|Application ||WB, E|
|Other Accession||Q8R5M4, NP_068815.2|
|Calculated MW||65921 Da|
|Antigen Region||71-96 aa|
|Other Names||Optineurin, E3-147K-interacting protein, FIP-2, Huntingtin yeast partner L, Huntingtin-interacting protein 7, HIP-7, Huntingtin-interacting protein L, NEMO-related protein, Optic neuropathy-inducing protein, Transcription factor IIIA-interacting protein, TFIIIA-IntP, OPTN, FIP2, GLC1E, HIP7, HYPL, NRP|
|Target/Specificity||This OPTN antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 71-96 amino acids from the Central region of human OPTN.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||OPTN Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||FIP2, GLC1E, HIP7, HYPL, NRP|
|Function||Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. May constitute a cellular target for adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby affecting cell death.|
|Cellular Location||Cytoplasm, perinuclear region. Golgi apparatus. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle. Recycling endosome Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy|
|Tissue Location||Present in aqueous humor of the eye (at protein level). Highly expressed in trabecular meshwork. Expressed nonpigmented ciliary epithelium, retina, brain, adrenal cortex, fetus, lymphocyte, fibroblast, skeletal muscle, heart, liver, brain and placenta.|
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Provided below are standard protocols that you may find useful for product applications.
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.
McDonald, K.K., et al. J. Hum. Genet. 55(10):697-700(2010)
Cheng, J.W., et al. Med. Sci. Monit. 16 (8), CR369-CR377 (2010) :
Albagha, O.M., et al. Nat. Genet. 42(6):520-524(2010)
Maruyama, H., et al. Nature 465(7295):223-226(2010)
Park, B., et al. PLoS ONE 5 (7), E11547 (2010) :
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