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Component of the Cul4a-Rbx1-Ddb1-Vprbp/Dcaf1 E3 ubiquitin-protein ligase complex, Vprbp/Dcaf1 may function as the substrate recognition module within this complex (By similarity). Additionally we are shipping and many more products for this protein.
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Human Polyclonal VPRBP Primary Antibody for IP, WB - ABIN438378
Salsman, Jagannathan, Paladino, Chan, Dellaire, Raught, Frappier: Proteomic profiling of the human cytomegalovirus UL35 gene products reveals a role for UL35 in the DNA repair response. in Journal of virology 2011
Show all 2 Pubmed References
Human Polyclonal VPRBP Primary Antibody for IP, WB - ABIN438377
Huang, Chiang, Lin, Chiou, Chow: HIV-1 Vpr triggers mitochondrial destruction by impairing Mfn2-mediated ER-mitochondria interaction. in PLoS ONE 2012
The study suggests that DCAF1 is involved in hepatitis C virus (HCV) replication through regulation of miR (show MLXIP Antibodies)-122, and thus provides new insights into the interaction between HCV and the host cell.
RNA interference-mediated knockdown of differentially regulated host factors identified Vpr binding protein (VprBP) as proviral host factor because its downregulation inhibited efficient propagation of seasonal influenza A virus.
High VPRBP expression is associated with high-grade serous ovarian cancer.
Data show that neurofibromin 2 (Merlin (show NF2 Antibodies)) suppresses proliferation and adhesion, at least partly, through inhibiting kinase suppressor of Ras 1 (KSR1 (show KSR1 Antibodies)) and DCAF1 protein.
Together, these results characterize a novel postintegration restriction of HIV-1 replication in monocyte-derived dendritic cells and show that the interaction of Vpr with the DCAF1/DDB1 E3 ubiquitin ligase (show MUL1 Antibodies) complex and the yet-to-be-identified host factor might alleviate this restriction by inducing transcription from the viral long terminal repeat.
This study presents the crystal structure of the DDB1-DCAF1-HIV-1-Vpr-uracil-DNA glycosylase (show UNG Antibodies) (cyclin U (show CCNO Antibodies)) complex.
VprBP transcription was repressed by cellular miRNA-1236, which contributes to HIV-1 restriction in monocytes. miR (show MLXIP Antibodies)-1236 inhibitors enhanced translation of VprBP and promoted infection. miR (show MLXIP Antibodies)-1236 mimetics suppressed translation of VprBP.
MCM10 (show MCM10 Antibodies) is the natural substrate of the Cul4-DDB1[VprBP] E3 ubiquitin ligase (show MUL1 Antibodies) whose degradation is regulated by VprBP, but Vpr enhances the proteasomal degradation of MCM10 (show MCM10 Antibodies) by interacting with VprBP.
Vpr downregulated APOBEC3G (show APOBEC3G Antibodies) through Vpr-binding protein (VprBP)-mediated proteasomal degradation, and further confirmed that the reduction of APOBEC3G (show APOBEC3G Antibodies) encapsidation associated with Vpr was due to Vpr's degradation-inducing activity.
Vpr and Vpx share a highly similar DCAF1-binding motif, they interact with a different set of residues in DCAF1.
DCAF1 is required for T-cell expansion and function during anti-viral and autoimmune responses.
VprBP Is Required for Efficient Editing and Selection of Igkappa+ B Cells, but Is Dispensable for Iglambda+ and Marginal Zone B Cell Maturation (show TNFRSF17 Antibodies) and Selection
CRL4(VPRBP) ubiquitin ligase is a guardian of female reproductive life in germ cells and a maternal reprogramming factor after fertilization.
multi-subunit cullin RING E3 ligase complex VprBP/DDB1/Cul4A (show CUL4A Antibodies)/Roc1 (show RIT1 Antibodies) associates with full-length RAG1 (show RAG1 Antibodies) through VprBP
Data show that human immunodeficiency virus type 1 Vpr-binding protein VprBP binds stoichiometrically with DDB1 through its WD40 domain (show DCAF12L2 Antibodies) and through DDB1 to CUL4A (show CUL4A Antibodies), subunits of the COP9 (show COPS8 Antibodies)/signalsome.
Component of the Cul4a-Rbx1-Ddb1-Vprbp/Dcaf1 E3 ubiquitin-protein ligase complex, Vprbp/Dcaf1 may function as the substrate recognition module within this complex (By similarity). Associated with chromatin in a Ddb1-independent and cell cycle- dependent manner, Vprbp/Dcaf1 is recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis (By similarity).
, Vpr (HIV-1) binding protein
, Vpr-binding protein
, HIV-1 Vpr binding protein-like
, HIV-1 Vpr binding protein
, protein VPRBP-like
, DDB1 and CUL4 associated factor 1
, DDB1- and CUL4-associated factor 1
, HIV-1 Vpr-binding protein
, vpr-interacting protein