UBE2G1 Protein

Ubiquitin-conjugating enzyme E2G 1 Protein Datasheet

UBE2G1 Protein Product Information

• Synonym: E217K, UBC7, UBE2G
• Protein Construction: A DNA sequence encoding the human UBE2G1 (P62253) (Met 1-Glu 170) was expressed and purified, with additional two amino acids (Gly & Pro) at the N-terminus.
• Source: Human
• Expression Host: E.coli

UBE2G1 Protein QC Testing

• Purity: > 85 % 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: Gly
• Molecular Mass: The recombinant human UBE2G1 consists of 172 amino acids and has a calculated molecular mass of 19.5 KDa as estimated in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from 0.2μm filtered solution of PBS, 10%glycerol, pH7.5
  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: UBE2G1 protein

UBE2G1 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.

UBE2G1 Protein Description

UBE2G1 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.

References

1. Sjoerd J L van Wijk. et al., 2009, Mol Syst Biol. 5: 317.
2. Nandi D. et al., 2006, Journal of biosciences. 31 (1): 137-55.