Recombinant Human Optineurin (OPTN) Protein (His)

Name: Recombinant Human Optineurin (OPTN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02569P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Optineurin (OPTN) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q96CV9
Target Symbol	OPTN
Synonyms	14.7K interacting protein; Ag9 C5; ALS12; E3 14.7K interacting protein; E3-14.7K-interacting protein; FIP 2; FIP-2; FIP2; Glaucoma 1 open angle E (adult onset); Glaucoma 1 open angle E; GLC1E; HIP 7; HIP-7; HIP7; Huntingtin interacting protein 7; Huntingtin interacting protein HYPL; Huntingtin interacting protein L; Huntingtin yeast partner L; Huntingtin-interacting protein 7; Huntingtin-interacting protein L; HYPL; Injury inducible protein I 55; NEMO related protein; NEMO-related protein; NRP; Optic neuropathy inducing protein; Optic neuropathy-inducing protein; Optineurin; OPTN; OPTN_HUMAN; TFIIIA IntP; TFIIIA-IntP; Transcription factor IIIA interacting protein; Transcription factor IIIA-interacting protein; Tumor necrosis factor alpha inducible cellular protein containing leucine zipper domains
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MSHQPLSCLTEKEDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKNYFEHEELTVSQLLLCLREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSKAELMKKRLQEKCQALERKNSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII
Expression Range	1-577aa
Protein Length	Full Length
Mol. Weight	69.9 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation. In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta. Plays a neuroprotective role in the eye and optic nerve. 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 recruitment 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.; (Microbial infection) May constitute a cellular target for adenovirus E3 14.7 and Bluetongue virus protein NS3 to inhibit innate immune response.
Subcellular Location	Cytoplasm, perinuclear region. Golgi apparatus. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle. Recycling endosome.
Database References	HGNC: 17142 OMIM: 137760 KEGG: hsa:10133 STRING: 9606.ENSP00000263036 UniGene: PMID: 29782529 Results suggest that Optn potentiates LC3-II production and maturation of the phagophore into the autophagosome, by facilitating the recruitment of the Atg12-5-16L1 complex to Wipi2-positive phagophores. PMID: 29133525 Immunohistochemical analyses of motor neurons from OPTN-associated amyotrophic lateral sclerosis patients reveal that linear ubiquitin and activated NF-kappaB are partially co-localized with cytoplasmic inclusions, and that activation of caspases is elevated. PMID: 27552911 This study describes the crystal structures of optineurin/TBK1 complex and the related NAP1/TBK1 complex, uncovering the detailed molecular mechanism governing the optineurin and TBK1 interaction, and revealing a general binding mode between TBK1 and its associated adaptor proteins. PMID: 27620379 Data suggest that OPTN mRNA and protein expression are significantly decreased in fetal membranes and myometrium during spontaneous term labor; there appears to be no effect of preterm labor on OPTN expression in fetal membranes. In cultured myometrial cells, RNA interference of OPTN up-regulates expression of inflammation mediators in response to IL1B (inteleukin-1B). PMID: 27133964 When yeast genetic interaction partners held in common between human OPTN and ANG were validated in mammalian cells and zebrafish, MAP2K5 kinase emerged as a potential drug target for amyotrophic lateral sclerosis therapy PMID: 28596290 A new variant associated with Paget's Disease of Bone in OPTN, reinforcing the relevance of this gene for the development of this bone disease. PMID: 28993189 OPTN colocalizes with LC3 (autophagic vesicle marker) and alpha-synuclein positive puncta in rotenone-treated animals, potentially indicating an important role in autophagy and PD pathogenesis PMID: 27473339 Given the critical roles of TBK1, important regulatory mechanisms are required to regulate its activity. Among these, Optineurin (Optn) was shown to negatively regulate the interferon response, in addition to its important role in membrane trafficking, protein secretion, autophagy and cell division. PMID: 26976762 E50K, M98K, Q398X and E478G mutations in OPTN affect neuronal viability under normal or oxidative stress conditions. PMID: 26956627 We report a five-generation pedigree with a complex pattern of primary open angle glaucoma(POAG) inheritance; familial clustering of POAG in this pedigree is consistent with dominant inheritance of a glaucoma-causing gene, mutations were not detected in genes previously associated with autosomal dominant glaucoma, suggesting the involvement of a novel disease-causing gene in this pedigree. PMID: 27355837 These results suggest that the IRAK1-binding protein OPTN negatively regulates IL-1beta/LPS-induced NF-kappaB activation by preventing polyubiquitination of TRAF6. PMID: 28882891 This study therefore provides novel information regarding the role of Optn during T-cell activation, suggesting the possible importance of Optn during inflammation and/or autoimmune diseases. PMID: 28192730 Frontotemporal dementia -linked mutations in gene OPTN encoding autophagy adaptor proteins , indicate that impaired autophagy might cause Frontotemporal dementia. PMID: 27166223 The present study provides insight into the genetic or haplotype variants