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VprBP Polyclonal Antibody, Bethyl Laboratories

Rabbit Polyclonal Antibody

$151.31

Specifications

Antigen VprBP
Applications Western Blot
Classification Polyclonal
Conjugate Unconjugated
Form Liquid
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Products 1
Catalog Number Mfr. No. Quantity Price Quantity & Availability  
Catalog Number Mfr. No. Quantity Price Quantity & Availability  
50-156-1241
Encompass_Preferred
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Bethyl Laboratories, Inc
A301888AT
20 μL
Each of 1 for $151.31
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Description

Description

The recommended shelf life for this product is 1 year from date of receipt. Based on 100% sequence identity, this antibody is predicted to react with Mouse

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 (PubMed:23063525). 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 (PubMed:23362280). 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 (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). 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.
Specifications

Specifications

VprBP
Polyclonal
Liquid
RUO
TBS with 0.1% BSA and 0.09% sodium azide
DCAF1, DDB1 and CUL4 associated factor 1, DDB1- and CUL4-associated factor 1, HIV-1 Vpr-binding protein, KIAA0800, MGC102804, serine/threonine-protein kinase VPRBP, Vpr (HIV-1) binding protein, Vpr-binding protein, VPRBP, vpr-interacting protein
DCAF1
IgG
Antigen affinity chromatography
Antibody
Western Blot
Unconjugated
Rabbit
Human
Q9Y4B6
9730
Between 1457 and 1507
Primary
4° C
DCAF1
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SDS
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