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Rabbit Anti-DCAF1 Recombinant Antibody (EPR16012) (CBMAB-V0137-LY)

This product is antibody recognizes DCAF1. The antibody EPR16012 immunoassay techniques such as: WB, IHC-P, FC, ICC/IF.
See all DCAF1 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
EPR16012
Antibody Isotype
IgG
Application
WB, IHC-P, FC, ICC/IF

Basic Information

Immunogen
Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human VPRBP aa 1450 to the C-terminus
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
DDB1 And CUL4 Associated Factor 1
Introduction
DCAF1 (DDB1 And CUL4 Associated Factor 1) is a Protein Coding gene. Diseases associated with DCAF1 include Aicardi-Goutieres Syndrome. Among its related pathways are Innate Immune System and Class I MHC mediated antigen processing and presentation.
Entrez Gene ID
Human9730
Mouse321006
Rat315987
UniProt ID
Alternative Names
DDB1 And CUL4 Associated Factor 1; Serine/Threonine-Protein Kinase VPRBP; Vpr (HIV-1) Binding Protein; HIV-1 Vpr-Binding Protein; Vpr-Interacting Protein; VPRBP; RIP;
Function
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: DCAF1 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).

(Microbial infection) 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.

(Microbial infection) 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.
Biological Process
B cell differentiation Source: UniProtKB
Cell competition in a multicellular organism Source: UniProtKB
Histone H2A-T120 phosphorylation Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Protein ubiquitination Source: UniProtKB-UniPathway
V(D)J recombination Source: UniProtKB
Viral process Source: UniProtKB-KW
Cellular Location
Cytoplasm; Nucleus. Associated with chromatin in a DDB1-independent and cell cycle-dependent manner: recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis.

Chen, J., Liang, J. Q., Zhen, Y. F., Chang, L., Zhou, Z. T., & Shen, X. J. (2021). DCAF1-targeting microRNA-3175 activates Nrf2 signaling and inhibits dexamethasone-induced oxidative injury in human osteoblasts. Cell Death & Disease, 12(11), 1-11.

Zong, Y., Shan, H., Yin, F., Ma, X., Jiang, C., Wang, N., ... & Yu, X. (2021). Ddb1-Cullin4-Associated-Factor 1 in Macrophages Restricts the Staphylococcus aureus-Induced Osteomyelitis. Journal of Inflammation Research, 14, 1667.

Guo, Z., & Yisong, W. A. N. (2021). The role of DCAF1-GSTP1-ROS axis in regulating T cell senescence in immunological ageing and tumors.

Guo, Z., Wang, G., Wu, B., Chou, W. C., Cheng, L., Zhou, C., ... & Wan, Y. Y. (2020). DCAF1 regulates Treg senescence via the ROS axis during immunological aging. The Journal of clinical investigation, 130(11), 5893-5908.

Chen, Y., Evankovich, J. W., Lear, T. B., Tuncer, F., Kennerdell, J. R., Camarco, D. P., ... & Chen, B. B. (2020). A small molecule NRF2 activator BC-1901S ameliorates inflammation through DCAF1/NRF2 axis. Redox biology, 32, 101485.

Schabla, N. M., Mondal, K., & Swanson, P. C. (2019). DCAF1 (VprBP): emerging physiological roles for a unique dual-service E3 ubiquitin ligase substrate receptor. Journal of molecular cell biology, 11(9), 725-735.

Yan, Y., Li, C., Sun, B., & Yang, R. (2018). DCAF1 is involved in HCV replication through regulation of miR-122. Archives of virology, 163(4), 977-985.

Wang, X., Arceci, A., Bird, K., Mills, C. A., Choudhury, R., Kernan, J. L., ... & Emanuele, M. J. (2017). VprBP/DCAF1 regulates the degradation and nonproteolytic activation of the cell cycle transcription factor FoxM1. Molecular and cellular biology, 37(13), e00609-16.

Zhou, X., DeLucia, M., Hao, C., Hrecka, K., Monnie, C., Skowronski, J., & Ahn, J. (2017). HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase. Journal of Biological Chemistry, 292(51), 21117-21127.

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For research use only. Not intended for any clinical use.

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