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Data show that ubiquitin E2 enzymes UBE2D1 (show UBE2D1 Antibodies)/2/3 and E3 ligase RNF138 (show RNF138 Antibodies) accumulate at DNA-damage sites and act at early resection stages by promoting CtIP (show RBBP8 Antibodies) protein ubiquitylation and accrual.
These data reveal novel insights into the Otub1 (show OTUB1 Antibodies) inhibition of E2 wherein monoubiquitination promotes the interaction of Otub1 (show OTUB1 Antibodies) with UbcH5 (show UBE2D1 Antibodies) and the function to suppress it.
UbcH5c~Ubiqitin binding stabilizes an active conformation of the Shigella flexneri OspG kinase, greatly enhancing its activity.
UBE2D3 participates in the process of radiosensitivity in human breast cancer cells by regulating TERT (show TERT Antibodies) and cyclin D1 (show CCND1 Antibodies).
although a reduction in interdomain dynamics of UbcH5c~Ub is observed upon binding to E4B, Ub retains an extensive degree of flexibility
The crystal structure of a complex of the Bmi1 (show BMI1 Antibodies)/Ring1b (show RNF2 Antibodies) RING-RING heterodimer & UbcH5c shows that UbcH5c interacts with Ring1b (show RNF2 Antibodies) only.
UbcH5c approximately Ub conjugate populates an array of extended conformations, and the population of Ubc13 (show UBE2N Antibodies) approximately Ub conjugates favors a closed conformation in which the hydrophobic surface of Ub faces helix 2 of Ubc13 (show UBE2N Antibodies)
determined structures of E4B U box free and bound to UbcH5c and Ubc4 (show UBE2D2 Antibodies) E2s; findings show E4B U box is a monomer stabilized by a network of hydrogen bonds; findings suggest allosteric regulation of UbcH5c and Ubc4 (show UBE2D2 Antibodies) by E4B U box
Combined Actions of UbcH5c and Cdc34 (show CDC34 Antibodies) Promote Rapid and Efficient Polyubiquitination of IkBa (show NFKBIA Antibodies)
role of WW3 and WW4 domains of Nedd4-2 in dopamine transporter ubiquitination was demonstrated; siRNA analysis demonstrated that this polyubiquitination is mediated by Nedd4-2 cooperation with UBE2D and UBE2L3 E2 ubiquitin-conjugating enzymes
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Multiple spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been determined.
ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog, yeast)
, ubiquitin-conjugating enzyme E2D 3
, ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog)
, E2(17)KB 3
, ubiquitin carrier protein D3
, ubiquitin-conjugating enzyme E2 D3
, ubiquitin-conjugating enzyme E2(17)KB 3
, ubiquitin-conjugating enzyme E2-17 kDa 3
, ubiquitin-conjugating enzyme E2D 3 (homologous to yeast UBC4/5)
, ubiquitin-protein ligase D3
, ubiquitin-conjugating enzyme E2D 2
, ubiquitin carrier protein 4
, ubiquitin carrier protein D2
, ubiquitin conjugating enzyme E2
, ubiquitin-conjugating enzyme E2 D2
, ubiquitin-protein ligase D2
, phosphoarginine phosphatase