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OS9 encodes a protein that is highly expressed in osteosarcomas. Additionally we are shipping OS9 Antibodies (65) and many more products for this protein.
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OS-9 regulates the secretory transport of TRPV4 (show TRPV4 Proteins) and appears to protect TRPV4 (show TRPV4 Proteins) subunits from the precocious ubiquitination and ER-associated degradation.
Data suggest renal cell lines exhibit an OS9-mediated ERAD (endoplasmic reticulum-associated degradation) pathway that degrades Nkcc2/Slc12a1 (solute carrier family 12 member 1 (show SLC12A1 Proteins)) prior to glycosylation/processing.
The depletion of OS-9 in 3T3-L1 adipocytes impaired cell function in terms of triacylglycerol storage, and slightly influenced cell differentiation.
OS-9 up-regulates occludin (show OCLN Proteins) and claudin-1 (show CLDN7 Proteins) by activating the MAP kinase (MAPK (show MAPK1 Proteins)) pathway, and thus protects the epithelial barrier function of Caco-2 monolayer under hypoxia condition.
EDEM2 (show EDEM2 Proteins) and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog (show SHH Proteins)
Unique regions mediate the interaction between OS-9 and GRP94 (show HSP90B1 Proteins).
It delivers mutant neuroserpin (show SERPINI1 Proteins) to ERAD by recognition of glycan side chains and provide the first in vivo proof of involvement of ERAD in degradation of mutant neuroserpin (show SERPINI1 Proteins).
long non-coding RNA ENST00000480739 suppresses tumour cell invasion by regulating OS-9 and HIF-1alpha (show HIF1A Proteins) in pancreatic ductal adenocarcinoma.
Data indicate that the interaction of OS-9 and XTP3-B with CD147(CG) was inhibited by mutations to conserved residues in their lectin domains.
OS-9 plays no direct functional role in HIF degradation since physical interaction of OS-9 with oxygen sensing HIF prolyl hydroxylases cannot occur in vivo due to their different subcellular localization
The OS-9 specifically recognizes Manalpha1,6Manalpha1,6Man residues on the processed C-arm through the continuous double tryptophan (WW) motif.
The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation
Identification of a peptide, resulting from a point mutation in gene OS-9, recognized by cytolytic T lymphocytes on a human melanoma.
This gene encodes a protein that is highly expressed in osteosarcomas. This protein binds to the hypoxia-inducible factor 1 (HIF-1), a key regulator of the hypoxic response and angiogenesis, and promotes the degradation of one of its subunits. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
amplified in osteosarcoma
, osteosarcoma amplified 9, endoplasmic reticulum associated protein
, protein OS-9
, osteosarcoma amplified 9
, amplified in osteosarcoma 9
, endoplasmic reticulum lectin 2
, erlectin 2