Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by interferon. Functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner. Catalyzes ISGylation of IRF3 which results in sustained activation, it attenuates IRF3-PIN1 interaction, which antagonizes IRF3 ubiquitination and degradation, and boosts the antiviral response. Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets. Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant-negative effect on virus infectivity. Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner. In an interferon-stimulated cell, newly translated viral proteins are primary targets of ISG15.
Primary Antibodies
polyclonal
human
hect domain and RLD 5
Rabbit
IgG
Unconjugated
liquid
ELISA, WB
128 kDa
≥95% as determined by SDS-PAGE
Immunogen affinity purified
WB: 1:500-1:2000
100µg
PBS with 0.02% sodium azide and 50% glycerol pH 7.3,-20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
HERC5
CEB1, CEBP1
This product is for research use only.
Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by int...
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Ver másHECT And RLD Domain Containing E3 Ubiquitin Protein Ligase 5 is a recombinant enzyme.
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