E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates ''Lys-6''-, ''Lys-11''-, ''Lys-48''- and ''Lys-63''-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation (PubMed:18408734, PubMed:19307308, PubMed:35013556). Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (PubMed:18408734, PubMed:19307308, PubMed:20943951). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (PubMed:20212317). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (PubMed:19779455, PubMed:20026589). Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation (PubMed:12885770). Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (PubMed:35013556).

E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (Small nuclear ring finger protein) (Protein SNURF)
RNF4 SNURF RES4-26 RES4-26; SLX5; SNURF

P78317

Human, Rat, Mouse

WB

WB 1:500-2000

Mouse

Human recombinant protein fragment corresponding to amino acids 1-190 of human RNF4 (NP_002929) produced in E.coli.

Monoclonal

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at -20 °C. Stable for 12 months from date of receipt.