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>   Home   >   Products   >   Primary Antibodies   >   [KO] OTUB1 Mouse mAb   

[KO] OTUB1 Mouse mAb

 
Catalog #
ABZ1157
Application
WB, IHC-P
Uniprot Id
Q96FW1
Reactivity
Rat
Isotype
IgG1
 
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 Catalog #AvailabilitySizeQuantityUnit Price Save For Later Wish List
ABZ1157-100 2 weeks 100 µL $499.00
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ABZ1157-20 2 weeks 20 µL $149.00
ABZ1157-50 2 weeks 50 µL $325.00
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Product Overview

Name[KO] OTUB1 Mouse mAb
Accession (Primary)Q96FW1
Host SpeciesMouse
IsotypeIgG1
Immunogen
Full length human recombinant protein of human OTUB1 produced in 293T cell.
Species Reactivity
Reacts WithRat
Calculated MW
Calculated MW: 31 kDa; Observed MW: 36 kDa
Buffer System
Liquid in PBS containing 50% glycerol, 1% BSA and 0.02% sodium azide, pH 7.3.
Storage
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Recommended Dilution
WB: 1/500-1/1000; IHC: 1/50-1/100
Clonality No.
1E3
Purification
Affinity Purified
Conjugation
Unconjugated
Modification
Unmodified
Form
Liquid
Background
Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain.MiscellaneousIn the structure described by PubMed:18954305, the His-265 active site of the catalytic triad is located too far to interact directly with the active site Cys-91. A possible explanation is that OTUB1 is in inactive conformation in absence of ubiquitin and a conformation change may move His-265 in the proximity of Cys-91 in presence of ubiquitin substrate.
Research Field
Epigenetics and Nuclear Signaling

Target Information: ( Q96FW1 )

NameOTUB1
Other Names
OTUB1; OTB1; OTU1; HSPC263; Ubiquitin thioesterase OTUB1; Deubiquitinating enzyme OTUB1; OTU domain-containing ubiquitin aldehyde-binding protein 1; Otubain-1; hOTU1; Ubiquitin-specific-processing protease OTUB1
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