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The protein encoded by UFD1L forms a complex with two other proteins, nuclear protein localization-4 and valosin-containing protein, and this complex is necessary for the degradation of ubiquitinated proteins. Additionally we are shipping Ubiquitin Fusion Degradation Protein 1 Homolog Antibodies (106) and Ubiquitin Fusion Degradation Protein 1 Homolog Kits (2) and many more products for this protein.
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We demonstrate that WT p97 (show EIF4G2 Proteins) can unfold proteins and that this activity is dependent on the p97 (show EIF4G2 Proteins) adaptor NPLOC4-UFD1L, ATP hydrolysis, and substrate ubiquitination, with branched chains providing maximal stimulation.
The study revealed a regulatory role of the p97 (show EIF4G2 Proteins)-Npl4-Ufd1 complex in regulating a partial degradation of the NF-kappaB (show NFKB1 Proteins) subunit p100 (show CUX1 Proteins).
p97-Ufd1-Npl4 is an integral part of G2/M checkpoint signaling and thereby suppresses chromosome instability.
Data indicate that the p97-UFD1L-NPL4 protein complex specifically associates with ubiquitinated IkappaBalpha via the interactions between p97 and the SCF(beta-TRCP) ubiquitin ligase.
This study demonistrated that UFD1L may participate in the core cognitive deficits observed in schizophrenia.
In coordination with the P97 (show EIF4G2 Proteins)-UFD1-NPL4 complex (P97 (show EIF4G2 Proteins)(UFD1/NPL4)), NUB1L promotes transfer of NEDD8 (show NEDD8 Proteins) to proteasome for degradation.
increased corpus callosum volume in children with 22q11DS is associated with UFD1L polymorphism.
Data indicate that Npl4-Ufd1 heterodimer is required for VCP (show vcp Proteins)-FAF1 (show FAF1 Proteins) interaction.
Data establish Cdc48/p97 (show vcp Proteins)-Ufd1-Npl4 as a crucial negative regulator of Aurora B (show AURKB Proteins) early in mitosis of human somatic cells and suggest that the activity of Aurora B (show AURKB Proteins) on chromosomes needs to be restrained to ensure faithful chromosome segregation.
Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control
The study revealed a regulatory role of the p97 (show EIF4G2 Proteins)-Npl4-Ufd1 complex in regulating a partial degradation of the NF-kappaB (show NFKB1 Proteins) subunit p100 (show PATL2 Proteins).
the p97-Ufd1-Npl4 complex couples ubiquitinated IP(3) receptors to proteasomal degradation and, thus, plays a key role in IP(3) receptor processing
structural analysis of the p97 (show EIF4G2 Proteins)-Npl4-Ufd1 interface
These findings identified a role for CDC-48(UFD-1/NPL-4) in DNA replication, which is important for cell cycle progression and genome stability.
The protein encoded by this gene forms a complex with two other proteins, nuclear protein localization-4 and valosin-containing protein, and this complex is necessary for the degradation of ubiquitinated proteins. In addition, this complex controls the disassembly of the mitotic spindle and the formation of a closed nuclear envelope after mitosis. Mutations in this gene have been associated with Catch 22 syndrome as well as cardiac and craniofacial defects. Alternative splicing results in multiple transcript variants encoding different isoforms. A related pseudogene has been identified on chromosome 18.
UB fusion protein 1
, ubiquitin fusion degradation protein 1 homolog
, ubiquitin fusion degradation 1-like protein
, ubiquitin fusion degradation 1-like
, ubiquitin fusion degradation 1 like (yeast)
, ubiquitin fusion degradation 1 like