DTX3L Protein, Human

DTX3L protein is an E3 ubiquitin protein ligase that cooperates with PARP9 in DNA damage repair and antiviral responses. It monoubiquitylates histones (H2A, H2B, H3, H4), especially “Lys-91” of H4, possibly signaling additional modifications. DTX3L Protein, Human is the recombinant human-derived DTX3L protein, expressed by E. coli , with tag free. The total length of DTX3L Protein, Human is 739 a.a., .

DTX3L Protein, an E3 ubiquitin-protein ligase, collaborates with ADP-ribosyltransferase PARP9 to fulfill key roles in DNA damage repair and interferon-mediated antiviral responses. It monoubiquitinates various histones, including H2A, H2B, H3, and H4, particularly at 'Lys-91' of histone H4 in response to DNA damage. The exact function of H4K91ub1 remains unclear but may serve as a licensing signal for additional histone H4 post-translational modifications. The PARP1-dependent PARP9-DTX3L-mediated ubiquitination facilitates the specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Additionally, DTX3L positively regulates STAT1-dependent interferon-stimulated gene transcription by monoubiquitinating histone H2B, promoting chromatin remodeling. Independently of its catalytic activity, DTX3L plays a crucial role in the sorting of CXCR4 from early endosomes to lysosomes, reducing E3 ligase ITCH activity and facilitating the ubiquitination of endosomal sorting complex required for transport (ESCRT-0) components HGS and STAM. Furthermore, in association with PARP9, DTX3L contributes to antiviral responses by mediating 'Lys-48'-linked ubiquitination of encephalomyocarditis virus (EMCV) and human rhinovirus (HRV) C3 proteases, leading to their proteasomal-mediated degradation. These diverse functions underscore the significance of DTX3L in regulating critical cellular processes.

Human

E. coli

Tag Free

Q8TDB6 (A2-E740)

/

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.