Abcam, ab167962, Recombinant Human UBC3B protein

Size: 20µg / 50µg
Recombinant Human UBC3B protein is a Human Full Length protein, in the 2 to 238 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:WB, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q712K3,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7Preservative: 1.02% ImidazoleConstituents: 25% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 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.
UBC3B also known as UBE2E2 is a ubiquitin-conjugating enzyme with a molecular mass of approximately 25 kDa. This enzyme plays a pivotal role mechanically in the ubiquitination process where it facilitates the transfer of ubiquitin from a ubiquitin-activating enzyme to substrate proteins. UBC3B is expressed in various tissues including the brain and the reproductive system indicating its broad functional importance in different biological contexts.
Biological function summary
The enzyme takes part in protein degradation processes and regulates the stability of numerous proteins by tagging them for degradation by the proteasome. UBC3B functions as part of multi-protein ubiquitin pathways and interacts with E3 ubiquitin ligases to identify specific proteins for tagging. Its activity helps maintain cellular protein homeostasis and impacts processes like cell cycle regulation and DNA repair.
Pathways
UBC3B is involved in ubiquitin-dependent proteolysis and is critical in the cellular stress response pathways. It collaborates closely with proteins like the E3 ligase HECTD1 within these pathways. This relationship helps regulate protein turnover and the cell's response to stress ensuring damaged or misfolded proteins are efficiently degraded to prevent cellular dysfunction.
Mutations or dysregulation of UBC3B are associated with cancer and neurodegenerative diseases. In cancer the altered ubiquitin pathways can lead to uncontrolled cell proliferation due to disrupted protein degradation. UBC3B interacts with proteins like p53 a tumor suppressor linking it to oncogenic processes. In neurodegenerative diseases the accumulation of ubiquitinated proteins due to erroneous UBC3B activity can cause neuronal cell damage.