Otoraplin Protein (OTOR) (AA 18-128)
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- Target See all Otoraplin (OTOR) Proteins
- Otoraplin (OTOR)
- Protein Type
- Recombinant
- Protein Characteristics
- AA 18-128
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Characteristics
- AA 18-128, expressed with an N-terminal Met.
- Purity
- > 95 % by SDS-PAGE analysis.
- Endotoxin Level
- < 0.2 EU/μg, determined by LAL method.
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Reconstituted in ddH2O at 100 μg/mL.
- Buffer
- Lyophilized after extensive dialysis against PBS.
- Storage
- -80 °C
- Storage Comment
- Lyophilized recombinant human Otoraplin (rhOTOR) remains stable up to 6 months at -80 °C from date of receipt. Upon reconstitution, rhOTOR remains stable up to 2 weeks at 4 °C or up to 3 months at -20 °C.
- Expiry Date
- 6 months
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- Target
- Otoraplin (OTOR)
- Abstract
- OTOR Products
- Synonyms
- FDP Protein, MIAL1 Protein, CDRAP Protein, Fdp Protein, MIA Protein, MIAL Protein, MGC133655 Protein, MGC86203 Protein, otoraplin Protein, otoraplin L homeolog Protein, OTOR Protein, Otor Protein, otor.L Protein, otor Protein
- Background
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Otoraplin (OTOR) is a cytokine first identified in 2000 and encodes a small protein of 128 amino acids with an SH3 domain. OTOR is a homologue to CD-RAP/MIA and contains a hydrophobic N-terminal region as a signal peptide, which indicates that OTOR is mainly secreted. Researchers found that high expression of OTOR is only seen in the cochlea, demonstrating its importance in hearing. Indeed, loss of the gene produces cochlear dysfunction and otosclerosis, a hearing disorder involving the bony tissue of the ear. OTOR exerts an influence on the surrounding otic capsule and functions in the extracellular matrix of the membranous portion of the cochlea. Recombinant human Otoraplin (rhOTOR) produced in E. coli is a single non-glycosylated polypeptide chain containing 112 amino acids. rhOTOR has a molecular mass of 12.7 kDa analyzed by reducing SDS-PAGE.
Synonyms: FDP, MIAL - Molecular Weight
- 12.7 kDa, observed by reducing SDS-PAGE.
- UniProt
- Q9NRC9
- Pathways
- Sensory Perception of Sound, Regulation of Carbohydrate Metabolic Process
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