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OTU domain, ubiquitin aldehyde binding 1

Cat:P06199

Summary:

【Derived From】: E.coli
【Endotoxin】: Not measured
【Amino Acid】: 1-272aa
【Purity】: ≥85% by SDS-PAGE.
【Name】: OTUB1
【Full Name】: OTU domain,ubiquitin aldehyde binding 1
【Uniprot】: Q96FW1
【Gene ID】: 55611
【Species Reactivity】: Human Mouse Rat
【Mol Mass】: 29.92kDa
【Application】: Immunology research
【Purification】: NI-NTA affinity purification
【Bioactive】: N0
【Tag】: With a 6×His tag at the N/C-terminus.
【Concentration】: 1mg/ml by SDS-PAGE.

Store:

【Reconstitution】: Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.)
【Storage】: Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks, stored at < -20℃ for 1 year.
【Formulation】: Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0.

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

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