UBE2D4 Protein (His Tag)

Ubiquitin-conjugating enzyme E2D 4 (putative) Protein Datasheet

UBE2D4 Protein Product Information

• Synonym: HBUCE1
• Protein Construction: A DNA sequence encoding the human UBE2D4 (Q9Y2X8) (Met 1-Met 1474) was expressed, with a polyhistide tag at the N-terminus.
• Source: Human
• Expression Host: E.coli

UBE2D4 Protein QC Testing

• Purity: > 95% as determined by SDS-PAGE.
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met
• Molecular Mass: The recombinant human UBE2D4 consisting of 162 amino acids and migrates as an approximately 18.5 kDa band in SDS-PAGE under reducing conditions as predicted.
• Formulation: Lyophilized from sterile 20mM Tris, 0.1M NaCl, 10%glycerol, 2mM DTT, pH8.0
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: UBE2D4 protein

UBE2D4 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

UBE2D4 Protein Description

UBE2D4 is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by an ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans. It has been identified the UBE2D family (UBE2D1–4) as E2 partners for IDOL that support both autoubiquitination and IDOL-dependent ubiquitination of the LDLR in a cell-free system.

References

1. Sjoerd J L van Wijk. et al., 2009, Mol Syst Biol. 5: 317.
2. Zhang L. et al., 2011, Genes Dev. 25 (12): 1262-74.
3. Nandi D. et al., 2006, Journal of biosciences. 31 (1): 137-55.