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Pan SUMO Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 14 - Pan SUMO Antibody AP1290a
    Immunohistochemical analysis of paraffin-embedded H.bladder section using Pan SUMO Antibody(Cat#AP1290a). AP1290a was diluted at 1:100 dilution. A peroxidase-conjugated goat anti-rabbit IgG at 1:400 dilution was used as the secondary antibody, followed by DAB staining.
  • 3 - Pan SUMO Antibody AP1290a
    Fluorescent confocal image of Hela cell stained with Pan SUMO Antibody(Cat#AP1290a).Hela cells were fixed with 4% PFA (20 min), permeabilized with Triton X-100 (0.1%, 10 min), then incubated with Pan SUMO primary antibody (1:25, 1 h at 37℃). For secondary antibody, Alexa Fluor® 488 conjugated donkey anti-rabbit antibody (green) was used (1:400, 50 min at 37℃).Cytoplasmic actin was counterstained with Alexa Fluor® 555 (red) conjugated Phalloidin (7units/ml, 1 h at 37℃). Nuclei were counterstained with DAPI (blue) (10 µg/ml, 10 min).Pan SUMO immunoreactivity is localized to Nucleus significantly.
  • 14 - Pan SUMO Antibody AP1290a
    Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by AEC staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.
  • 1 - Pan SUMO Antibody AP1290a
    SUMO3 Antibody (Cat. #AP1290a) western blot analysis in 293 cell line and rat liver tissue lysates (35ug/lane).This demonstrates the SUMO3 antibody detected the SUMO3 protein (arrow).
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
IF, IHC-P, WB, E
Primary Accession P55854
Reactivity Human, Rat
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Additional info
Gene ID 6612
Other Names Small ubiquitin-related modifier 3, SUMO-3, SMT3 homolog 1 {ECO:0000312|HGNC:HGNC:11124}, SUMO-2, Ubiquitin-like protein SMT3A, Smt3A, SUMO3 (HGNC:11124)
Target/Specificity "This Pan SUMO antibody recognizes SUMO2 and SUMO3. This antibody is generated from rabbits immunized with a recombinant protein encoding full length human SUMO3."
Dilution IHC-P~~1:50~100
IF~~1:10~50
WB~~1:1000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPan SUMO Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name SUMO3 (HGNC:11124)
Function Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 (PubMed:11451954, PubMed:18538659, PubMed:21965678). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).
Cellular Location Cytoplasm. Nucleus. Nucleus, PML body
Tissue Location Expressed predominantly in liver.
Research Areas
SUMO2/3 modification of activating transcription factor 5 (ATF5) controls its dynamic translocation at the centrosome.
Author : Yuan Y1,Gaither K2,Kim E3,Liu E4,Hu M5,Lengel K6,Qian D5,Xu Y3,Wang B5,Knipprath H7,Liu D2.
J Biol Chem. 2018 Jan 11. pii: jbc.RA117.001151. doi: 10.1074/jbc.RA117.001151. [Epub ahead of print]
29326161
Ehrlichia chaffeensis Exploits Host SUMOylation Pathways To Mediate Effector-Host Interactions and Promote Intracellular Survival.
Author : Dunphy PS1, Luo T1, McBride JW2.
Infect Immun. 2014 Oct;82(10):4154-68. doi: 10.1128/IAI.01984-14. Epub 2014 Jul 21.
25047847
Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search.
Author : Sun H1, Hunter T.
J Biol Chem. 2012 Dec 7;287(50):42071-83. doi: 10.1074/jbc.M112.410985. Epub 2012 Oct 18.
23086935
Generation and nuclear translocation of sumoylated transmembrane fragment of cell adhesion molecule L1.
Author : Lutz D1, Wolters-Eisfeld G, Joshi G, Djogo N, Jakovcevski I, Schachner M, Kleene R.
J Biol Chem. 2012 May 18;287(21):17161-75. doi: 10.1074/jbc.M112.346759. Epub 2012 Mar 19.
22431726

BACKGROUND

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.

REFERENCES

Yang, S.H., et al., Mol. Cell 13(4):611-617 (2004).
Bailey, D., et al., J. Biol. Chem. 279(1):692-703 (2004).
Ling, Y., et al., Nucleic Acids Res. 32(2):598-610 (2004).
Pountney, D.L., et al., Exp. Neurol. 184(1):436-446 (2003).
Ohshima, T., et al., J. Biol. Chem. 278(51):50833-50842 (2003).
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).
Lapenta, V., et al., Genomics 40(2):362-366 (1997).

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