Human SUMO Polyclonal Ab
Human SUMO Polyclonal Ab Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
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Background: SUMO
Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation (1-3). There are four known SUMOs (SUMO1-4). All SUMO proteins share a conserved Ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following cleavage of a C-terminal prosegment, the C-terminal glycine residue of SUMO is enzymatically attached to a lysine residue on a target protein. In humans, SUMO is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme (4-5). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (6). SUMOylation can occur without the requirement of a specific SUMO ligase (E3), where SUMO is transferred directly from UBE2I/Ubc9 to specific substrates. Unlike SUMO1, which is usually conjugated to proteins as a monomer, SUMO2 and SUMO3 are known to form high molecular weight polymers on proteins. SUMO precursor processing and deconjugation are catalyzed by a family of cysteine proteases known as SUMO-specific proteases (SENPs) and DeSUMOylating Isopeptidase 1 (7).
The ubiquitin-like SUMO proteins are conjugated to a variety of proteins in the presence of UbcH9 and the Aos1/Uba2 (yeast) or SAE1/SAE2 (human) activating enzyme. SUMOlyation can occur without the requirement of a specific E3 ligase activity, where SUMO is transferred directly from UbcH9 to specific substrates. SUMOlyated substrates are primarily localized to the nucleus (RanGAP-1, RANBP2, PML, p53, Sp100, HIPK2) but there are also cytosolic substrates (I kappa B alpha, GLUT1, GLUT4). SUMO modification has been implicated in functions such as nuclear transport, chromosome segregation, and transcriptional regulation.
- Desterro, J.M. et al. (1997) FEBS. Lett. 417:297.
- Bettermann, K. et al. (2012) Cancer Lett. 316:113.
- Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
- Okuma, T. et al. (1999) Biochem. Biophys. Res. Commun. 254:693.
- Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
- Johnson, E.S. et al. (1997) EMBO J. 16:5509.
- Shin, E.J. et al. (2012) EMBO Rep. 13:339.
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Citations for Human SUMO Polyclonal Ab
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Satellite cell senescence underlies myopathy in a mouse model of limb-girdle muscular dystrophy 2H.
Authors: Kudryashova E, Kramerova I, Spencer MJ
J. Clin. Invest., 2012-04-16;122(5):1764-76.
Species: Mouse
Sample Types: Cell Lysates
Applications: Western Blot -
Axin1 prevents Salmonella invasiveness and inflammatory response in intestinal epithelial cells.
Authors: Zhang YG, Wu S, Xia Y
PLoS ONE, 2012-04-11;7(4):e34942.
Species: Mouse
Sample Types: Cell Lysates
Applications: Western Blot
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