This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogen
This SUMO1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human SUMO1.
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Expiry Date
6 months
Saito, Souza, Costa, Meirelles, Gonçalves, Santos, Bressan, McComb, Costello, Whelan, Kobarg: "Human Regulatory Protein Ki-1/57 Is a Target of SUMOylation and Affects PML Nuclear Body Formation." in: Journal of proteome research, Vol. 16, Issue 9, pp. 3147-3157, (2018) (PubMed).
Janer, Werner, Takahashi-Fujigasaki, Daret, Fujigasaki, Takada, Duyckaerts, Brice, Dejean, Sittler: "SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7." in: Human molecular genetics, Vol. 19, Issue 1, pp. 181-95, (2009) (PubMed).
Ji, Degerny, Vintonenko, Deheuninck, Foveau, Leroy, Coll, Tulasne, Baert, Fafeur: "Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation." in: Oncogene, Vol. 26, Issue 3, pp. 395-406, (2007) (PubMed).
Bradley, van der Meer, Roodi, Yan, Chandrasekharan, Sun, Mernaugh, Parl: "Carcinogen-induced histone alteration in normal human mammary epithelial cells." in: Carcinogenesis, Vol. 28, Issue 10, pp. 2184-92, (2007) (PubMed).
Degerny, Monte, Beaudoin, Jaffray, Portois, Hay, de Launoit, Baert: "SUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activity." in: The Journal of biological chemistry, Vol. 280, Issue 26, pp. 24330-8, (2005) (PubMed).
Ling, Sankpal, Robertson, McNally, Karpova, Robertson: "Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription." in: Nucleic acids research, Vol. 32, Issue 2, pp. 598-610, (2004) (PubMed).
Bailey, OHare: "Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1." in: The Journal of biological chemistry, Vol. 279, Issue 1, pp. 692-703, (2003) (PubMed).
Pountney, Huang, Burns, Haan, Thompson, Blumbergs, Gai: "SUMO-1 marks the nuclear inclusions in familial neuronal intranuclear inclusion disease." in: Experimental neurology, Vol. 184, Issue 1, pp. 436-46, (2003) (PubMed).
Ohshima, Shimotohno: "Transforming growth factor-beta-mediated signaling via the p38 MAP kinase pathway activates Smad-dependent transcription through SUMO-1 modification of Smad4." in: The Journal of biological chemistry, Vol. 278, Issue 51, pp. 50833-42, (2003) (PubMed).
Target
SUMO1
(Small Ubiquitin Related Modifier Protein 1 (SUMO1))
Covalent modification of target lysines by SUMO (small ubiquitin-like modifier) modulates processes such as protein localization, transcription, nuclear transport, mitosis, DNA replication and repair, signal transduction, and viral reproduction. SUMO does not seem to be involved in protein degradation and may in fact function as an antagonist of ubiquitin in the degradation process. The SUMO family consists of SUMO1 and closely related homologs SUMO2, SUMO3, and SUMO4. Sumoylation has been shown to regulate a wide range of proteins, including MDM2, PIAS, PML, RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, Fas, Daxx, TNFRI, Topo-I, Topo-II, PARK2, WRN, Sp100, IkB-alpha, Androgen receptor (AR), GLUT1/4, CaMK, DNMT3B, TDG, HIF1A, CHD3, EXOSC9, RAD51, and viral targets such as CMV-IE1/2, EBV-BZLF1, and HPV/BPV-E1.