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Product Details
A301-887A-T
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human,
Mouse
Host/Isotype
Rabbit
/ IgG
Class
Polyclonal
Type
Antibody
Immunogen
Between 25 and 75
Conjugate
Form
Liquid
Concentration
200 µg/mL
Purification
Antigen affinity chromatography
Storage buffer
TBS, pH 7.0 to 8.0, with 0.1% BSA
Contains
0.09% sodium azide
Storage conditions
4° C
Shipping conditions
Wet ice
Product Specific Information
The recommended shelf life for this product is 1 year from date of receipt.
Target Information
Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex. The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: VPRBP is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition. Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors. Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2. In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT. In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: DDB1- and CUL4-associated factor 1; HIV-1 Vpr-binding protein; MGC102804; protein VPRBP; Serine/threonine-protein kinase VPRBP; Vpr (HIV-1) binding protein; Vpr-binding protein; Vpr-interacting protein; VprBP
Gene Aliases: AI447437; B930007L02Rik; DCAF1; KIAA0800; mKIAA0800; RIP; VPRBP
UniProt ID: (Human) Q9Y4B6, (Mouse) Q80TR8
Entrez Gene ID: (Human) 9730, (Mouse) 321006
negative regulation of transcription from RNA polymerase II promoter
transcription, DNA-templated
viral process
protein ubiquitination
B cell differentiation
V(D)J recombination
cell competition in a multicellular organism
histone H2A-T120 phosphorylation
regulation of transcription, DNA-templated
phosphorylation
chromatin modification
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