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SUMO2/3 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 1 - SUMO2/3 Antibody (C-term) AP1224a
    All lanes : Anti-SUMO2/3 Antibody (C-term) at 1:2000 dilution Lane 1: SH-SY5Y whole cell lysate Lane 2: Hela whole cell lysate Lane 3: Jurkat whole cell lysate Lane 4: HL-60 whole cell lysate Lane 5: Mouse cerebellum tissue lysate Lane 6: Mouse liver tissue lysate Lane 7: Rat liver tissue lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 12 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 3 - SUMO2/3 Antibody (C-term) AP1224a
    Fluorescent image of SH-SY5Y cells stained with SUMO2/3 Antibody (C-term) (Cat#AP1224a). AP1224a was diluted at 1:100 dilution. An Alexa Fluor 488-conjugated goat anti-rabbit lgG at 1:400 dilution was used as the secondary antibody (green). Cytoplasmic actin was counterstained with Alexa Fluor® 555 conjugated with Phalloidin (red).
  • 3 - SUMO2/3 Antibody (C-term) AP1224a
    Fluorescent image of Hela cells stained with SUMO2/3 Antibody (C-term) (Cat#AP1224a). AP1224a was diluted at 1:100 dilution. An Alexa Fluor 488-conjugated goat anti-rabbit lgG at 1:400 dilution was used as the secondary antibody (green). Cytoplasmic actin was counterstained with Alexa Fluor® 555 conjugated with Phalloidin (red).
  • 1 - SUMO2/3 Antibody (C-term) AP1224a
    SUMO2/3 Antibody (C-term) (Cat. #AP1224a) western blot analysis in Hela cell line and mouse liver tissue lysates (35ug/lane).This demonstrates the SUMO2/3 antibody detected the SUMO2/3 protein (arrow).
  • 14 - SUMO2/3 Antibody (C-term) AP1224a
    Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.
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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
IHC-P, WB, IF, E
Primary Accession P55854
Other Accession Q7SZ22, Q5XIF4, Q9Z172, Q6DI05, Q17QV3, P61959, P61958, P61957, Q2PFW2, P61956, Q6DHL4, Q6LDZ8, Q5ZJM9, P61955, Q6NV25, Q6GPW2, Q7ZTK7
Reactivity Human, Mouse, Rat
Predicted Xenopus, Zebrafish, Bovine, Chicken, Hamster, Monkey, Pig, Rat
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 11637 Da
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 SUMO2/3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 49-81 amino acids from the C-terminal region of human SUMO2/3.
Dilution WB~~1:1000
IF~~1:100
IHC-P~~1:50~100
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.
PrecautionsSUMO2/3 Antibody (C-term) 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
Adenovirus E4-ORF3 Targets PIAS3 and Together with E1B-55K Remodels SUMO Interactions in the Nucleus and at Virus Genome Replication Domains.
Author : Higginbotham JM1, O\'Shea CC2.
J Virol. 2015 Oct 15;89(20):10260-72. doi: 10.1128/JVI.01091-15. Epub 2015 Jul 29.
26223632
Signaling via the IL-20 receptor inhibits cutaneous production of IL-1β and IL-17A to promote infection with methicillin-resistant Staphylococcus aureus.
Author : Myles IA1,Fontecilla NM,Valdez PA,Vithayathil PJ,Naik S,Belkaid Y,Ouyang W,Datta SK.
Nat Immunol. 2013 Aug;14(8):804-11. doi: 10.1038/ni.2637. Epub 2013 Jun 23.
23793061
PKCζ mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation.
Author : Heo KS, Lee H, Nigro P, Thomas T, Le NT, Chang E, McClain C, Reinhart-King CA, King MR, Berk BC, Fujiwara K, Woo CH, Abe J.
J Cell Biol. 2011 May 30;193(5):867-84. doi: 10.1083/jcb.201010051.
21624955
Lysine deacetylation in ischaemic preconditioning: the role of SIRT1.
Author : Nadtochiy SM, Redman E, Rahman I, Brookes PS.
Cardiovasc Res. 2011 Feb 15;89(3):643-9. doi: 10.1093/cvr/cvq287. Epub 2010 Sep 7.
20823277
Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation.
Author : Snider NT1, Weerasinghe SV, Iñiguez-Lluhí JA, Herrmann H, Omary MB.
J Biol Chem. 2011 Jan 21;286(3):2273-84. doi: 10.1074/jbc.M110.171314. Epub 2010 Nov 9.
21062750
Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress.
Author : Cho KI, Yi H, Tserentsoodol N, Searle K, Ferreira PA.
Dis Model Mech. 2010 Sep-Oct;3(9-10):595-604. doi: 10.1242/dmm.004648. Epub 2010 Aug 3.
20682751
Spatial interplay between PIASy and FIP200 in the regulation of signal transduction and transcriptional activity.
Author : Martin N1, Schwamborn K, Urlaub H, Gan B, Guan JL, Dejean A.
Mol Cell Biol. 2008 Apr;28(8):2771-81. doi: 10.1128/MCB.01210-07. Epub 2008 Feb 19.
18285457
SUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activity.
Author : Degerny C, Monte D, Beaudoin C, Jaffray E, Portois L, Hay RT, de Launoit Y, Baert JL.
J Biol Chem. 2005 Jul 1;280(26):24330-8. Epub 2005 Apr 27.
15857832

BACKGROUND

SUMO2 and SUMO3 are members of the SUMO (small ubiquitin-like modifier) protein family. This protein family functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. In vertebrates, three members of the SUMO family have been described, SUMO 1 and the functionally distinct homologues SUMO 2 and SUMO 3. SUMO modification sites present in the N terminal regions of SUMO 2 and SUMO 3 are utilized by SAE1/SAE2 (SUMO E1) and Ubc9 (SUMO E2) to form polymeric chains of SUMO 2 and SUMO 3 on protein substrates, a property not shared by SUMO 1.

REFERENCES

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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