of MYOC and OPTN genes contributing to primary glaucoma. Haplotype variants identified in the present study may be regarded as potential contributing factors of primary glaucoma in Korea. PMID: 27485216 the E50K OPTN mutation markedly reduced the levels of miR-9, which led to alterations in REST and reduced expression levels of BDNF in RGC-5 cells. PMID: 27748809 ALS-linked mutations in OPTN and TBK1 can interfere with mitophagy, suggesting that inefficient turnover of damaged mitochondria may represent a key pathophysiological mechanism contributing to neurodegenerative disease. PMID: 27247382 We conclude that OPTN mutations are associated with Amyotrophic lateral sclerosis PMID: 26303227 In combination with phosphorylation of S177 and S513, this posttranslational modification promotes recruitment and retention of OPTN/TBK1 on ubiquitinated, damaged mitochondria PMID: 27035970 Familial linkage studies for primary angle-closure glaucoma have been performed and identified OPTN causative primary angle-closure glaucoma disease PMID: 26497787 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). PMID: 26503823 OPTN 691_692insAG is a founder mutation in Moroccan and Ashkenazi Jews with ALS. PMID: 26740678 A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. PMID: 26302410 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. PMID: 26142952 Optineurin binding to myosin VI was also decreased in tissue lysates from sporadic amyotrophic lateral sclerosis spinal cords. PMID: 25859013 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. PMID: 25855473 Data suggest OPTN is involved in upregulation of innate immunity in mitosis; mechanism involves phosphorylation/mitochondrial translocation of TBK1 (NF-kB-activating kinase) and phosphorylation/nuclear translocation of CYLD (cylindromatosis protein). PMID: 25923723 Loss-of-function variants in OPTN and TBK1 are associated with clinical and pathological frontotemporal dementia without motor neuron disease; TBK1 mutations are common cause of frontotemporal lobar degeneration with TAR DNA-binding protein 43 inclusions PMID: 25943890 that ubiquitin (Ub)-binding domain mutants compromise the maturation of autophagosomes, which in turn interfered with optineurin-mediated autophagy and clearance of inclusion bodies PMID: 25484089 optineurin is recruited to ubiquitinated mitochondria downstream of PARK2, and induces autophagosome assembly around mitochondria PMID: 25801386 ALS-linked mutations in both OPTN and UBQLN2 interfere with the constitution of specific endosomal vesicles, suggesting that the vesicles are involved in protein homeostasis and that these proteins function in common pathological processes. PMID: 25398946 two receptors previously linked to xenophagy, NDP52 and optineurin, are the primary receptors for PINK1- and parkin-mediated mitophagy PMID: 26266977 optineurin appears to play an important role in the maintenance of the podocyte Golgi complex. PMID: 25096716 Loss of optineurin in vivo results in elevated cell death and alters axonal trafficking dynamics PMID: 25329564 optineurin is an autophagy receptor in parkin-mediated mitophagy; defects in a single pathway can lead to neurodegenerative diseases with distinct pathologies PMID: 25294927 According to molecular genetic studies, OPTN causative gene involved in the development of Primary open-angle glaucoma. PMID: 25711070 under-expressed in subgroups of CD patients. The most common of these was optineurin (OPTN) which was under-expressed in approximately 10% of the CD patients. PMID: 24943399 that the loss-of-function, but not the proteinopathy itself, of OPTN leads to multisystem neurodegeneration. PMID: 23889540 HACE1-OPTN axis synergistically suppresses growth and tumorigenicity of lung cancer cells. PMID: 25026213 Three mutations of OPTN were identified in Japanese Amyotrophic lateral sclerosis patients PMID: 24085347 the crystal structure of Rab25 in complex with the C-terminal region of FIP2, which consists of a central dimeric FIP2 coiled-coil that mediates a heterotetrameric Rab25-(FIP2)2-Rab25 complex. PMID: 24056041 NMR and crystal structures of the autophagy modifier LC3B in complex with the LC3 interaction region of optineurin. PMID: 23805866 OPTN in cooperation with TDP-43 might be involved in the pathophysiological mechanisms of skeletal muscular degeneration in myopathy PMID: 22860700 Identification of a functional IRF-1-binding site in the first intron of human optineurin gene that mediates interferon-gamma-induced activation of the promoter, is reported. PMID: 23811275 Knockdown of Rab12 increased transferrin receptor level and reduced M98K-induced cell death. PMID: 23357852 Detection of a novel truncating OPTN mutation associated with an aggressive form of amyotrophic lateral sclerosis (ALS) and confirmation that OPTN mutations are a rare cause of ALS. PMID: 23062601 Progressive aphasia as the presenting symptom in a patient with amyotrophic lateral sclerosis with a novel mutation in the OPTN gene. PMID: 23282279 Optineurin acts as an adaptor to bring together Rab8 and its GTPase-activating protein TBC1D17. PMID: 22854040 The results of this study concluded that OPTN mutations associated with ALS are rare in British ALS patients. PMID: 22892313 This study suggests that mutations in OPTN are not the main cause of ALS in the Japanese population. PMID: 22708870

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.