Thermo Fisher Scientific VPRBP Polyclonal Antibody

Applications

Western Blot (WB)

• Tested dilution: 1:500–1:2,000

Product Specifications

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.
Also participates in B-cell development through recruitment by RAG1 to ubiquitinate proteins, limiting error-prone repair during V(D)J recombination.

Part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition.
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 regulatory regions of many tumor suppressor genes, down-regulating their transcription and found at high levels in several tumors.

Involved in JNK-mediated apoptosis during cell competition via interaction with LLGL1 and LLGL2.
During HIV-1 infection, recruited by HIV-1 Vpr to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function, causing G2 phase arrest and protecting viral proteins from degradation.
Similarly, during HIV-2 infection, recruited by HIV-2 Vpx to enhance macrophage infection and viral replication in monocyte/macrophage lineage cells.

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For more information, visit www.P65Warnings.ca.gov.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.