment in cochlear inner hair cells. in Journal of cell science 2015
The authors conclude that the TRC40 (show ASNA1 Antibodies) pathway is critical for hearing and propose that otoferlin is an essential substrate of this pathway in hair cells.
In Otof(I515T/I515T) inner hair cells (IHCs), otoferlin levels are diminished by 65%, synaptic vesicles are enlarged, and exocytosis during prolonged stimulation is strongly reduced indicating that otoferlin is critical for the reformation of properly sized and fusion-competent synaptic vesicles.
Our results confirmed that mutations in OTOF gene were a major cause of congenital Auditory neuropathy spectrum disorder (ANSD) in China. Identification of OTOF mutations can facilitate diagnosis, clinical intervention and counseling for congenital ANSD
findings suggest that the mutation found in C2C domain of the OTOF gene is likely to cause deafness in the studied family reflecting the importance of C2 domains of otoferlin in hearing loss
Two mutations in the otoferlin gene, nonsense mutation p.R425X, contributes to a premature stop codon, may result in a truncated polypeptide, which strongly suggests its pathogenicity for auditory neuropathy spectrum disorder. The missense mutation p.L1665P results in a single amino acid substitution in a highly conserved region.
Mutations in RAI1 (show DOM3Z Antibodies), OTOF, and SLC26A4 (show SLC26A4 Antibodies) may have roles in nonsyndromic hearing loss in Altaian families in Siberia
Our observation of the discordant audiologic phenotype within the same DFNB9 family is more likely due to the loss of OAE over time rather than a genotype-phenotype correlation.
audiological phenotype associated with different OTOF mutations appears to be consistently different suggesting the presence of a genotype-phenotype correlation
The C2F (show EMG1 Antibodies) and C2C domains of otoferlin preferentially bind phosphatidylinositol 4,5-bisphosphate (4,5)P2.
We characterize a novel otoferlin mutation discovered in a sibling pair diagnosed with auditory neuropathy spectrum disorder and investigate auditory nerve function through their cochlear implants.
Furthermore, this F-actin mesh network attached to the synaptic ribbons directly influences the efficiency of otoferlin-dependent exocytosis and its sensitivity to intracellular hydrostatic pressure.
Mice that carry a mutation in a calcium binding domain of Otoferlin, the putative calcium sensor at hair cell synapses, have normal distortion product otoacoustic emissions (DPOAEs), but auditory brain stem responses (ABRs) are absent.
a direct role for otoferlin in exocytosis and modulation of calcium-dependent membrane fusion
The analysis of otoferlin knockout mice gave the 1st insights into its function in inner hair cell calcium-dependent exocytosis & type-i vestibular hair cells. Review.
Co-localization studies revealed an overlap of Ergic2 (show ERGIC2 Antibodies) and Otoferlin signals in IHCs and neurons of cerebral cortical layer I making Ergic2 (show ERGIC2 Antibodies) the promising binding candidate
Otoferlin deletion does not affect transmitter release at hippocampal synapses.
Otoferlin is a calcium sensor that can directly regulate soluble N-ethyl-maleimide sensitive fusion protein attachment protein receptor-mediated membrane fusion reactions.
Otoferlin underlies highly efficient calcium ion-dependent membrane fusion, a process likely essential to increase the probability and synchrony of vesicle fusion events at the mature inner hair cell ribbon synapse.
Deficient vesicle replenishment underlies the hearing impairment of Otof(Pga/Pga) mice. Otoferlin may confer the high capacity for vesicle re-supply to the inner hair cell synapse.
Otoferlin is essential for a late step of synaptic vesicle exocytosis and may act as the major Ca(2 (show CA2 Antibodies)+) sensor triggering membrane fusion at the auditory inner hair cell ribbon synapse.
Mutations in this gene are a cause of neurosensory nonsyndromic recessive deafness, DFNB9. The short form of the encoded protein has 3 C2 domains, a single carboxy-terminal transmembrane domain found also in the C. elegans spermatogenesis factor FER-1 and human dysferlin, while the long form has 6 C2 domains. The homology suggests that this protein may be involved in vesicle membrane fusion. Several transcript variants encoding multiple isoforms have been found for this gene.
, fer-1-like protein 2
, otoferlin transcript variant 46-48