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OPTN encodes the coiled-coil containing protein optineurin. Additionally we are shipping Optineurin Kits (10) and Optineurin Proteins (7) and many more products for this protein.
Showing 10 out of 90 products:
Cow (Bovine) Polyclonal OPTN Primary Antibody for WB - ABIN2779546
Morton, Hesson, Peggie, Cohen: Enhanced binding of TBK1 by an optineurin mutant that causes a familial form of primary open angle glaucoma. in FEBS letters 2008
ALS (show IGFALS Antibodies)-linked mutations in OPTN and TBK1 (show TBK1 Antibodies) can interfere with mitophagy, suggesting that inefficient turnover of damaged mitochondria may represent a key pathophysiological mechanism contributing to neurodegenerative disease.
We conclude that OPTN mutations are associated with Amyotrophic lateral sclerosis
In combination with phosphorylation of S177 and S513, this posttranslational modification promotes recruitment and retention of OPTN/TBK1 (show TBK1 Antibodies) on ubiquitinated, damaged mitochondria
Familial linkage studies for primary angle-closure glaucoma have been performed and identified OPTN causative primary angle-closure glaucoma disease
Nine OPTN variants were identified in Chinese sporadic ALS patients, including 5 known SNPs and four novel missense mutations: c.407C > T (p.A136V), c.1184A > G (p.K395R), c.1352T > C (p.I451T), and c.1546G > C (p.E516Q) (all heterozygous).
OPTN 691_692insAG is a founder mutation in Moroccan and Ashkenazi Jews with ALS.
A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells.
Optineurin can also mediate the removal of protein aggregates through an ubiquitin-independent mechanism. This protein in addition can induce autophagy upon overexpression or mutation.
Optineurin binding to myosin VI was al (show MYO6 Antibodies)so decreased in tissue lysates from sporadic amyotrophic lateral sclerosis spinal cords.
Optineurin mediates its functions by interacting with various proteins and disease-causing mutations alter these interactions leading to functional defects in membrane vesicle trafficking, autophagy, signaling.
OPTN-deficient mice were more susceptible to infection with Salmonella, confirming in vivo the importance of OPTN in bacterial clearance.
Optineurin knockdown enhances osteoclast differentiation. Optineurin inhibits osteoclast formation by modulating NF-kappaB (show NFKB1 Antibodies) and IFN-beta (show IFNB1 Antibodies) signaling.
Mutation in Optineurin gene is associated with Glaucoma.
Disruption in optineurin and myosin VI (show MYO6 Antibodies)-mediated cellular trafficking is associated with amyotrophic lateral sclerosis.
OPTN plays a role in acute inflammation and neutrophil recruitment, potentially via defective macrophage proinflammatory cytokine secretion.
that ubiquitin (Ub)-binding domain mutants compromise the maturation of autophagosomes, which in turn interfered with optineurin-mediated autophagy and clearance of inclusion bodies
results indicated that optineurin trimers may be the basic unit of these oligomers. The oligomeric state can be affected by many factors that induce covalent bonds, such as H2O2 or E50K
Loss of optineurin in vivo results in elevated cell death and alters axonal trafficking dynamics
HACE1 (show HACE1 Antibodies)-OPTN axis synergistically suppresses growth and tumorigenicity of lung cancer cells.
Mutants in which the entire Ub-binding C-terminal region is deleted showed that optineurin is dispensable for NF-kappaB (show NFKB1 Antibodies) activation but necessary for optimal IRF3 (show IRF3 Antibodies) activation in immune cells.
The optineurin gene and protein are evolutionary conserved between humans and the rhesus monkey. High similarity of ocular expression and tissue distribution between the two optineurin proteins.
This gene encodes the coiled-coil containing protein optineurin. Optineurin may play a role in normal-tension glaucoma and adult-onset primary open angle glaucoma. Optineurin interacts with adenovirus E3-14.7K protein and may utilize tumor necrosis factor-alpha or Fas-ligand pathways to mediate apoptosis, inflammation or vasoconstriction. Optineurin may also function in cellular morphogenesis and membrane trafficking, vesicle trafficking, and transcription activation through its interactions with the RAB8, huntingtin, and transcription factor IIIA proteins. Alternative splicing results in multiple transcript variants encoding the same protein.
, E3-14.7K-interacting protein
, Huntingtin interacting protein L
, huntingtin yeast partner L
, huntingtin-interacting protein 7
, huntingtin-interacting protein L
, nemo-related protein
, optic neuropathy-inducing protein
, transcription factor IIIA-interacting protein
, transcrption factor IIIA-interacting protein
, tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains
, 14.7K-interacting protein 2
, FIP-2-like protein