Abcam, ab268635, Recombinant human HERC4 protein (Active)

Size: 20µg
Recombinant human HERC4 protein (Active) is a Human Fragment protein, expressed in Baculovirus infected Sf9 cells, with >80%, suitable for SDS-PAGE, FuncS.
Key facts
Purity:>80% SDS-PAGE,
Expression system:Baculovirus infected Sf9 cells,
Tags:GST tag N-Terminus,
Applications:SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:The specific activity of ab268635 was determined to be 6 nmol/min/mg in ubiquitination assay using wild-type ubiquitin substrate.,
Accession:Q5GLZ8,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.5Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
HERC4 also known as HECT and RLD domain-containing E3 ubiquitin protein ligase 4 is a protein that mechanically functions as an E3 ubiquitin ligase. Weighing approximately 120 kDa HERC4 facilitates the transfer of ubiquitin from E2 ubiquitin-conjugating enzymes to substrate proteins tagging them for degradation by the proteasome. The protein is expressed in various tissues including the brain heart and lung indicating its broad functional significance across different biological systems.
Biological function summary
HERC4 plays an important role in regulating protein turnover and cellular processes. As part of the ubiquitin-proteasome system it ensures protein quality control and homeostasis by targeting misfolded or damaged proteins. While HERC4 does not traditionally form complexes its activity influences the stability and function of other proteins within the cell. This implicates HERC4 in not only cellular maintenance but also processes such as cell cycle regulation and signal transduction.
Pathways
The ubiquitin-proteasome pathway involves HERC4 contributing to the degradation of regulatory proteins that control various cellular activities. The protein interacts with pathways like cell cycle progression and stress response. It maintains a functional relationship with proteins such as p53 a known tumor suppressor and other E3 ligases that manage the proteolytic balance in the cell demonstrating its integration into critical regulatory networks.
HERC4 has connections to cancer and neurodegenerative diseases. In cancer aberrant ubiquitination activities involving HERC4 can disrupt normal protein regulation leading to uncontrolled cell growth. It may interact with oncogenic proteins that escape degradation promoting tumor progression. In neurodegenerative disorders such as Parkinson's disease dysregulation of the ubiquitin-proteasome system potentially involving HERC4 connects with proteins like Parkin impacting neuronal survival and function. Understanding HERC4's role in these pathways provides insights into potential therapeutic targets for these conditions.