flow cytometry: 1-3 μg/test using HeLa cells immunoblotting: 2-4 μg/mL using whole extracts of HEK-293 cells. immunofluorescence: 0.25-0.5 μg/mL using HeLa cells.
RNF4 (ring finger protein 4), initially identified as a transcriptional cofactor, is an E3 ubiquitin ligase. As this protein contains both the SUMO-interacting motif (SIM) and RING finger domains, it links sumoylation to ubiquitination.
Immunogen
synthetic peptide corresponding to a sequence at the C terminal region of human RNF4
Biochem/physiol Actions
RNF4 (ring finger protein 4) plays a wide variety of physiological roles, such as targeting of proteins for degradation, including promyelocytic leukemia protein (PML), CENP-I (centromere protein I), hypoxia-inducible factor (HIF), PARP-1 (poly [ADP-ribose] polymerase 1) etc. It also induces the base excision repair machinery, thus controlling DNA methylation. It is involved in DNA demethylation therefore, promoting gene transcription. RNF4 acts upon the oncogenic protein, Tax, of human T-cell leukemia virus type 1 (HTLV-1), and it regulates its nucleo-cytoplasmic localization. Arsenic trioxide (ATO) facilitates the sumoylation of promyelocytic leukemia (PML) bodies, thus, increasing their RNF4-mediated SUMO-dependent ubiquitylation and degradation. RNF4 functions as a co-regulator of androgen receptor-dependent transcription and is expressed in mice testis. Therefore, it might be involved in spermatid maturation.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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We have recently reported that poly-SUMO-2/3 conjugates are subject to a ubiquitin-dependent proteolytic control in human cells. Here we show that arsenic trioxide (ATO) increases SUMO-2/3 modification of promyelocytic leukemia (PML) leading to its subsequent ubiquitylation in vivo. The SUMO-binding
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