Ubiquitin Antibody Mouse Monoclonal

Ubiquitin Mouse Monoclonal Antibody
$0.00
SKU
Cat. # AUB01

Anti-ubiquitin antibody is a pan-ubiquitin, mouse monoclonal antibody that is part of the Signal-Seeker™ product line. The antibody was raised against full length bovine ubiquitin. The antibody has been shown to recognize poly-ubiquitin, mono-ubiquitin, and free ubiquitin (Fig 1). Ubiquitin is a highly conserved protein and AUB01 is predicted to recognize ubiquitin from a wide range of species (5). AUB01 is purified by Protein G affinity chromatography and is supplied as a lyophilized white powder.

Host/Isotype
Mouse / IgG1

Clone
P4D1

Species Reactivity
Wide range of species

RRID

AB_2884970



Validated Applications

Western Blot using Ubiquitin Antibody

Anti-Ubiquitin Antibody (Cat. # AUB01) was used at a 1:500 dilution. Bovine thymus ubiquitin was run as follows; Lane 1-50 ng, Lane 2-25 ng. Lane 3– 12.5 ng, Lane 4-6.25 ng, Lane 5-3.12 ng. Lanes 6 & 7 represent 20 µg of Swiss 3T3 cell lysate from cells treated for 5h with 10 µM MG132 (Lane 6) or untreated cells (Lane 7). Arrow indicates free ubiquitin band (8 kD), higher molecular weight bands are ubiquitinated proteins. To see the full Western blot protocol, see the product datasheet.

AUB01-WB_1
Immunofluorescence Ubiquitin Antibody

HeLa cells were stained and visualized by fluorescence microscopy as described in the IF method below. Ubiquitin targeted cytoplasmic and nuclear proteins and free ubiquitin were stained using AUB01 at 1:500 dilution. To see the full Immunofluorescence protocol, see the product datasheet.
AUB01_IF_Image



Ubiquitin Background

Ubiquitin (Ub) and ubiquitin-like proteins (Ubls, e.g. SUMO, Nedd) are a group of approximately 15 proteins that have a molecular weight of around 8 kD. During the ubiquitination process, these are conjugated via activating (E1), conjugating (E2) and ligating (E3) enzymes to lysines of a target protein (1). Mammalian cells express over 600 potential ubiquitin ligases which exceeds that of the kinase superfamily of PTM proteins (2).

One function of ubiquitination is to target proteins for proteosomal degradation. This role can range from a general housekeeping function that clears miss folded proteins from a cell to involvement in tightly regulated spatio-temporal cell signaling events (1). An emerging function of ubiquitination is its ability to activate proteins via the creation of unique protein:protein interactions (3). In common with many other PTMs, ubiquitination is reversible. Ubiquitin-specific proteases (USPs or DUBs) remove ubiquitins from target proteins (4). The reversible nature of ubiquitination further enhances the potential of this PTM to dynamically regulate protein function.


References

1) Grabbe, C. et al. 2011. The spatial and temporal organization of ubiquitin networks. Nat. Rev. Mol. Cell. Biol. 12:295-307.

2) Deshaies R.J. & Joazeiro, C.A. 2009. RING domain E3 ligases. Ann. Rev. Biochem. 78: 399-434.

3) Lomeli, H. & Vazquez. 2011. Emerging roles of the SUMO pathway. Cell Mol. Life Sci. 68:4045-4064.

4) Faesen, A.C. et al. 2012. The role of UBL domains in ubiquitin specific proteases. Biochem. Soc. Trans. 40:539-545.

5) Zuin, A. et al. 2014. Ubiquitin signaling: Extreme conservation as a source of diversity. Cells 3:690-701.


For more information contact: signalseeker@cytoskeleton.com

Associated Products:

Signal-Seeker™ Ubiquitination Detection Kit (Cat. # BK161)

Signal-Seeker™ Ubiquitin Affinity Beads (Cat.# UBA01B-beads)

Signal-Seeker™: BlastR™ Rapid Lysate Prep Kit (Cat. # BLR01)

For product Datasheets and MSDSs please click on the PDF links below.

Sample Size Datasheet (Cat. AUB01-S):  

Bulk Size Datasheet (Cat. AUB01-XL):  

Certificate of Analysis:  Lot 001

For the most recent publications citing this and other Signal-Seeker™ products, see our Signal-Seeker™ Validation Data Page click here

AuthorTitleJournalYearArticle Link
Takeda, Kenji et al.A Novel Approach: Investigating the Intracellular Clearance Mechanism of Glyceraldehyde-Derived Advanced Glycation End-Products Using the Artificial Checkpoint Kinase 1 d270KD Mutant as a Substrate ModelCells2023ISSN 2073-4409
Martin, Thomas G. et al.Dysregulated Autophagy and Sarcomere Dysfunction in Patients With Heart Failure With Co-Occurrence of P63A and P380S BAG3 VariantsJournal of the American Heart Association2023ISSN 2047-9980
Wang, Longlong et al.Disrupting the HDAC6-ubiquitin interaction impairs infection by influenza and Zika virus and cellular stress pathwaysCell Reports2022
Martin, Thomas G. et al.Cardiomyocyte contractile impairment in heart failure results from reduced BAG3-mediated sarcomeric protein turnoverNature Communications2021ISSN 2041-1723
Manzione, Maria Giulia et al.Co-regulation of the antagonistic RepoMan:Aurora-B pair in proliferating cellsMolecular Biology of the Cell2020ISSN 1939-4586
Rivas, José et al.KCTD5, a novel TRPM4-regulatory protein required for cell migration as a new predictor for breast cancer prognosisFASEB Journal2020ISSN 1530-6860
Wenzel, H. Jürgen et al.Astroglial-targeted expression of the fragile X CGG repeat premutation in mice yields RAN translation, motor deficits and possible evidence for cell-to-cell propagation of FXTAS pathologyActa neuropathologica communications2019ISSN 2051-5960
Álvarez, Alhejandra et al.KCTD5 and ubiquitin proteasome signaling are required for Helicobacter pylori adherenceFrontiers in Cellular and Infection Microbiology2017ISSN 2235-2988
Braganza, Andrea et al.UBE3B is a calmodulin-regulated, mitochondrion-associated E3 ubiquitin ligaseJournal of Biological Chemistry2017ISSN 1083-351X
Horita, Henrick et al.Identifying Regulatory Posttranslational Modifications of PD-L1: A Focus on MonoubiquitinatonNeoplasia (United States)2017ISSN 1476-5586
Hukema, Renate K. et al.Reversibility of neuropathology and motor deficits in an inducible mouse model for FXTASHuman Molecular Genetics2015ISSN 1460-2083

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