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 (HRI). 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 and is obtained by proprietary chromatographic techniques.
Reconstitution
Reconstituted in ddH2O at 100 ug/mL.
Formulation
Lyophilized after extensive dialysis against PBS.
Molecular Weight
12.7 kDa, observed by reducing SDS-PAGE.
Source
E. coli
Host
Human
Accession Number
Q9NRC9
Endotoxin Level
0.2 EU/ug, determined by LAL method.
Notes
For research use only
Bioactivity
Data not available.
Synonyms
FDP, MIAL
Sequence
MVHGIFMDRL ASKKLCADDE CVYTISLASA QEDYNAPDCRFINVKKGQQI YVYSKLVKEN GAGEFWAGSV YGDGQDEMGVVGYFPRNLVK EQRVYQEATK EVPTTDIDFF CE
Purity
95% by SDS-PAGE analysis.
Storage
Lyophilized recombinant human Otoraplin (rhOTOR) remains stable up to 6 months at lower than -70°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.