基因名称(Gene Name)
DTX3L BBAP
蛋白名称
E3 ubiquitin-protein ligase DTX3L (B-lymphoma- and BAL-associated protein) (Protein deltex-3-like) (Rhysin-2) (Rhysin2)
免疫原
Synthesized peptide derived from human DTX3L
特异性
This antibody detects endogenous levels of DTX3L at Human, Mouse
组成
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
来源
Polyclonal, Rabbit,IgG
纯化工艺
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
储存
-15°C to -25°C/1 year(Do not lower than -25°C)
功能
E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses . Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4 . In response to DNA damage, mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1) . The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me) . PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites . By monoubiquitinating histone H2B H2BC9/H2BJ and thereby promoting chromatin remodeling, positively regulates STAT1-dependent interferon-stimulated gene transcription and thus STAT1-mediated control of viral replication . Independently of its catalytic activity, promotes the sorting of chemokine receptor CXCR4 from early endosome to lysosome following CXCL12 stimulation by reducing E3 ligase ITCH activity and thus ITCH-mediated ubiquitination of endosomal sorting complex required for transport ESCRT-0 components HGS and STAM . In addition, required for the recruitment of HGS and STAM to early endosomes . In association with PARP9, plays a role in antiviral responses by mediating 'Lys-48'-linked ubiquitination of encephalomyocarditis virus (EMCV) and human rhinovirus (HRV) C3 proteases and thus promoting their proteosomal-mediated degradation .
