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SUMO-1 Antibody

Rabbit Monoclonal Antibody

  • WB - SUMO-1 Antibody AJ1746a
    A. Western blot analysis of Anti-SUMO-1 RabMAb (Cat. #AJ1746a), dilution 1:1,000. A-Hela B-NIH 3T3
  • IHC - SUMO-1 Antibody AJ1746a
    B. Immunohistochemical analysis of paraffin-embedded human lung carcinoma using anti-SUMO-1 RabMAb (Cat. #AJ1746a).
  • IF - SUMO-1 Antibody AJ1746a
    C. Immunofluorescent staining of HeLa cells using anti-SUMO-1 RabMAb (Cat. #AJ1746a).
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession P63165
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Monoclonal
Clone Names Y299
Calculated MW 11557 Da
Gene ID 7341
Other Names Small ubiquitin-related modifier 1, SUMO-1, GAP-modifying protein 1, GMP1, SMT3 homolog 3, Sentrin, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein SMT3C, Smt3C, Ubiquitin-like protein UBL1, SUMO1, SMT3C, SMT3H3, UBL1
Target/Specificity A synthetic peptide corresponding to residues near the C-term of human SUMO-1 was used as immunogen.
Dilution WB~~1:1000~10000
Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsSUMO-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name SUMO1
Synonyms SMT3C, SMT3H3, UBL1
Function Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376).
Cellular Location Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body. Cell membrane. Nucleus. Note=Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body. {ECO:0000250|UniProtKB:P63166, ECO:0000269|PubMed:24651376}
Research Areas
Citations ( 0 )


Small ubiquitin-related modifier-1 (SUMO-1), also known as SMT3, Sentrin, GMP1 UBL1 and PIC1, is a member of the ubiquitin like family (1-2). Structurally similar to ubuquitin, SUMO-1 does not mark protein for degradation (SUMOlation) but instead seems to be involved in the modulation of protein-protein interaction. It also participates in a number of cellular processes such as nuclear transport, transcriptional regulation, apoptosis and protein stability. Like ubiquitin, SUMO-1 is covalently bound to a variety of proteins (p53, Jun, p73 alpha) via a three step enzymatic pathway (3-4), as well as requiring specific proteases to activate the protein. SUMO-1 is also known to form a complex with RanGAP1 (5).


1. Wen-Ming Yang , Ya-Li Yao , Jian-Min Sun, James R. Davie and Edward Seto. Volume 272, Number 44, Issue of October 31, 1997 pp. 28001-28007
2. Li, J., Wang, J., Nawaz, Z., Liu, J.M., Qin, J. and Wong, J., 2000. EMBO J. 19, pp. 4342
3. Desterro, J. M., Rodriguez, M. S., Kemp, G. D., and Hay, R. T. (1999) J. Biol. Chem. 274,
4. Kim, K. I., Baek, S. H., and Chung, C. H. (2002) J. Cell. Physiol. 191, 257-268
5. Saitoh, H. Hinchey, J.( 2000) J.Biol. Chemistry. 275, March3: 6252-6258,

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Cat# AJ1746a
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