Recombinant Mouse Otoferlin (OTOF) Protein (His&Myc)

Name: Recombinant Mouse Otoferlin (OTOF) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07239P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Otoferlin (OTOF) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9ESF1
Target Symbol	OTOF
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	KVPLPEDVSREAGYDPTYGMFQGIPSNDPINVLVRIYVVRATDLHPADINGKADPYIAIKLGKTDIRDKENYISKQLNPVFGKSFDIEASFPMESMLTVAVYDWDLVGTDDLIGETKIDLENRFYSKHRATCGIAQTYSIHGYNIWRDPMKPSQILTRLCKEGKVDGPHFGPHGRVRVANRVFTGPSEIEDENGQRKPTDEHVALSALRHWEDIPRVGCRLVPEHVETRPLLNPDKPGIEQGRLELWVDMFPMDMPAPGTPLDISPRKPKKYELRVIVWNTDEVVLEDDDFFTGEKSSDIFVRGWLKGQQEDKQDTDVHYHSLTGEGNFNWRYLFPFDYLAAEEKIVMSKKESMFSWDETEYKIPARLTLQIWDADHFSADDFLGAIELDLNRFPRGAKTAKQCTMEM
Expression Range	1461-1868aa
Protein Length	Partial
Mol. Weight	54.2 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. Note=Detected at basolateral cell membrane with synaptic vesicles surrounding the ribbon and at the presynaptic plasma membrane in the inner hair cells (IHCs) at postnatal day 30 (P30). Colocalizes with GPR25 and RAB8B in inner hair cells.
Protein Families	Ferlin family
Database References	KEGG: mmu:83762 STRING: 10090.ENSMUSP00000073803 UniGene: Mm.244502
Tissue Specificity	Isoform 1 is expressed in cochlea and brain. Expressed in the cochlear and vestibular hair cells. Expressed in both inner and outer hair cells (IHCs and OHCs) and cochlear ganglions neurons at postnatal day 2 (P2) and 6 (P6). Expressed only in IHCs at pos

Gene Functions References

Otoferlin thus functions as a Ca(2+) sensor, setting the rates of primed vesicle fusion with the presynaptic plasma membrane and synaptic vesicle pool replenishment in the inner hair cell active zone. PMID: 29111973
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. PMID: 26568308
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. PMID: 25253474
a direct role for otoferlin in exocytosis and modulation of calcium-dependent membrane fusion PMID: 24478316
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. PMID: 22959777
Co-localization studies revealed an overlap of Ergic2 and Otoferlin signals in IHCs and neurons of cerebral cortical layer I making Ergic2 the promising binding candidate PMID: 22613993
Otoferlin deletion does not affect transmitter release at hippocampal synapses. PMID: 21451027
Otoferlin is a calcium sensor that can directly regulate soluble N-ethyl-maleimide sensitive fusion protein attachment protein receptor-mediated membrane fusion reactions. PMID: 20921140
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. PMID: 20926654
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. PMID: 20562868
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
Missense mutation of Otof underlies deafness phenotype of ENU-induced deaf5 mutation. PMID: 17967520
Otoferlin, the putative major calcium sensor at inner hair cell ribbon synapses, is also essential to synaptic exocytosis in immature outer hair cells. PMID: 18287496
Otoferlin-Rab8b interaction links otoferlin to the basolateral endocytic and secretory trafficking. PMID: 18772196
Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3. PMID: 19004828
Otoferlin and myosin VI mutant showed a reduced basolateral synaptic surface area and altered topography of the inner hair cell. PMID: 19417007
Otoferlin is essential for a high-affinity Ca(2+) sensor function that allows efficient and linear encoding of low-intensity stimuli at the vestibular hair cell synapse. PMID: 19710301

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.