Recombinant Human HERC5 protein - BSA and Azide free (His tag N-Terminus)
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Recombinant Human HERC5 protein - BSA and Azide free (His tag N-Terminus) is a Human Fragment protein, in the 681 to 1024 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
CEB1, CEBP1, HERC5, E3 ISG15--protein ligase HERC5, Cyclin-E-binding protein 1, HECT domain and RCC1-like domain-containing protein 5
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human HERC5 protein - BSA and Azide free (His tag N-Terminus) (AB180352)
15% SDS-PAGE analysis of ab180352 (3 μg)
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The HERC5 protein contributes to innate immune response by modifying proteins involved in antiviral defense. It adds ISG15 to newly synthesized proteins marking them for rapid degradation or altering their activities. HERC5 operates as a solitary protein rather than forming part of a larger complex. Through its ISGylation activity HERC5 plays a significant role in enhancing the antiviral state of cells inhibiting viral replication and modulating cellular processes during stress responses.
Pathways
HERC5 actively integrates into the antiviral defense mechanism and ubiquitin-proteasome pathway. It associates with pathways related to protein modification and immune signaling significantly affecting how cells respond to viral infections. Proteins like ISG15 and ubiquitin-conjugating enzymes interact with HERC5 in these pathways highlighting its importance in maintaining cellular homeostasis and protecting against pathogens.
Specifications
Form
Liquid
General info
Function
Major E3 ligase for ISG15 conjugation (PubMed : 26355087, PubMed : 27534820, PubMed : 27564865, PubMed : 34572049, PubMed : 37279284). 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. Mediates ISGylation of the phosphatase PTEN leading to its degradation, thus alleviating its suppression of the PI3K-AKT signaling pathway and promoting the production of cytokines that facilitate bacterial clearance (PubMed : 37279284). Interferes with the function of key viral structural proteins such as ebolavirus structural protein VP40 or HIV-1 protein GAG (PubMed : 22093708, PubMed : 34572049). 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. Promotes parkin/PRKN ubiquitin E3 ligase activity by suppressing the intramolecular interaction that maintains its autoinhibited conformation (PubMed : 27534820).. (Microbial infection) Functions as an E3 ligase for ISGylation of hepatitis B virus protein X leading to enhanced viral replication due to increased interferon resistance.
Post-translational modifications
ISGylated.
Target data
Complementary Products
Product promise
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