Antibody detailed product information

Code No. M114-3 プリントPrint out
Anti-SUMO-2/3 mAb
This antibody reacts with SUMO-2/3 (15 kDa) but not react with SUMO-1 (15~17 kDa) on Western blotting.
Price ¥48,000
Size 100 µg/100 µL
Availability (in Japan) 10 or more
(In Japan at 00:05, Oct 14, 2019 in JST)
Clonality Monoclonal
Clone 1E7
(Immunized Animal)
Mouse IgG2b
Applications WB 2 µg/mL  
IC 5 µg/mL  
ChIP* reported.  (PMID: 26259101)
Other(PLA) reported.  (PMID: 28600321)
Recombinant Human full-length SUMO-3
Reactivity [Gene ID]

Human[6613/6612], Mouse[170930/20610], Rat[690244/499417]

Storage buffer 1 mg/mL in PBS/50% glycerol, pH 7.2
Storage temp. -20°C
Conjugate Unlabeled
Manufacturer MBL
Alternative names SUMO2, SUMO3, HSMT3, SMT3A, SMT3B, Smt3A, Smt3B, SMT3H1, SMT3H2
Background Sumoylation, the covalent attachment of a small ubiquitin-like modifier (SUMO) peptide to lysine residues of targeted substrate, has recently emerged as an important mechanism in transcriptional control. In humans and mice, the SUMO family consists of three members, SUMO-1, -2, and -3. SUMO-2 (SMT3A, Sentrin-3) and SUMO-3 (SMT3B, Sentrin-2) are similar (~95% identical), but less closely related to SUMO-1 (~50% identical). Whereas many proteins modified by SUMO-1 were identified, many as yet unidentified proteins are modified by SUMO-2/3 after exposure of cells to various stress stimuli.
Related products M113-3 Anti-SUMO-1 mAb
D058-3 Anti-Multi Ubiquitin mAb
MK-12-3 Anti-Ubiquitin mAb
Product category Research area:Ubiquitin proteasome


Western Blotting

  1. Klein UR et al. RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. Mol. Biol. Cell 20, 410-8 (2009)(PMID:18946085)
  2. Du JX et al. A small ubiquitin-related modifier-interacting motif functions as the transcriptional activation domain of Krüppel-like factor 4. J biol. Chem. 285, 28298-308 (2010)(PMID:20584900)
  3. Fernández-Miranda G et al. SUMOylation modulates the function of Aurora-B kinase. J Cell Sci. 123, 2823-33 (2010)(PMID:20663916)
  4. Finkbeiner E et al. The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex. EMBO J. 30, 1067-78 (2011)(PMID:21326211)
  5. Fanis P et al. Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation. Mol Cell Proteomics 11, 1263-73 (2012)(PMID:23122649)
  6. Psakhye I, Jentsch S. Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell 151, 807-20 (2012)(PMID:23122649)
  7. Guo C et al. SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia. EMBO J. 32, 1514-28 (2013)(PMID:23524851)
  8. Berndt A et al. In vivo characterization of the properties of SUMO1-specific monobodies. Biochem J. 456, 385-95 (2013)(PMID:24040933)
  9. Paakinaho V et al. Electrophilic lipid mediator 15-deoxy-Δ12,14-prostaglandin j2 modifies glucocorticoid signaling via receptor SUMOylation. Mol Cell Biol. 34, 202-13 (2014)(PMID:24980431)
  10. Sutinen P et al. Nuclear mobility and activity of FOXA1 with androgen receptor are regulated by SUMOylation. Mol Endocrinol. 28, 1719-28 (2014)(PMID:25127374)
  11. Niskanen EA et al. Global SUMOylation on active chromatin is an acute heat stress response restricting transcription. Genome Biol. 16, 153 (2015)(PMID:26259101)
  12. Yan Y et al. SUMOylation of AMPKα1 by PIAS4 specifically regulates mTORC1 signalling. Nat Commun. 6, 8979 (2015)(PMID:26616021)
  13. Lecona E et al. USP7 is a SUMO deubiquitinase essential for DNA replication. Nat Struct Mol Biol. 23, 270-7 (2016)(PMID:26950370)
  14. Du L et al. Role of SUMO activating enzyme in cancer stem cell maintenance and self-renewal. Nat Commun. 7, 12326 (2016)(PMID:27465491)
  15. Ambaye N et al. Streptonigrin Inhibits SENP1 and Reduces the Protein Level of Hypoxia-Inducible Factor 1α (HIF1α) in Cells. Biochemistry 57, 1807-1813 (2018)(PMID:29481054)
  16. Eifler K et al. SUMO targets the APC/C to regulate transition from metaphase to anaphase. Nat Commun. 9, 1119 (2018)(PMID:29549242)
  17. Li YJ et al. Regulation of miR-34b/c-targeted gene expression program by SUMOylation. Nucleic Acids Res. 46, 7108-7123 (2018)(PMID:29893976)
  18. Zhang FP et al. Lack of androgen receptor SUMOylation results in male infertility due to epididymal dysfunction. Nat Commun. 10, 777 (2019) (PMID:30770815)


  1. Niskanen EA et al. Global SUMOylation on active chromatin is an acute heat stress response restricting transcription. Genome Biol. 16, 153 (2015)(PMID:26259101)


  1. Lecona E et al. USP7 is a SUMO deubiquitinase essential for DNA replication. Nat Struct Mol Biol. 23, 270-7 (2016)(PMID:26950370)


  1. Gilistro E et al. Importin-β and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function. J Cell Sci. 130, 2564-2578 (2017)(PMID:28600321)
  • The availability is based on the information in Japan at 00:05, Oct 14, 2019 in JST.
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  • Abbreviations for applications:
    WB: Western Blotting, IH: Immunohistochemistry, IC: Immunocytochemistry, IP: Immunoprecipitation
    FCM: Flow Cytometry, NT: Neutralization, IF: Immunofluorescence, RIP: RNP Immunoprecipitation
    ChIP: Chromatin Immunoprecipitation, CoIP: Co-Immunoprecipitation
    DB: Dot Blotting, NB: Northern Blotting, RNA FISH: RNA Fluorescence in situ hybridization
  • For applications and reactivity:
    *: The use is reported in a research article (Not tested by MBL). Please check the data sheet for detailed information.
    **: The use is reported from the licenser (Under evaluation or not tested by MBL).
  • For storage temparature: RT: room temparature
  • Please note that products in this website might be changed or discontinued without notification in advance for quality improvement.
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