Recombinant Human Otoferlin (OTOF) Protein (His)

Name: Recombinant Human Otoferlin (OTOF) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07050P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Otoferlin (OTOF) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9HC10
Target Symbol	OTOF
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KVPLPEDVSREAGYDSTYGMFQGIPSNDPINVLVRVYVVRATDLHPADINGKADPYIAIRLGKTDIRDKENYISKQLNPVFGKSFDIEASFPMESMLTVAVYDWDLVGTDDLIGETKIDLENRFYSKHRATCGIAQTYSTHGYNIWRDPMKPSQILTRLCKDGKVDGPHFGPPGRVKVANRVFTGPSEIEDENGQRKPTDEHVALLALRHWEDIPRAGCRLVPEHVETRPLLNPDKPGIEQGRLELWVDMFPMDMPAPGTPLDISPRKPKKYELRVIIWNTDEVVLEDDDFFTGEKSSDIFVRGWLKGQQEDKQDTDVHYHSLTGEGNFNWRYLFPFDYLAAEEKIVISKKESMFSWDETEYKIPARLTLQIWDADHFSADDFLGAIELDLNRFPRGAKTAKQCTMEM
Expression Range	1461-1868aa
Protein Length	Partial
Mol. Weight	52.6 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion and in the control of neurotransmitter release at these output synapses. Interacts in a calcium-dependent manner to the presynaptic SNARE proteins at ribbon synapses of cochlear inner hair cells (IHCs) to trigger exocytosis of neurotransmitter. Also essential to synaptic exocytosis in immature outer hair cells (OHCs). May also play a role within the recycling of endosomes.
Subcellular Location	Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Cell junction, synapse, presynaptic cell membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein.
Protein Families	Ferlin family
Database References	HGNC: 8515 OMIM: 601071 KEGG: hsa:9381 STRING: 9606.ENSP00000272371 UniGene: Hs.91608
Associated Diseases	Deafness, autosomal recessive, 9 (DFNB9); Auditory neuropathy, autosomal recessive, 1 (AUNB1)
Tissue Specificity	Isoform 1 and isoform 3 are found in adult brain. Isoform 2 is expressed in the fetus and in adult brain, heart, placenta, skeletal muscle and kidney.

Gene Functions References

two mutations-c.5098G > C (p.Glu1700Gln) and c.1702C > T (p.Arg568Trp)-in the OTOF gene were found to be correlated with ANSD. PMID: 30368385
ConclusionOur findings implicate OTOF as a potential major contributor to hearing loss in the Saudi population, while highlighting the low contribution of GJB2, thus offering important considerations for clinical testing strategies for Saudi patients. PMID: 29048421
This study suggested considerable genetic heterogeneity in the causation of hearing loss in Dhadkai. Recessive mutations were observed in at least three genes causing hearing loss: OTOF (p.R708X), SLC26A4 (p.Y556X) and CLDN14 (p.V85D). Mutation p.R708X appeared to be the major cause of hearing impairment in Dhadkai. PMID: 29434063
Although both otoferlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type calcium channel Cav1.3. PMID: 28696301
three unrelated 2 to 6 year-old children who were diagnosed as auditory neuropathy patients who complained of severe hearing loss when they had fever had otoferlin (OTOF) homozygous or compound heterozygous mutations with the genotypes c.2975_2978delAG/c.4819C>T, c.4819C>T/c.4819C>T, or c.2382_2383delC/c.1621G>A PMID: 26778470
The authors conclude that the TRC40 pathway is critical for hearing and propose that otoferlin is an essential substrate of this pathway in hair cells. PMID: 27458190
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. PMID: 27729456
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 PMID: 26818607
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 PMID: 27652356
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. PMID: 28335750
Mutations in RAI1, OTOF, and SLC26A4 may have roles in nonsyndromic hearing loss in Altaian families in Siberia PMID: 27082237
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. PMID: 24814232
audiological phenotype associated with different OTOF mutations appears to be consistently different suggesting the presence of a genotype-phenotype correlation PMID: 24746455
The C2F and C2C domains of otoferlin preferentially bind phosphatidylinositol 4,5-bisphosphate (4,5)P2. PMID: 24999532
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. PMID: 24135434
OTOF gene mutataion is found in a Chinese patient with auditory neuropathy spectrum disorder. PMID: 24001616
The six probable pathogenic variants of OTOF genes were novel: 2 nonsense mutations (p.W717X, p.S1368X) and 4 missense mutations (p.D450E, p.R1583H, p.V1778I, p. E1803A). PMID: 24053799
The study concludes that OTOF mutations are not the major cause of autosomal recessive nonsyndromic hearing loss in the Iranian population. PMID: 22906306
nine different mutations of OTOF were detected(seven of them were novel)in Japanese patients with auditory neuropathy PMID: 22575033
Otoferlin is a multi-C2 domain protein associated with genetic human deafness. It functions in hair-cell exocytosis. Several otoferlin C2 domains bind to Ca2+, phospholipids, & proteins. Review. PMID: 22959777
OTOF and PJVK gene variants have a role in auditory neuropathy spectrum disorder in Chinese patients PMID: 21935370
OTOF does not seem to contribute to the pathogenesis of autosomal dominant auditory neuropathy in this family study. PMID: 18035737
The predominance of the p.E1700Q mutation and the evidence of its founder effect indicate a distinct OTOF mutation spectrum in Taiwanese patients with auditory neuropathy. PMID: 20224275
The mutatuion screening confirms that the OTOF gene contributes to auditory neuropathy and to termperature-sensitive auditory neuropathy. PMID: 20504331
Purpose of this paper is to analyse OTOF gene in a series of subjects affected by auditory neuropathy. Genetic analysis identified five new mutations. PMID: 20211493
This study revealed a novel mutation p.Glu1804del in exon 44 of OTOF. The mutation was found to be homozygous in the three patients and segregated with the temperature-dependent deafness within the family. PMID: 20230791
Mutations in the OTOF gene are frequent causes of auditory neuropathy in Brazil and our results confirm that they are spread worldwide. PMID: 19461658
mechano-electrical transduction and cochlear amplification are normal in patients with OTOF mutations. Potentials are consistent with decreased neurotransmitter release resulting in abnormal dendritic activation and impairment of auditory nerve firing. PMID: 19636622
Q829X, a novel mutation in OTOF, is the third most frequent mutation causing prelingual non-syndromic hearing loss reported so far in the Spanish population. PMID: 12114484
Substitutions in the conserved Ca-binding C2C domain of otoferlin cause DFNB9, a form of nonsyndromic autosomal recessive deafness. 2 new mutations were found in exon 15 of the long splice form: 490 (Pro > Gln) and 515 (Ile > Thr. PMID: 12127154
There are uncommon cytidine-homopolymer dimorphisms in 5'-UTR of the human otoferlin gene. PMID: 12469219
Mutations in the OTOF gene cause a non-syndromic recessive auditory neuropathy. PMID: 12525542
Mutations in OTOF cause both profound hearing loss and a type of hearing loss where otoacoustic emissions are spared called auditory neuropathy. PMID: 16371502
Otoferlin is essential for a late step of synaptic vesicle exocytosis and may act as the major Ca(2+) sensor triggering membrane fusion at the auditory inner hair cell ribbon synapse. PMID: 17055430
Results confirm that mutation of the OTOF gene correlates with a phenotype of prelingual, profound nonsyndromic hearing impairment, and indicate that OTOF mutations are a major cause of inherited auditory neuropathy. PMID: 18381613
Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3. PMID: 19004828
we demonstrate the existence of an alternative splice isoform of OTOF expressed in the human cochlea PMID: 19250381

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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