HPA021046
Anti-UBR4 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-600 kDa retinoblastoma protein-associated factor, Anti-E3 ubiquitin-protein ligase UBR4, Anti-N-recognin-4, Anti-RBAF600, Anti-Retinoblastoma-associated factor of 600 kDa, Anti-Zinc finger UBR1-type protein 1, Anti-p600
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About This Item
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
human
technique(s)
immunohistochemistry: 1:50- 1:200
immunogen sequence
VEFGGNDLLQVYNAQQIKHRLNSTGMYVANTKPGGFTIEISNNNSTMVMTGMRIQIGTQAIERAPSYIEIFGRTMQLNLSRSRWFDFPFTREEALQADKKLNLFIGASVDPAGVTMIDAVKIYGKTKEQF
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... UBR4(23352)
General description
The gene UBR4 (ubiquitin protein ligase E3 component n-recognin 4) is mapped to human chromosome 1p36.13. The protein localizes in the cytoplasm and the nucleus. UBR4 is also referred to as p600.
Immunogen
E3 ubiquitin-protein ligase UBR4 recombinant protein epitope signature tag (PrEST)
Application
Anti-UBR4 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Biochem/physiol Actions
UBR4 (ubiquitin protein ligase E3 component n-recognin 4) interacts with retinoblastoma protein in the nucleus and functions as a chromatin scaffold. In the cytoplasm, UBR4 regulates cytoskeletal dynamics and membrane morphogenesis. It is important for formation of integrin-mediated ruffled membrane and cell survival. UBR4 forms an E2-E3 complex with RAD6 (ubiquitin-conjugating enzyme E2) and KCMF1 (potassium channel modulatory factor 1). The complex regulates lysosome-mediated degradation of N-end rule substrates. UBR4 associates with human papillomavirus type 16 (HPV-16) E7 oncoprotein and participates in anchorage-independent growth in cancer cells.
Features and Benefits
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Linkage
Corresponding Antigen APREST72607
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
Correction: Novel Genetic Locus Implicated for HIV-1 Acquisition with Putative Regulatory Links to HIV Replication and Infectivity: A Genome-Wide Association Study.
Eric O Johnson et al.
PloS one, 10(5), e0129671-e0129671 (2015-05-30)
Kari Parsons et al.
Cellular and molecular life sciences : CMLS, 72(6), 1149-1160 (2014-11-27)
A decade ago, the large 600 kDa mammalian protein p600 (also known as UBR4) was discovered as a multifunctional protein with roles in anoikis, viral transformation and protein degradation. Recently, p600 has emerged as a critical protein in the mammalian brain
Jenny H Hong et al.
Molecular & cellular proteomics : MCP, 14(3), 674-685 (2015-01-15)
RAD6 is a ubiquitin E2 protein with roles in a number of different biological processes. Here, using affinity purification coupled with mass spectrometry, we identify a number of new RAD6 binding partners, including the poorly characterized ubiquitin E3 ligases KCMF1
Yoshihiro Nakatani et al.
Proceedings of the National Academy of Sciences of the United States of America, 102(42), 15093-15098 (2005-10-11)
In this article, we identify and characterize p600, a unique 600-kDa retinoblastoma protein- and calmodulin-binding protein. In the nucleus, p600 and retinoblastoma protein seem to act as a chromatin scaffold. In the cytoplasm, p600 and clathrin form a meshwork structure
Richard T Timms et al.
Science (New York, N.Y.), 365(6448) (2019-07-06)
The N-terminal residue influences protein stability through N-degron pathways. We used stability profiling of the human N-terminome to uncover multiple additional features of N-degron pathways. In addition to uncovering extended specificities of UBR E3 ligases, we characterized two related Cullin-RING
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