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RNF144B Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q7Z419
Clone Names 110808263
Additional Information
Gene ID 255488
Other Names E3 ubiquitin-protein ligase RNF144B, 632-, IBR domain-containing protein 2, RING finger protein 144B, p53-inducible RING finger protein, RNF144B, IBRDC2, P53RFP
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name RNF144B
Synonyms IBRDC2, P53RFP
Function E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se.
Cellular Location Mitochondrion membrane; Single-pass membrane protein. Cytoplasm Note=Mostly cytosololic, accumulates in submitochondrial domains specifically upon apoptosis induction, in synchrony with BAX activation
Tissue Location Broadly expressed, with lowest levels in brain and thymus, and highest levels detectable in heart, ovary and testis
Research Areas
Citations (0)
citation

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Background

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a TP53/p53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se.

References

Sayan, B.S., et al. Proc. Natl. Acad. Sci. U.S.A. 107(29):12877-12882(2010)Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Benard, G., et al. EMBO J. 29(8):1458-1471(2010)Markson, G., et al. Genome Res. 19(10):1905-1911(2009)van Wijk, S.J., et al. Mol. Syst. Biol. 5, 295 (2009) :

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$ 277.78
Cat# BP18585c
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