Product nameRecombinant Human RBCK1 protein
See all RBCK1 proteins and peptides
Protein lengthProtein fragment
Amino Acid Sequence
Amino acids3 to 99
Tagsproprietary tag N-Terminus
Our Abpromise guarantee covers the use of ab161073 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesProtein concentration is above or equal to 0.05 mg/ml.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.31% Glutathione, 0.79% Tris HCl
- Chromosome 20 open reading frame 18
- HBV associated factor 4
FunctionActs as an E3 ubiquitin-protein ligase, or as part of an E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteoasome. Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates. LUBAC conjugates linear polyubiquitin to IKBKG at 'Lys-285' and 'Lys-309' and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Binds polyubiquitin of different linkage types.
Sequence similaritiesContains 1 B box-type zinc finger.
Contains 1 RanBP2-type zinc finger.
Contains 1 RING-type zinc finger.
Contains 1 ubiquitin-like domain.
modificationsAuto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome.
Phosphorylated. In vitro, phosphorylation inhibits auto-ubiquitination activity.
- Information by UniProt
ab161073 has not yet been referenced specifically in any publications.